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Conserved domains on  [gi|777776|gb|AAA65200|]
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apical endosomal glycoprotein [Rattus norvegicus]

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 ...
 654-811 3.50e-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: 180.23  E-value: 3.50e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       654 DQEVSCNFERDS-CSWHTGHLTDAHWHRVKSH----GSQYDHTTGQGFFMFLDPmDPPARGQGALLLTRPQVPVVPKECL 728
Cdd:smart00137    1 TSPGNCDFEEGStCGWHQDSNDDGHWERVSSAtgipGPNRDHTTGNGHFMFFET-SSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       729 SFWYHLHGPQIGTLCLAMR-REGEEDTLLWSRSGTHGNRWHQAWVTLHHqlqPSTKYQLLFEGLR-DGYHGTMGLDDMAV 806
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVReNNGSQDTLLWSRSGTQGGQWLQAEVALSS---WPQPFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 777776       807 RPGPC 811
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 817-972 2.54e-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: 154.83  E-value: 2.54e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      817 CSFEDSD-CGFS--PGDWGLWTRQNNASGLGpwGPWIDHTTGTAQGHYMVVDTSpnLLPKGHVASLTSEEHPPLSRPACL 893
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      894 SFWYHLSFHNPGTLRVFVEESTRRQE---LSISGHGGFAWRLGSVNVQA-EQAWKVVFEAMASGVEHSYMALDDISLQDG 969
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDtllWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 777776      970 PCA 972
Cdd:pfam00629  157 PCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 972-1138 6.81e-42

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: 150.96  E-value: 6.81e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       972 AQPGSCDFESG-LCGWSHLPWPGlggYSWDWSSGATpsRYPRPSVDHTVGTeaGHFAFFETSVLGPGgQAAWLGSEPLPA 1050
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDD---GHWERVSSAT--GIPGPNRDHTTGN--GHFMFFETSSGAEG-QTARLLSPPLYE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      1051 TA-VSCLHFWYYMGFPAHfykGELRVLLSSTQGQLA--VWHRGGHLRDQWLQVQIEVSSS-EEFQIVFEATLGGqPALGP 1126
Cdd:smart00137   73 NRsTHCLTFWYYMYGSGS---GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGK-GHSGY 148

                           170
                    ....*....|..
gi 777776      1127 IALDDVEYLAGQ 1138
Cdd:smart00137  149 IALDDILLSNGP 160
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 62-221 1.46e-41

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: 149.80  E-value: 1.46e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776        62 NTPFTCNFEQD-PCGWQDISTSGYRWLRDRAGAGLDssGPHSDHTRGTdlGWYMAVGTHSGKEPSTRTLRSPVMREAAPT 140
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATGIP--GPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       141 CELRLWYHTDSRDVAELRLDLT--HGMETLTLWQSSGPWGP-WPGRELAVNTgrIQGDFKVTFSATRNATHRGAVALDDM 217
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGqWLQAEVALSS--WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....
gi 777776       218 EFWD 221
Cdd:smart00137  155 LLSN 158
MAM super family cl42956
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 251-424 7.77e-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.


The actual alignment was detected with superfamily member smart00137:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 139.40  E-value: 7.77e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       251 DGEDNCGDssdEDPLICSHHMATDFEtglGPWTQLEGWTRNfsagsmvspAWPHRDHSRNS-AYGFFLVSVAKPGTTAVL 329
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSATGI---------PGPNRDHTTGNgHFMFFETSSGAEGQTARL 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       330 YSPEFQGSVSYNCsFTFYYYLHGSEANQFQLFVqaQGLNTTQPPvLLRSRHGELGTAWVRDRVNIQS-AHPFRILLAGET 408
Cdd:smart00137   66 LSPPLYENRSTHC-LTFWYYMYGSGSGTLNVYV--RENNGSQDT-LLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTR 141

                           170
                    ....*....|....*...
gi 777776       409 GPG--GFVGLDDLIMSNH 424
Cdd:smart00137  142 GKGhsGYIALDDILLSNG 159
MAM super family cl47572
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 492-646 1.79e-23

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.


The actual alignment was detected with superfamily member pfam00629:

Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 98.20  E-value: 1.79e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      492 TDFESASAGGWEDISIGKLQWQRAEA-QESGKPARD-TNRNAPGHFLSLRKAWGQLRSEARALTPTLGPSG-PHCeLHMT 568
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSDhTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQC-LRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      569 YYFHSHPQGFLALAVVENGFR--ELLWQAPSSSSGGWTLQKILLGARRWPFQLEFVSLVdlDGPGQQGAGVDNVTL--RD 644
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGP 157


                   ..
gi 777776      645 CN 646
Cdd:pfam00629  158 CP 159
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 231-263 1.32e-08

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: 51.44  E-value: 1.32e-08
                         10        20        30
                 ....*....|....*....|....*....|...
gi 777776    231 CPLGHHHCQNKACVEPHQLCDGEDNCGDSSDED 263
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 456-489 1.19e-04

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: 40.27  E-value: 1.19e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 777776    456 CDAGHLSC-DELCVPPEQLCDFQQHCAEGEDEEKC 489
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 ...
 654-811 3.50e-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: 180.23  E-value: 3.50e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       654 DQEVSCNFERDS-CSWHTGHLTDAHWHRVKSH----GSQYDHTTGQGFFMFLDPmDPPARGQGALLLTRPQVPVVPKECL 728
Cdd:smart00137    1 TSPGNCDFEEGStCGWHQDSNDDGHWERVSSAtgipGPNRDHTTGNGHFMFFET-SSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       729 SFWYHLHGPQIGTLCLAMR-REGEEDTLLWSRSGTHGNRWHQAWVTLHHqlqPSTKYQLLFEGLR-DGYHGTMGLDDMAV 806
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVReNNGSQDTLLWSRSGTQGGQWLQAEVALSS---WPQPFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 777776       807 RPGPC 811
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 817-972 2.54e-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: 154.83  E-value: 2.54e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      817 CSFEDSD-CGFS--PGDWGLWTRQNNASGLGpwGPWIDHTTGTAQGHYMVVDTSpnLLPKGHVASLTSEEHPPLSRPACL 893
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      894 SFWYHLSFHNPGTLRVFVEESTRRQE---LSISGHGGFAWRLGSVNVQA-EQAWKVVFEAMASGVEHSYMALDDISLQDG 969
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDtllWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 777776      970 PCA 972
Cdd:pfam00629  157 PCP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 659-812 4.09e-42

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: 151.36  E-value: 4.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      659 CNFERDS-CSWHTGHLTDAHWHRVKSH----GSQYDHT--TGQGFFMFLDPMDPPArGQGALLLTRPQVPVVPKECLSFW 731
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPsvktGPSSDHTqgTGSGHFMYVDTSSGAP-GQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      732 YHLHGPQIGTLCLAMRREGEE-DTLLWSRSGTHGNRWHQAWVTLHHQLQPstkYQLLFEGLRD-GYHGTMGLDDMAVRPG 809
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTlDTLLWSISGDQGPSWKEARVTLSSSTQP---FQVVFEGIRGgGSRGGIALDDISLSSG 156


                   ...
gi 777776      810 PCW 812
Cdd:pfam00629  157 PCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 972-1138 6.81e-42

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: 150.96  E-value: 6.81e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       972 AQPGSCDFESG-LCGWSHLPWPGlggYSWDWSSGATpsRYPRPSVDHTVGTeaGHFAFFETSVLGPGgQAAWLGSEPLPA 1050
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDD---GHWERVSSAT--GIPGPNRDHTTGN--GHFMFFETSSGAEG-QTARLLSPPLYE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      1051 TA-VSCLHFWYYMGFPAHfykGELRVLLSSTQGQLA--VWHRGGHLRDQWLQVQIEVSSS-EEFQIVFEATLGGqPALGP 1126
Cdd:smart00137   73 NRsTHCLTFWYYMYGSGS---GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGK-GHSGY 148

                           170
                    ....*....|..
gi 777776      1127 IALDDVEYLAGQ 1138
Cdd:smart00137  149 IALDDILLSNGP 160
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 62-221 1.46e-41

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: 149.80  E-value: 1.46e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776        62 NTPFTCNFEQD-PCGWQDISTSGYRWLRDRAGAGLDssGPHSDHTRGTdlGWYMAVGTHSGKEPSTRTLRSPVMREAAPT 140
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATGIP--GPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       141 CELRLWYHTDSRDVAELRLDLT--HGMETLTLWQSSGPWGP-WPGRELAVNTgrIQGDFKVTFSATRNATHRGAVALDDM 217
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGqWLQAEVALSS--WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....
gi 777776       218 EFWD 221
Cdd:smart00137  155 LLSN 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 817-971 1.19e-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: 147.14  E-value: 1.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    817 CSFEDSDCGFSPG--DWGLWTRQNNASGlgPWGPWIDHTTGTAQGHYMVVDTSPNllPKGHVASLTSEEHPPLSRPACLS 894
Cdd:cd06263    1 CDFEDGLCGWTQDstDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSG--REGQKARLLSPLLPPPRSSHCLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    895 FWYHLSFHNPGTLRVFV-EESTRRQEL--SISGHGGFAWRLGSVNVQAEQA-WKVVFEAMASGVEHSYMALDDISLQDGP 970
Cdd:cd06263   77 FWYHMYGSGVGTLNVYVrEEGGGLGTLlwSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSPGP 156


                 .
gi 777776    971 C 971
Cdd:cd06263  157 C 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 659-811 6.03e-38

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: 139.44  E-value: 6.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    659 CNFERDSCSWHTGHLTDAHWHRVKS------HGSQYDHTTGQGFFMFLDpMDPPARGQGALLLTRPQVPVVPKECLSFWY 732
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDFDWTRVSGstpspgTPPDHTHGTGSGHYLYVE-SSSGREGQKARLLSPLLPPPRSSHCLSFWY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    733 HLHGPQIGTLCLAMRREGEE-DTLLWSRSGTHGNRWHQAWVTLHHQLQPstkYQLLFEGLRD-GYHGTMGLDDMAVRPGP 810
Cdd:cd06263   80 HMYGSGVGTLNVYVREEGGGlGTLLWSASGGQGNQWQEAEVTLSASSKP---FQVVFEGVRGsGSRGDIALDDISLSPGP 156


                 .
gi 777776    811 C 811
Cdd:cd06263  157 C 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 251-424 7.77e-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: 139.40  E-value: 7.77e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       251 DGEDNCGDssdEDPLICSHHMATDFEtglGPWTQLEGWTRNfsagsmvspAWPHRDHSRNS-AYGFFLVSVAKPGTTAVL 329
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSATGI---------PGPNRDHTTGNgHFMFFETSSGAEGQTARL 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       330 YSPEFQGSVSYNCsFTFYYYLHGSEANQFQLFVqaQGLNTTQPPvLLRSRHGELGTAWVRDRVNIQS-AHPFRILLAGET 408
Cdd:smart00137   66 LSPPLYENRSTHC-LTFWYYMYGSGSGTLNVYV--RENNGSQDT-LLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTR 141

                           170
                    ....*....|....*...
gi 777776       409 GPG--GFVGLDDLIMSNH 424
Cdd:smart00137  142 GKGhsGYIALDDILLSNG 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 977-1140 1.74e-36

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: 135.18  E-value: 1.74e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      977 CDFESG-LCGWSHLPWPGLggyswDWSSGATPSRYPRPSVDHTVGTEAGHFAFFETSvLGPGGQAAWLGSEPLPATAVS- 1054
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDF-----DWERVSGPSVKTGPSSDHTQGTGSGHFMYVDTS-SGAPGQTARLLSPLLPPSRSPq 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776     1055 CLHFWYYMGFPahfYKGELRVLLSSTQGQL--AVWHRGGHLRDQWLQVQIEVSS-SEEFQIVFEATLGGqPALGPIALDD 1131
Cdd:pfam00629   75 CLRFWYHMSGS---GVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGG-GSRGGIALDD 150


                   ....*....
gi 777776     1132 VEyLAGQHC 1140
Cdd:pfam00629  151 IS-LSSGPC 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 977-1138 7.57e-34

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: 127.88  E-value: 7.57e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    977 CDFESGLCGWSHLPWPGLggySWDWSSGATPSRYPRPsvDHTVGTEAGHFAFFETSVlGPGGQAAWLGSEPLPATA-VSC 1055
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDF---DWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPRsSHC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776   1056 LHFWYYMGFPAHfykGELRVLLSSTQGQL--AVWHRGGHLRDQWLQVQIEVSS-SEEFQIVFEATLGGQPAlGPIALDDV 1132
Cdd:cd06263   75 LSFWYHMYGSGV---GTLNVYVREEGGGLgtLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSR-GDIALDDI 150


                 ....*.
gi 777776   1133 EYLAGQ 1138
Cdd:cd06263  151 SLSPGP 156
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 67-216 4.26e-29

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: 114.38  E-value: 4.26e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       67 CNFEQDP-CGWQDISTSGYRWLRDRAGAGldSSGPHSDHTRGTDLGWYMAVGTHSGKEPSTRTLRSPVMREAAPTCELRL 145
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 777776      146 WYHTDSRDVAELRLDLTH--GMETLTLWQSSGPWGP-WpgRELAVNTGRIQGDFKVTFSATRNATHRGAVALDD 216
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVREngGTLDTLLWSISGDQGPsW--KEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDD 150
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 273-425 5.33e-29

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: 114.00  E-value: 5.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      273 TDFETG-LGPWTQLE----GWTRNfsaGSMVSPAWPHRDHSRNSAYGFFLV---SVAKPGTTAVLYSPEFQGSVSYNCsF 344
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERV---SGPSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      345 TFYYYLHGSEANQFQLFVQAQGlntTQPPVLLRSRHGELGTAWVRDRVNIQS-AHPFRILLAGE--TGPGGFVGLDD-LI 420
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENG---GTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIrgGGSRGGIALDDiSL 153


                   ....*
gi 777776      421 MSNHC 425
Cdd:pfam00629  154 SSGPC 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 817-971 5.14e-28

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: 111.28  E-value: 5.14e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       817 CSFED-SDCGF--SPGDWGLWTRQNNASGlgPWGPWIDHTTGTaqGHYMVVDTSPnlLPKGHVASLTSEEHPPLSRPACL 893
Cdd:smart00137    6 CDFEEgSTCGWhqDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSS--GAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       894 SFWYHLSFHNPGTLRVFVEESTRRQE---LSISGHGGFAWRLGSVNVQAE-QAWKVVFEAMASGVEHSYMALDDISLQDG 969
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVRENNGSQDtllWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGKGHSGYIALDDILLSNG 159


                    ..
gi 777776       970 PC 971
Cdd:smart00137  160 PC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 67-221 7.25e-28

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: 110.55  E-value: 7.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776     67 CNFEQDPCGWQDISTSGYRWLRDRAGAGldSSGPHSDHTRGTDLGWYMAVGTHSGKEPSTRTLRSPVMREAAPT-CeLRL 145
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSShC-LSF 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 777776    146 WYHTDSRDVAELRLDLTHGMETLT--LWQSSGPWGP-WpgRELAVNTGRIQGDFKVTFSATRNATHRGAVALDDMEFWD 221
Cdd:cd06263   78 WYHMYGSGVGTLNVYVREEGGGLGtlLWSASGGQGNqW--QEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 492-646 1.79e-23

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: 98.20  E-value: 1.79e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      492 TDFESASAGGWEDISIGKLQWQRAEA-QESGKPARD-TNRNAPGHFLSLRKAWGQLRSEARALTPTLGPSG-PHCeLHMT 568
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSDhTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQC-LRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      569 YYFHSHPQGFLALAVVENGFR--ELLWQAPSSSSGGWTLQKILLGARRWPFQLEFVSLVdlDGPGQQGAGVDNVTL--RD 644
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGP 157


                   ..
gi 777776      645 CN 646
Cdd:pfam00629  158 CP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 274-424 1.16e-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: 84.35  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    274 DFETGLGPWTQLEG----WTRNFSAGSMVSPawpHRDHSRNSAYGFFLV---SVAKPGTTAVLYSPEFQGSVSYNCsFTF 346
Cdd:cd06263    2 DFEDGLCGWTQDSTddfdWTRVSGSTPSPGT---PPDHTHGTGSGHYLYvesSSGREGQKARLLSPLLPPPRSSHC-LSF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    347 YYYLHGSEANQFQLFVQAQGlntTQPPVLLRSRHGELGTAWVRDRVNIQSAH-PFRILLAGETGPG--GFVGLDDLIMSN 423
Cdd:cd06263   78 WYHMYGSGVGTLNVYVREEG---GGLGTLLWSASGGQGNQWQEAEVTLSASSkPFQVVFEGVRGSGsrGDIALDDISLSP 154


                 .
gi 777776    424 H 424
Cdd:cd06263  155 G 155
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 493-644 1.60e-15

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: 75.11  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    493 DFESaSAGGWEDISIGKLQWQRAEAQE--SGKPARDTNRNAPGHFLSLRKAWGQLRSEARALTPTL-GPSGPHCeLHMTY 569
Cdd:cd06263    2 DFED-GLCGWTQDSTDDFDWTRVSGSTpsPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLpPPRSSHC-LSFWY 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 777776    570 YFHSHPQGFLALAVVENG--FRELLWQAPSSSSGGWTLQKILLGARRWPFQLEFVSLVdldGPGQQGA-GVDNVTLRD 644
Cdd:cd06263   80 HMYGSGVGTLNVYVREEGggLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVR---GSGSRGDiALDDISLSP 154
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 231-263 1.32e-08

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: 51.44  E-value: 1.32e-08
                         10        20        30
                 ....*....|....*....|....*....|...
gi 777776    231 CPLGHHHCQNKACVEPHQLCDGEDNCGDSSDED 263
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 230-262 3.13e-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: 50.32  E-value: 3.13e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 777776       230 RCPLGHHHCQNKACVEPHQLCDGEDNCGDSSDE 262
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 456-489 1.19e-04

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: 40.27  E-value: 1.19e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 777776    456 CDAGHLSC-DELCVPPEQLCDFQQHCAEGEDEEKC 489
Cdd:cd00112    1 CPPNEFRCaNGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
230-262 3.96e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 38.77  E-value: 3.96e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 777776      230 RCPLGHHHCQNKACVEPHQLCDGEDNCGDSSDE 262
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
 
Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 654-811 3.50e-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: 180.23  E-value: 3.50e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       654 DQEVSCNFERDS-CSWHTGHLTDAHWHRVKSH----GSQYDHTTGQGFFMFLDPmDPPARGQGALLLTRPQVPVVPKECL 728
Cdd:smart00137    1 TSPGNCDFEEGStCGWHQDSNDDGHWERVSSAtgipGPNRDHTTGNGHFMFFET-SSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       729 SFWYHLHGPQIGTLCLAMR-REGEEDTLLWSRSGTHGNRWHQAWVTLHHqlqPSTKYQLLFEGLR-DGYHGTMGLDDMAV 806
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVReNNGSQDTLLWSRSGTQGGQWLQAEVALSS---WPQPFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 777776       807 RPGPC 811
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 817-972 2.54e-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: 154.83  E-value: 2.54e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      817 CSFEDSD-CGFS--PGDWGLWTRQNNASGLGpwGPWIDHTTGTAQGHYMVVDTSpnLLPKGHVASLTSEEHPPLSRPACL 893
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      894 SFWYHLSFHNPGTLRVFVEESTRRQE---LSISGHGGFAWRLGSVNVQA-EQAWKVVFEAMASGVEHSYMALDDISLQDG 969
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDtllWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 777776      970 PCA 972
Cdd:pfam00629  157 PCP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 659-812 4.09e-42

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: 151.36  E-value: 4.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      659 CNFERDS-CSWHTGHLTDAHWHRVKSH----GSQYDHT--TGQGFFMFLDPMDPPArGQGALLLTRPQVPVVPKECLSFW 731
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPsvktGPSSDHTqgTGSGHFMYVDTSSGAP-GQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      732 YHLHGPQIGTLCLAMRREGEE-DTLLWSRSGTHGNRWHQAWVTLHHQLQPstkYQLLFEGLRD-GYHGTMGLDDMAVRPG 809
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTlDTLLWSISGDQGPSWKEARVTLSSSTQP---FQVVFEGIRGgGSRGGIALDDISLSSG 156


                   ...
gi 777776      810 PCW 812
Cdd:pfam00629  157 PCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 972-1138 6.81e-42

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: 150.96  E-value: 6.81e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       972 AQPGSCDFESG-LCGWSHLPWPGlggYSWDWSSGATpsRYPRPSVDHTVGTeaGHFAFFETSVLGPGgQAAWLGSEPLPA 1050
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDD---GHWERVSSAT--GIPGPNRDHTTGN--GHFMFFETSSGAEG-QTARLLSPPLYE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      1051 TA-VSCLHFWYYMGFPAHfykGELRVLLSSTQGQLA--VWHRGGHLRDQWLQVQIEVSSS-EEFQIVFEATLGGqPALGP 1126
Cdd:smart00137   73 NRsTHCLTFWYYMYGSGS---GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGK-GHSGY 148

                           170
                    ....*....|..
gi 777776      1127 IALDDVEYLAGQ 1138
Cdd:smart00137  149 IALDDILLSNGP 160
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 62-221 1.46e-41

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: 149.80  E-value: 1.46e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776        62 NTPFTCNFEQD-PCGWQDISTSGYRWLRDRAGAGLDssGPHSDHTRGTdlGWYMAVGTHSGKEPSTRTLRSPVMREAAPT 140
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATGIP--GPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       141 CELRLWYHTDSRDVAELRLDLT--HGMETLTLWQSSGPWGP-WPGRELAVNTgrIQGDFKVTFSATRNATHRGAVALDDM 217
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGqWLQAEVALSS--WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....
gi 777776       218 EFWD 221
Cdd:smart00137  155 LLSN 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 817-971 1.19e-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: 147.14  E-value: 1.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    817 CSFEDSDCGFSPG--DWGLWTRQNNASGlgPWGPWIDHTTGTAQGHYMVVDTSPNllPKGHVASLTSEEHPPLSRPACLS 894
Cdd:cd06263    1 CDFEDGLCGWTQDstDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSG--REGQKARLLSPLLPPPRSSHCLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    895 FWYHLSFHNPGTLRVFV-EESTRRQEL--SISGHGGFAWRLGSVNVQAEQA-WKVVFEAMASGVEHSYMALDDISLQDGP 970
Cdd:cd06263   77 FWYHMYGSGVGTLNVYVrEEGGGLGTLlwSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSPGP 156


                 .
gi 777776    971 C 971
Cdd:cd06263  157 C 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 659-811 6.03e-38

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: 139.44  E-value: 6.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    659 CNFERDSCSWHTGHLTDAHWHRVKS------HGSQYDHTTGQGFFMFLDpMDPPARGQGALLLTRPQVPVVPKECLSFWY 732
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDFDWTRVSGstpspgTPPDHTHGTGSGHYLYVE-SSSGREGQKARLLSPLLPPPRSSHCLSFWY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    733 HLHGPQIGTLCLAMRREGEE-DTLLWSRSGTHGNRWHQAWVTLHHQLQPstkYQLLFEGLRD-GYHGTMGLDDMAVRPGP 810
Cdd:cd06263   80 HMYGSGVGTLNVYVREEGGGlGTLLWSASGGQGNQWQEAEVTLSASSKP---FQVVFEGVRGsGSRGDIALDDISLSPGP 156


                 .
gi 777776    811 C 811
Cdd:cd06263  157 C 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 251-424 7.77e-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: 139.40  E-value: 7.77e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       251 DGEDNCGDssdEDPLICSHHMATDFEtglGPWTQLEGWTRNfsagsmvspAWPHRDHSRNS-AYGFFLVSVAKPGTTAVL 329
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSATGI---------PGPNRDHTTGNgHFMFFETSSGAEGQTARL 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       330 YSPEFQGSVSYNCsFTFYYYLHGSEANQFQLFVqaQGLNTTQPPvLLRSRHGELGTAWVRDRVNIQS-AHPFRILLAGET 408
Cdd:smart00137   66 LSPPLYENRSTHC-LTFWYYMYGSGSGTLNVYV--RENNGSQDT-LLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTR 141

                           170
                    ....*....|....*...
gi 777776       409 GPG--GFVGLDDLIMSNH 424
Cdd:smart00137  142 GKGhsGYIALDDILLSNG 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 977-1140 1.74e-36

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: 135.18  E-value: 1.74e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      977 CDFESG-LCGWSHLPWPGLggyswDWSSGATPSRYPRPSVDHTVGTEAGHFAFFETSvLGPGGQAAWLGSEPLPATAVS- 1054
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDF-----DWERVSGPSVKTGPSSDHTQGTGSGHFMYVDTS-SGAPGQTARLLSPLLPPSRSPq 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776     1055 CLHFWYYMGFPahfYKGELRVLLSSTQGQL--AVWHRGGHLRDQWLQVQIEVSS-SEEFQIVFEATLGGqPALGPIALDD 1131
Cdd:pfam00629   75 CLRFWYHMSGS---GVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGG-GSRGGIALDD 150


                   ....*....
gi 777776     1132 VEyLAGQHC 1140
Cdd:pfam00629  151 IS-LSSGPC 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 977-1138 7.57e-34

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: 127.88  E-value: 7.57e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    977 CDFESGLCGWSHLPWPGLggySWDWSSGATPSRYPRPsvDHTVGTEAGHFAFFETSVlGPGGQAAWLGSEPLPATA-VSC 1055
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDF---DWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPRsSHC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776   1056 LHFWYYMGFPAHfykGELRVLLSSTQGQL--AVWHRGGHLRDQWLQVQIEVSS-SEEFQIVFEATLGGQPAlGPIALDDV 1132
Cdd:cd06263   75 LSFWYHMYGSGV---GTLNVYVREEGGGLgtLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSR-GDIALDDI 150


                 ....*.
gi 777776   1133 EYLAGQ 1138
Cdd:cd06263  151 SLSPGP 156
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 67-216 4.26e-29

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: 114.38  E-value: 4.26e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       67 CNFEQDP-CGWQDISTSGYRWLRDRAGAGldSSGPHSDHTRGTDLGWYMAVGTHSGKEPSTRTLRSPVMREAAPTCELRL 145
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 777776      146 WYHTDSRDVAELRLDLTH--GMETLTLWQSSGPWGP-WpgRELAVNTGRIQGDFKVTFSATRNATHRGAVALDD 216
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVREngGTLDTLLWSISGDQGPsW--KEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDD 150
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 273-425 5.33e-29

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: 114.00  E-value: 5.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      273 TDFETG-LGPWTQLE----GWTRNfsaGSMVSPAWPHRDHSRNSAYGFFLV---SVAKPGTTAVLYSPEFQGSVSYNCsF 344
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERV---SGPSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      345 TFYYYLHGSEANQFQLFVQAQGlntTQPPVLLRSRHGELGTAWVRDRVNIQS-AHPFRILLAGE--TGPGGFVGLDD-LI 420
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENG---GTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIrgGGSRGGIALDDiSL 153


                   ....*
gi 777776      421 MSNHC 425
Cdd:pfam00629  154 SSGPC 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 817-971 5.14e-28

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: 111.28  E-value: 5.14e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       817 CSFED-SDCGF--SPGDWGLWTRQNNASGlgPWGPWIDHTTGTaqGHYMVVDTSPnlLPKGHVASLTSEEHPPLSRPACL 893
Cdd:smart00137    6 CDFEEgSTCGWhqDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSS--GAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776       894 SFWYHLSFHNPGTLRVFVEESTRRQE---LSISGHGGFAWRLGSVNVQAE-QAWKVVFEAMASGVEHSYMALDDISLQDG 969
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVRENNGSQDtllWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGKGHSGYIALDDILLSNG 159


                    ..
gi 777776       970 PC 971
Cdd:smart00137  160 PC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 67-221 7.25e-28

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: 110.55  E-value: 7.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776     67 CNFEQDPCGWQDISTSGYRWLRDRAGAGldSSGPHSDHTRGTDLGWYMAVGTHSGKEPSTRTLRSPVMREAAPT-CeLRL 145
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSShC-LSF 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 777776    146 WYHTDSRDVAELRLDLTHGMETLT--LWQSSGPWGP-WpgRELAVNTGRIQGDFKVTFSATRNATHRGAVALDDMEFWD 221
Cdd:cd06263   78 WYHMYGSGVGTLNVYVREEGGGLGtlLWSASGGQGNqW--QEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 492-646 1.79e-23

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: 98.20  E-value: 1.79e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      492 TDFESASAGGWEDISIGKLQWQRAEA-QESGKPARD-TNRNAPGHFLSLRKAWGQLRSEARALTPTLGPSG-PHCeLHMT 568
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSDhTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQC-LRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776      569 YYFHSHPQGFLALAVVENGFR--ELLWQAPSSSSGGWTLQKILLGARRWPFQLEFVSLVdlDGPGQQGAGVDNVTL--RD 644
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGP 157


                   ..
gi 777776      645 CN 646
Cdd:pfam00629  158 CP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 274-424 1.16e-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: 84.35  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    274 DFETGLGPWTQLEG----WTRNFSAGSMVSPawpHRDHSRNSAYGFFLV---SVAKPGTTAVLYSPEFQGSVSYNCsFTF 346
Cdd:cd06263    2 DFEDGLCGWTQDSTddfdWTRVSGSTPSPGT---PPDHTHGTGSGHYLYvesSSGREGQKARLLSPLLPPPRSSHC-LSF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    347 YYYLHGSEANQFQLFVQAQGlntTQPPVLLRSRHGELGTAWVRDRVNIQSAH-PFRILLAGETGPG--GFVGLDDLIMSN 423
Cdd:cd06263   78 WYHMYGSGVGTLNVYVREEG---GGLGTLLWSASGGQGNQWQEAEVTLSASSkPFQVVFEGVRGSGsrGDIALDDISLSP 154


                 .
gi 777776    424 H 424
Cdd:cd06263  155 G 155
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 493-644 1.60e-15

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: 75.11  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777776    493 DFESaSAGGWEDISIGKLQWQRAEAQE--SGKPARDTNRNAPGHFLSLRKAWGQLRSEARALTPTL-GPSGPHCeLHMTY 569
Cdd:cd06263    2 DFED-GLCGWTQDSTDDFDWTRVSGSTpsPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLpPPRSSHC-LSFWY 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 777776    570 YFHSHPQGFLALAVVENG--FRELLWQAPSSSSGGWTLQKILLGARRWPFQLEFVSLVdldGPGQQGA-GVDNVTLRD 644
Cdd:cd06263   80 HMYGSGVGTLNVYVREEGggLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVR---GSGSRGDiALDDISLSP 154
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 231-263 1.32e-08

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: 51.44  E-value: 1.32e-08
                         10        20        30
                 ....*....|....*....|....*....|...
gi 777776    231 CPLGHHHCQNKACVEPHQLCDGEDNCGDSSDED 263
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 230-262 3.13e-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: 50.32  E-value: 3.13e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 777776       230 RCPLGHHHCQNKACVEPHQLCDGEDNCGDSSDE 262
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 456-489 1.19e-04

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: 40.27  E-value: 1.19e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 777776    456 CDAGHLSC-DELCVPPEQLCDFQQHCAEGEDEEKC 489
Cdd:cd00112    1 CPPNEFRCaNGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
230-262 3.96e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 38.77  E-value: 3.96e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 777776      230 RCPLGHHHCQNKACVEPHQLCDGEDNCGDSSDE 262
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
 
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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