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Conserved domains on  [gi|238814398|ref|NP_001074668|]
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apical endosomal glycoprotein precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 660-817 5.33e-52

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 179.85  E-value: 5.33e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    660 DQELSCNFERDS-CSWHTGHLTDAHWHRIKSH----GSQLDHTTGQGFFMFLDpTDPPARGQGALLLTRPQVPVVPKECL 734
Cdd:smart00137    1 TSPGNCDFEEGStCGWHQDSNDDGHWERVSSAtgipGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    735 SFWYRLYGPQIGTLCLAMR-REREEDILLWSRSGTHGNRWHQAWVTLHHQPEastKYQLLFEGLRN-GYHGTMALDDIAV 812
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVReNNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRGkGHSGYIALDDILL 156


                    ....*
gi 238814398    813 RPGPC 817
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 823-978 7.15e-40

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


:

Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 145.20  E-value: 7.15e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   823 CSFEDSD-CGFS--PGGWGLWTHQSnaSGLASWGPWIDHTTGTAQGHYMVVDTSpnVLPKGHVAALTSEEHQPLSQPACL 899
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVS--GPSVKTGPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   900 TFWYHMSVPNPGTLRVHVEESTRRQE---LSISAHGRSAWRLGSVNVQA-EQAWKVVFEAVAAGVEYSYMALDDISLQDG 975
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDtllWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 238814398   976 PCP 978
Cdd:pfam00629  157 PCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 978-1144 9.35e-40

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 144.79  E-value: 9.35e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    978 PQPGSCDFETG-LCGWSHLPWPslgGYSWDWSSGATPSRYPQpsVDHTLGTeaGHFAFFETSVLGPGgQAAWLRSEPLPA 1056
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSND---DGHWERVSSATGIPGPN--RDHTTGN--GHFMFFETSSGAEG-QTARLLSPPLYE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   1057 T-TVSCLRFWYYMGFPEHfykGELRVLLSSARGQLA--VWYQGGHLRDQWLQVQIELSNS-EEFQIVFEATLGGqPALGP 1132
Cdd:smart00137   73 NrSTHCLTFWYYMYGSGS---GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGK-GHSGY 148

                           170
                    ....*....|..
gi 238814398   1133 IAIDDVQYLAGQ 1144
Cdd:smart00137  149 IALDDILLSNGP 160
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 66-224 2.99e-38

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 140.56  E-value: 2.99e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398     66 STSFTCNFEQDS-CGWQDISTSGYRWLRDRAGAvlHGPGPHSDHTHGTdlGWYMAVGTHSGKEPSTATLRSPVMREAAPT 144
Cdd:smart00137    1 TSPGNCDFEEGStCGWHQDSNDDGHWERVSSAT--GIPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    145 CELRLWYHIASRDVAELRLDLT--HGVETLTLWQTSGPWGPGWQELAVNTGRIQGDFKVTFSATRNATHRGAVALDDVEF 222
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ..
gi 238814398    223 RD 224
Cdd:smart00137  157 SN 158
MAM super family cl42956
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 254-427 2.16e-34

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


The actual alignment was detected with superfamily member smart00137:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 129.39  E-value: 2.16e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    254 DGEDNCGDrsdEDPLICSHHMATDFEtglGPWNQLEGWTRNhsagsmvspAWPHRDHSRNS-AYGFFLISVAKPGTTAVL 332
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSATGI---------PGPNRDHTTGNgHFMFFETSSGAEGQTARL 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    333 YSPEFQGSVSNNCsFTFYYYLHGSEASHFQLFLqaQGLNTPQVPvLLRSRHGELGTAWVRDRVDIQS-AHPFRILLAGET 411
Cdd:smart00137   66 LSPPLYENRSTHC-LTFWYYMYGSGSGTLNVYV--RENNGSQDT-LLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTR 141

                           170
                    ....*....|....*...
gi 238814398    412 GPG--GVVGLDDLIMSSH 427
Cdd:smart00137  142 GKGhsGYIALDDILLSNG 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 498-652 7.15e-27

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


:

Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 107.83  E-value: 7.15e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   498 TDFESASAGGWEDISVGKLQWQWVEA-QEKSKPAGDANRDAP-GHFLSLQKAWGQLRSEARALTPALGPSG-PHCeLHMA 574
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSDHTQGTGsGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQC-LRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   575 YYFQSHPQGFLALVVVENGFR--ELLWQAPGGGSGSWTEEKIILGARRRPFQLEFVSLVdlDGPGQQGAGVDNVTL--RD 650
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGP 157


                   ..
gi 238814398   651 CN 652
Cdd:pfam00629  158 CP 159
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 234-266 7.43e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 52.21  E-value: 7.43e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 238814398  234 CPLGHHHCQNKACVEPHQLCDGEDNCGDRSDED 266
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 462-495 8.94e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 43.73  E-value: 8.94e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 238814398  462 CEPGHLSCGD-LCVPPEQLCDFQKHCAEGEDEHKC 495
Cdd:cd00112     1 CPPNEFRCANgRCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 660-817 5.33e-52

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 179.85  E-value: 5.33e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    660 DQELSCNFERDS-CSWHTGHLTDAHWHRIKSH----GSQLDHTTGQGFFMFLDpTDPPARGQGALLLTRPQVPVVPKECL 734
Cdd:smart00137    1 TSPGNCDFEEGStCGWHQDSNDDGHWERVSSAtgipGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    735 SFWYRLYGPQIGTLCLAMR-REREEDILLWSRSGTHGNRWHQAWVTLHHQPEastKYQLLFEGLRN-GYHGTMALDDIAV 812
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVReNNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRGkGHSGYIALDDILL 156


                    ....*
gi 238814398    813 RPGPC 817
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 665-818 1.63e-43

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 155.60  E-value: 1.63e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   665 CNFERDS-CSWHTGHLTDAHWHRIKSH----GSQLDHT--TGQGFFMFLDPTDPPArGQGALLLTRPQVPVVPKECLSFW 737
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPsvktGPSSDHTqgTGSGHFMYVDTSSGAP-GQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   738 YRLYGPQIGTLCLAMRREREE-DILLWSRSGTHGNRWHQAWVTLHHQPEastKYQLLFEGLR-NGYHGTMALDDIAVRPG 815
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTlDTLLWSISGDQGPSWKEARVTLSSSTQ---PFQVVFEGIRgGGSRGGIALDDISLSSG 156


                   ...
gi 238814398   816 PCW 818
Cdd:pfam00629  157 PCP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 823-978 7.15e-40

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 145.20  E-value: 7.15e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   823 CSFEDSD-CGFS--PGGWGLWTHQSnaSGLASWGPWIDHTTGTAQGHYMVVDTSpnVLPKGHVAALTSEEHQPLSQPACL 899
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVS--GPSVKTGPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   900 TFWYHMSVPNPGTLRVHVEESTRRQE---LSISAHGRSAWRLGSVNVQA-EQAWKVVFEAVAAGVEYSYMALDDISLQDG 975
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDtllWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 238814398   976 PCP 978
Cdd:pfam00629  157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 823-977 8.07e-40

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 144.83  E-value: 8.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  823 CSFEDSDCGFSPG--GWGLWTHQSNASGlaSWGPWIDHTTGTAQGHYMVVDTSPNvlPKGHVAALTSEEHQPLSQPACLT 900
Cdd:cd06263     1 CDFEDGLCGWTQDstDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSG--REGQKARLLSPLLPPPRSSHCLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  901 FWYHMSVPNPGTLRVHV-EESTRRQEL--SISAHGRSAWRLGSVNVQAEQA-WKVVFEAVAAGVEYSYMALDDISLQDGP 976
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVrEEGGGLGTLlwSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSPGP 156


                  .
gi 238814398  977 C 977
Cdd:cd06263   157 C 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 978-1144 9.35e-40

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 144.79  E-value: 9.35e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    978 PQPGSCDFETG-LCGWSHLPWPslgGYSWDWSSGATPSRYPQpsVDHTLGTeaGHFAFFETSVLGPGgQAAWLRSEPLPA 1056
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSND---DGHWERVSSATGIPGPN--RDHTTGN--GHFMFFETSSGAEG-QTARLLSPPLYE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   1057 T-TVSCLRFWYYMGFPEHfykGELRVLLSSARGQLA--VWYQGGHLRDQWLQVQIELSNS-EEFQIVFEATLGGqPALGP 1132
Cdd:smart00137   73 NrSTHCLTFWYYMYGSGS---GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGK-GHSGY 148

                           170
                    ....*....|..
gi 238814398   1133 IAIDDVQYLAGQ 1144
Cdd:smart00137  149 IALDDILLSNGP 160
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 665-817 2.32e-39

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 143.67  E-value: 2.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  665 CNFERDSCSWHTGHLTDAHWHRIKS------HGSQLDHTTGQGFFMFLDpTDPPARGQGALLLTRPQVPVVPKECLSFWY 738
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGstpspgTPPDHTHGTGSGHYLYVE-SSSGREGQKARLLSPLLPPPRSSHCLSFWY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  739 RLYGPQIGTLCLAMRREREE-DILLWSRSGTHGNRWHQAWVTLHHQPEastKYQLLFEGLR-NGYHGTMALDDIAVRPGP 816
Cdd:cd06263    80 HMYGSGVGTLNVYVREEGGGlGTLLWSASGGQGNQWQEAEVTLSASSK---PFQVVFEGVRgSGSRGDIALDDISLSPGP 156


                  .
gi 238814398  817 C 817
Cdd:cd06263   157 C 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 983-1146 2.16e-38

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 140.96  E-value: 2.16e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   983 CDFETG-LCGWSHlpwPSLGGYSWDWSSGatPSRYPQPSVDHTLGTEAGHFAFFETSvLGPGGQAAWLRSEPLPAT-TVS 1060
Cdd:pfam00629    1 CDFEDGnLCGWTQ---DSSDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDTS-SGAPGQTARLLSPLLPPSrSPQ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  1061 CLRFWYYMGFPehfYKGELRVLLSSARGQL--AVWYQGGHLRDQWLQVQIELS-NSEEFQIVFEATLGGqPALGPIAIDD 1137
Cdd:pfam00629   75 CLRFWYHMSGS---GVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSsSTQPFQVVFEGIRGG-GSRGGIALDD 150


                   ....*....
gi 238814398  1138 VQyLAGQQC 1146
Cdd:pfam00629  151 IS-LSSGPC 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 66-224 2.99e-38

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 140.56  E-value: 2.99e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398     66 STSFTCNFEQDS-CGWQDISTSGYRWLRDRAGAvlHGPGPHSDHTHGTdlGWYMAVGTHSGKEPSTATLRSPVMREAAPT 144
Cdd:smart00137    1 TSPGNCDFEEGStCGWHQDSNDDGHWERVSSAT--GIPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    145 CELRLWYHIASRDVAELRLDLT--HGVETLTLWQTSGPWGPGWQELAVNTGRIQGDFKVTFSATRNATHRGAVALDDVEF 222
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ..
gi 238814398    223 RD 224
Cdd:smart00137  157 SN 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 71-226 5.12e-37

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 136.72  E-value: 5.12e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    71 CNFEQDS-CGWQDISTSGYRWLRDRAGAVlhGPGPHSDHTHGTDLGWYMAVGTHSGKEPSTATLRSPVMREAAPTCELRL 149
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   150 WYHIASRDVAELRLDLTHGVETL--TLWQTSGPWGPGWQELAVNTGRIQGDFKVTFSATRNATHRGAVALDDVEF--RDC 225
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISLssGPC 158


                   .
gi 238814398   226 G 226
Cdd:pfam00629  159 P 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 71-224 5.10e-36

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 134.04  E-value: 5.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   71 CNFEQDSCGWQDISTSGYRWLRDRAGAVLHGPGPhsDHTHGTDLGWYMAVGTHSGKEPSTATLRSPVMREAAPT-CeLRL 149
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSShC-LSF 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238814398  150 WYHIASRDVAELRL---DLTHGVETLtLWQTSGPWGPGWQELAVNTGRIQGDFKVTFSATRNATHRGAVALDDVEFRD 224
Cdd:cd06263    78 WYHMYGSGVGTLNVyvrEEGGGLGTL-LWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 983-1144 6.96e-35

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 130.58  E-value: 6.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  983 CDFETGLCGWSHLPWpslGGYSWDWSSGATPSRYPQPsvDHTLGTEAGHFAFFETSVlGPGGQAAWLRSEPLPAT-TVSC 1061
Cdd:cd06263     1 CDFEDGLCGWTQDST---DDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398 1062 LRFWYYMGFPEHfykGELRVLLSSARGQL--AVWYQGGHLRDQWLQVQIELS-NSEEFQIVFEATLGGQPAlGPIAIDDV 1138
Cdd:cd06263    75 LSFWYHMYGSGV---GTLNVYVREEGGGLgtLLWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSR-GDIALDDI 150


                  ....*.
gi 238814398 1139 QYLAGQ 1144
Cdd:cd06263   151 SLSPGP 156
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 254-427 2.16e-34

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 129.39  E-value: 2.16e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    254 DGEDNCGDrsdEDPLICSHHMATDFEtglGPWNQLEGWTRNhsagsmvspAWPHRDHSRNS-AYGFFLISVAKPGTTAVL 332
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSATGI---------PGPNRDHTTGNgHFMFFETSSGAEGQTARL 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    333 YSPEFQGSVSNNCsFTFYYYLHGSEASHFQLFLqaQGLNTPQVPvLLRSRHGELGTAWVRDRVDIQS-AHPFRILLAGET 411
Cdd:smart00137   66 LSPPLYENRSTHC-LTFWYYMYGSGSGTLNVYV--RENNGSQDT-LLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTR 141

                           170
                    ....*....|....*...
gi 238814398    412 GPG--GVVGLDDLIMSSH 427
Cdd:smart00137  142 GKGhsGYIALDDILLSNG 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 276-429 4.86e-28

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 111.30  E-value: 4.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   276 TDFETG-LGPWNQLE----GWTRNHSagsMVSPAWPHRDHSRNSAYGFFLI---SVAKPGTTAVLYSPEFQGSVSNNCsF 347
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERVSG---PSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   348 TFYYYLHGSEASHFQLFLQAQGlntPQVPVLLRSRHGELGTAWVRDRVDIQS-AHPFRILLAGE--TGPGGVVGLDDLIM 424
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENG---GTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIrgGGSRGGIALDDISL 153


                   ....*.
gi 238814398   425 SS-HCM 429
Cdd:pfam00629  154 SSgPCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 822-977 5.31e-27

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 108.20  E-value: 5.31e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    822 SCSFED-SDCGF--SPGGWGLWTHQSNASGLAswGPWIDHTTGTaqGHYMVVDTSPnvLPKGHVAALTSEEHQPLSQPAC 898
Cdd:smart00137    5 NCDFEEgSTCGWhqDSNDDGHWERVSSATGIP--GPNRDHTTGN--GHFMFFETSS--GAEGQTARLLSPPLYENRSTHC 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    899 LTFWYHMSVPNPGTLRVHVEESTRRQE---LSISAHGRSAWRLGSVNVQAE-QAWKVVFEAVAAGVEYSYMALDDISLQD 974
Cdd:smart00137   79 LTFWYYMYGSGSGTLNVYVRENNGSQDtllWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 238814398    975 GPC 977
Cdd:smart00137  159 GPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 498-652 7.15e-27

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 107.83  E-value: 7.15e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   498 TDFESASAGGWEDISVGKLQWQWVEA-QEKSKPAGDANRDAP-GHFLSLQKAWGQLRSEARALTPALGPSG-PHCeLHMA 574
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSDHTQGTGsGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQC-LRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   575 YYFQSHPQGFLALVVVENGFR--ELLWQAPGGGSGSWTEEKIILGARRRPFQLEFVSLVdlDGPGQQGAGVDNVTL--RD 650
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGP 157


                   ..
gi 238814398   651 CN 652
Cdd:pfam00629  158 CP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 499-650 5.56e-18

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 82.43  E-value: 5.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  499 DFESaSAGGWEDISVGKLQWQWVEAQEKSK--PAGDANRDAPGHFLSLQKAWGQLRSEARALTPAL-GPSGPHCeLHMAY 575
Cdd:cd06263     2 DFED-GLCGWTQDSTDDFDWTRVSGSTPSPgtPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLpPPRSSHC-LSFWY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238814398  576 YFQSHPQGFLALVVVENG--FRELLWQAPGGGSGSWTEEKIILGARRRPFQLEFVSLVdldGPGQQGA-GVDNVTLRD 650
Cdd:cd06263    80 HMYGSGVGTLNVYVREEGggLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVR---GSGSRGDiALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 277-427 1.72e-17

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 80.88  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  277 DFETGLGPWNQLEG----WTRNHSAGSMVSPawpHRDHSRNSAYGFFLI---SVAKPGTTAVLYSPEFQGSVSNNCsFTF 349
Cdd:cd06263     2 DFEDGLCGWTQDSTddfdWTRVSGSTPSPGT---PPDHTHGTGSGHYLYvesSSGREGQKARLLSPLLPPPRSSHC-LSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  350 YYYLHGSEASHFQLFLQAQGLNTPQvpvLLRSRHGELGTAWVRDRVDIQSAH-PFRILLAGETGPG--GVVGLDDLIMSS 426
Cdd:cd06263    78 WYHMYGSGVGTLNVYVREEGGGLGT---LLWSASGGQGNQWQEAEVTLSASSkPFQVVFEGVRGSGsrGDIALDDISLSP 154


                  .
gi 238814398  427 H 427
Cdd:cd06263   155 G 155
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 234-266 7.43e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 52.21  E-value: 7.43e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 238814398  234 CPLGHHHCQNKACVEPHQLCDGEDNCGDRSDED 266
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 233-265 2.46e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 50.71  E-value: 2.46e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 238814398    233 RCPLGHHHCQNKACVEPHQLCDGEDNCGDRSDE 265
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 462-495 8.94e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 43.73  E-value: 8.94e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 238814398  462 CEPGHLSCGD-LCVPPEQLCDFQKHCAEGEDEHKC 495
Cdd:cd00112     1 CPPNEFRCANgRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
233-265 1.20e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.31  E-value: 1.20e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 238814398   233 RCPLGHHHCQNKACVEPHQLCDGEDNCGDRSDE 265
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 461-492 3.80e-04

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 38.77  E-value: 3.80e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 238814398    461 TCEPGHLSCGD-LCVPPEQLCDFQKHCAEGEDE 492
Cdd:smart00192    1 TCPPGEFQCDNgRCIPSSWVCDGVDDCGDGSDE 33
 
Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 660-817 5.33e-52

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 179.85  E-value: 5.33e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    660 DQELSCNFERDS-CSWHTGHLTDAHWHRIKSH----GSQLDHTTGQGFFMFLDpTDPPARGQGALLLTRPQVPVVPKECL 734
Cdd:smart00137    1 TSPGNCDFEEGStCGWHQDSNDDGHWERVSSAtgipGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    735 SFWYRLYGPQIGTLCLAMR-REREEDILLWSRSGTHGNRWHQAWVTLHHQPEastKYQLLFEGLRN-GYHGTMALDDIAV 812
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVReNNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRGkGHSGYIALDDILL 156


                    ....*
gi 238814398    813 RPGPC 817
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 665-818 1.63e-43

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 155.60  E-value: 1.63e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   665 CNFERDS-CSWHTGHLTDAHWHRIKSH----GSQLDHT--TGQGFFMFLDPTDPPArGQGALLLTRPQVPVVPKECLSFW 737
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPsvktGPSSDHTqgTGSGHFMYVDTSSGAP-GQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   738 YRLYGPQIGTLCLAMRREREE-DILLWSRSGTHGNRWHQAWVTLHHQPEastKYQLLFEGLR-NGYHGTMALDDIAVRPG 815
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTlDTLLWSISGDQGPSWKEARVTLSSSTQ---PFQVVFEGIRgGGSRGGIALDDISLSSG 156


                   ...
gi 238814398   816 PCW 818
Cdd:pfam00629  157 PCP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 823-978 7.15e-40

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 145.20  E-value: 7.15e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   823 CSFEDSD-CGFS--PGGWGLWTHQSnaSGLASWGPWIDHTTGTAQGHYMVVDTSpnVLPKGHVAALTSEEHQPLSQPACL 899
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVS--GPSVKTGPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   900 TFWYHMSVPNPGTLRVHVEESTRRQE---LSISAHGRSAWRLGSVNVQA-EQAWKVVFEAVAAGVEYSYMALDDISLQDG 975
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDtllWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 238814398   976 PCP 978
Cdd:pfam00629  157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 823-977 8.07e-40

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 144.83  E-value: 8.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  823 CSFEDSDCGFSPG--GWGLWTHQSNASGlaSWGPWIDHTTGTAQGHYMVVDTSPNvlPKGHVAALTSEEHQPLSQPACLT 900
Cdd:cd06263     1 CDFEDGLCGWTQDstDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSG--REGQKARLLSPLLPPPRSSHCLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  901 FWYHMSVPNPGTLRVHV-EESTRRQEL--SISAHGRSAWRLGSVNVQAEQA-WKVVFEAVAAGVEYSYMALDDISLQDGP 976
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVrEEGGGLGTLlwSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSPGP 156


                  .
gi 238814398  977 C 977
Cdd:cd06263   157 C 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 978-1144 9.35e-40

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 144.79  E-value: 9.35e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    978 PQPGSCDFETG-LCGWSHLPWPslgGYSWDWSSGATPSRYPQpsVDHTLGTeaGHFAFFETSVLGPGgQAAWLRSEPLPA 1056
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSND---DGHWERVSSATGIPGPN--RDHTTGN--GHFMFFETSSGAEG-QTARLLSPPLYE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   1057 T-TVSCLRFWYYMGFPEHfykGELRVLLSSARGQLA--VWYQGGHLRDQWLQVQIELSNS-EEFQIVFEATLGGqPALGP 1132
Cdd:smart00137   73 NrSTHCLTFWYYMYGSGS---GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGK-GHSGY 148

                           170
                    ....*....|..
gi 238814398   1133 IAIDDVQYLAGQ 1144
Cdd:smart00137  149 IALDDILLSNGP 160
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 665-817 2.32e-39

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 143.67  E-value: 2.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  665 CNFERDSCSWHTGHLTDAHWHRIKS------HGSQLDHTTGQGFFMFLDpTDPPARGQGALLLTRPQVPVVPKECLSFWY 738
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGstpspgTPPDHTHGTGSGHYLYVE-SSSGREGQKARLLSPLLPPPRSSHCLSFWY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  739 RLYGPQIGTLCLAMRREREE-DILLWSRSGTHGNRWHQAWVTLHHQPEastKYQLLFEGLR-NGYHGTMALDDIAVRPGP 816
Cdd:cd06263    80 HMYGSGVGTLNVYVREEGGGlGTLLWSASGGQGNQWQEAEVTLSASSK---PFQVVFEGVRgSGSRGDIALDDISLSPGP 156


                  .
gi 238814398  817 C 817
Cdd:cd06263   157 C 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 983-1146 2.16e-38

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 140.96  E-value: 2.16e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   983 CDFETG-LCGWSHlpwPSLGGYSWDWSSGatPSRYPQPSVDHTLGTEAGHFAFFETSvLGPGGQAAWLRSEPLPAT-TVS 1060
Cdd:pfam00629    1 CDFEDGnLCGWTQ---DSSDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDTS-SGAPGQTARLLSPLLPPSrSPQ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  1061 CLRFWYYMGFPehfYKGELRVLLSSARGQL--AVWYQGGHLRDQWLQVQIELS-NSEEFQIVFEATLGGqPALGPIAIDD 1137
Cdd:pfam00629   75 CLRFWYHMSGS---GVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSsSTQPFQVVFEGIRGG-GSRGGIALDD 150


                   ....*....
gi 238814398  1138 VQyLAGQQC 1146
Cdd:pfam00629  151 IS-LSSGPC 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 66-224 2.99e-38

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 140.56  E-value: 2.99e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398     66 STSFTCNFEQDS-CGWQDISTSGYRWLRDRAGAvlHGPGPHSDHTHGTdlGWYMAVGTHSGKEPSTATLRSPVMREAAPT 144
Cdd:smart00137    1 TSPGNCDFEEGStCGWHQDSNDDGHWERVSSAT--GIPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    145 CELRLWYHIASRDVAELRLDLT--HGVETLTLWQTSGPWGPGWQELAVNTGRIQGDFKVTFSATRNATHRGAVALDDVEF 222
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ..
gi 238814398    223 RD 224
Cdd:smart00137  157 SN 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 71-226 5.12e-37

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 136.72  E-value: 5.12e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    71 CNFEQDS-CGWQDISTSGYRWLRDRAGAVlhGPGPHSDHTHGTDLGWYMAVGTHSGKEPSTATLRSPVMREAAPTCELRL 149
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   150 WYHIASRDVAELRLDLTHGVETL--TLWQTSGPWGPGWQELAVNTGRIQGDFKVTFSATRNATHRGAVALDDVEF--RDC 225
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISLssGPC 158


                   .
gi 238814398   226 G 226
Cdd:pfam00629  159 P 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 71-224 5.10e-36

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 134.04  E-value: 5.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   71 CNFEQDSCGWQDISTSGYRWLRDRAGAVLHGPGPhsDHTHGTDLGWYMAVGTHSGKEPSTATLRSPVMREAAPT-CeLRL 149
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSShC-LSF 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238814398  150 WYHIASRDVAELRL---DLTHGVETLtLWQTSGPWGPGWQELAVNTGRIQGDFKVTFSATRNATHRGAVALDDVEFRD 224
Cdd:cd06263    78 WYHMYGSGVGTLNVyvrEEGGGLGTL-LWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 983-1144 6.96e-35

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 130.58  E-value: 6.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  983 CDFETGLCGWSHLPWpslGGYSWDWSSGATPSRYPQPsvDHTLGTEAGHFAFFETSVlGPGGQAAWLRSEPLPAT-TVSC 1061
Cdd:cd06263     1 CDFEDGLCGWTQDST---DDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398 1062 LRFWYYMGFPEHfykGELRVLLSSARGQL--AVWYQGGHLRDQWLQVQIELS-NSEEFQIVFEATLGGQPAlGPIAIDDV 1138
Cdd:cd06263    75 LSFWYHMYGSGV---GTLNVYVREEGGGLgtLLWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSR-GDIALDDI 150


                  ....*.
gi 238814398 1139 QYLAGQ 1144
Cdd:cd06263   151 SLSPGP 156
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 254-427 2.16e-34

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 129.39  E-value: 2.16e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    254 DGEDNCGDrsdEDPLICSHHMATDFEtglGPWNQLEGWTRNhsagsmvspAWPHRDHSRNS-AYGFFLISVAKPGTTAVL 332
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSATGI---------PGPNRDHTTGNgHFMFFETSSGAEGQTARL 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    333 YSPEFQGSVSNNCsFTFYYYLHGSEASHFQLFLqaQGLNTPQVPvLLRSRHGELGTAWVRDRVDIQS-AHPFRILLAGET 411
Cdd:smart00137   66 LSPPLYENRSTHC-LTFWYYMYGSGSGTLNVYV--RENNGSQDT-LLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTR 141

                           170
                    ....*....|....*...
gi 238814398    412 GPG--GVVGLDDLIMSSH 427
Cdd:smart00137  142 GKGhsGYIALDDILLSNG 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 276-429 4.86e-28

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 111.30  E-value: 4.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   276 TDFETG-LGPWNQLE----GWTRNHSagsMVSPAWPHRDHSRNSAYGFFLI---SVAKPGTTAVLYSPEFQGSVSNNCsF 347
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERVSG---PSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   348 TFYYYLHGSEASHFQLFLQAQGlntPQVPVLLRSRHGELGTAWVRDRVDIQS-AHPFRILLAGE--TGPGGVVGLDDLIM 424
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENG---GTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIrgGGSRGGIALDDISL 153


                   ....*.
gi 238814398   425 SS-HCM 429
Cdd:pfam00629  154 SSgPCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 822-977 5.31e-27

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 108.20  E-value: 5.31e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    822 SCSFED-SDCGF--SPGGWGLWTHQSNASGLAswGPWIDHTTGTaqGHYMVVDTSPnvLPKGHVAALTSEEHQPLSQPAC 898
Cdd:smart00137    5 NCDFEEgSTCGWhqDSNDDGHWERVSSATGIP--GPNRDHTTGN--GHFMFFETSS--GAEGQTARLLSPPLYENRSTHC 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398    899 LTFWYHMSVPNPGTLRVHVEESTRRQE---LSISAHGRSAWRLGSVNVQAE-QAWKVVFEAVAAGVEYSYMALDDISLQD 974
Cdd:smart00137   79 LTFWYYMYGSGSGTLNVYVRENNGSQDtllWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 238814398    975 GPC 977
Cdd:smart00137  159 GPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 498-652 7.15e-27

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 107.83  E-value: 7.15e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   498 TDFESASAGGWEDISVGKLQWQWVEA-QEKSKPAGDANRDAP-GHFLSLQKAWGQLRSEARALTPALGPSG-PHCeLHMA 574
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSDHTQGTGsGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQC-LRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398   575 YYFQSHPQGFLALVVVENGFR--ELLWQAPGGGSGSWTEEKIILGARRRPFQLEFVSLVdlDGPGQQGAGVDNVTL--RD 650
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGP 157


                   ..
gi 238814398   651 CN 652
Cdd:pfam00629  158 CP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 499-650 5.56e-18

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 82.43  E-value: 5.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  499 DFESaSAGGWEDISVGKLQWQWVEAQEKSK--PAGDANRDAPGHFLSLQKAWGQLRSEARALTPAL-GPSGPHCeLHMAY 575
Cdd:cd06263     2 DFED-GLCGWTQDSTDDFDWTRVSGSTPSPgtPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLpPPRSSHC-LSFWY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238814398  576 YFQSHPQGFLALVVVENG--FRELLWQAPGGGSGSWTEEKIILGARRRPFQLEFVSLVdldGPGQQGA-GVDNVTLRD 650
Cdd:cd06263    80 HMYGSGVGTLNVYVREEGggLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVR---GSGSRGDiALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 277-427 1.72e-17

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 80.88  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  277 DFETGLGPWNQLEG----WTRNHSAGSMVSPawpHRDHSRNSAYGFFLI---SVAKPGTTAVLYSPEFQGSVSNNCsFTF 349
Cdd:cd06263     2 DFEDGLCGWTQDSTddfdWTRVSGSTPSPGT---PPDHTHGTGSGHYLYvesSSGREGQKARLLSPLLPPPRSSHC-LSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814398  350 YYYLHGSEASHFQLFLQAQGLNTPQvpvLLRSRHGELGTAWVRDRVDIQSAH-PFRILLAGETGPG--GVVGLDDLIMSS 426
Cdd:cd06263    78 WYHMYGSGVGTLNVYVREEGGGLGT---LLWSASGGQGNQWQEAEVTLSASSkPFQVVFEGVRGSGsrGDIALDDISLSP 154


                  .
gi 238814398  427 H 427
Cdd:cd06263   155 G 155
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 234-266 7.43e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 52.21  E-value: 7.43e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 238814398  234 CPLGHHHCQNKACVEPHQLCDGEDNCGDRSDED 266
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 233-265 2.46e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 50.71  E-value: 2.46e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 238814398    233 RCPLGHHHCQNKACVEPHQLCDGEDNCGDRSDE 265
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 462-495 8.94e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 43.73  E-value: 8.94e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 238814398  462 CEPGHLSCGD-LCVPPEQLCDFQKHCAEGEDEHKC 495
Cdd:cd00112     1 CPPNEFRCANgRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
233-265 1.20e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.31  E-value: 1.20e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 238814398   233 RCPLGHHHCQNKACVEPHQLCDGEDNCGDRSDE 265
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 461-492 3.80e-04

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 38.77  E-value: 3.80e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 238814398    461 TCEPGHLSCGD-LCVPPEQLCDFQKHCAEGEDE 492
Cdd:smart00192    1 TCPPGEFQCDNgRCIPSSWVCDGVDDCGDGSDE 33
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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