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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011  827 CNFETGICNWEQDAKDDFDWTRSQGPTPTLNTGPmkDNTLGTAKGHYLYIESSEPQaFQDSAALLSPILNATDTKGCtFR 906
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGR-EGQKARLLSPLLPPPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960011  907 FYYHMFGKRIYRLAIYQRIWSDSRGQLLWQIFGNQGNRWIRKHLNISS-RQPFQILVEASVGDGFTGDIAIDDLSFMD 983
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGDIALDDISLSP 154

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011 1052 CSFEKrSLCKWYQpipvhllQDSNTFRWGLGNGISIHHGeenhrPSVDHTQNTTDGWYLYADSSNGKFGDTADILTPIIS 1131
Cdd:cd06263     1 CDFED-GLCGWTQ-------DSTDDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011 1132 LT-GPKCtLVFWTHMNGATVGSLQVLIKKDN--VTSKLWAQTGQQGAQWKRAEVFLG-IRSHTQIVFRAKRGISYIGDVA 1207
Cdd:cd06263    68 PPrSSHC-LSFWYHMYGSGVGTLNVYVREEGggLGTLLWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIA 146

                  ....*...
gi 767960011 1208 VDDISFQD 1215
Cdd:cd06263   147 LDDISLSP 154

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011  616 CDFEANSCDWfEAISGDHFDWIRSSQSELSADfehqaPPRDHSLNASQGHFMFILKKSSSLWQVAKLQSPTFSQT-GPGC 694
Cdd:cd06263     1 CDFEDGLCGW-TQDSTDDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011  695 iLSFWFYNYGLSVGAAELQLHMENSHDSTVIWRVLYNQGKQWLEATIQLGRLSQPFHLSLDKVSLGIYDGVSAIDDIRFE 774
Cdd:cd06263    75 -LSFWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLS 153

                  .
gi 767960011  775 N 775
Cdd:cd06263   154 P 154

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011   93 CDFEDGLCHMTQDQSLQPSWTKRSGMIGLS-PPFYDHNGDVSAHFLSLVSRVDSISSS--LRSRVFLPTNDQHdCqITFY 169
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPgTPPDHTHGTGSGHYLYVESSSGREGQKarLLSPLLPPPRSSH-C-LSFW 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960011  170 YF-SCQVSGKLMVGLQTACGGPIQHLWQNTAALPNQWERNVIKIQS-SQRFQVVFEGQMASTYEQDevIAIDDISFSSG 246
Cdd:cd06263    79 YHmYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGD--IALDDISLSPG 155

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.

                            10        20        30
                    ....*....|....*....|....*....|...
gi 767960011   1225 KCTDHEFMCANKHCIAKDKLCDFVNDCADNSDE 1257
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33

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.

                            10        20        30
                    ....*....|....*....|....*....|..
gi 767960011    454 CSADEFPCTSGQCIAKESVCDSRQDCSDESDE 485
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33

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

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 767960011 1865 CEADQFSCiYTLQCVPLSGKCDGHEDCIDGSDEMDC 1900
Cdd:cd00112     1 CPPNEFRC-ANGRCIPSSWVCDGEDDCGDGSDEENC 35

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

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767960011 1445 CPLGYRECHNGKCYRLEQSCNFVDNCGDNTDENEC 1479
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.

                           10        20        30
                   ....*....|....*....|....*....|.
gi 767960011  1987 CPLNYCRNGGTCVVEKNGPMCRCRQGWKGNR 2017
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011  827 CNFETGICNWEQDAKDDFDWTRSQGPTPTLNTGPmkDNTLGTAKGHYLYIESSEPQaFQDSAALLSPILNATDTKGCtFR 906
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGR-EGQKARLLSPLLPPPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960011  907 FYYHMFGKRIYRLAIYQRIWSDSRGQLLWQIFGNQGNRWIRKHLNISS-RQPFQILVEASVGDGFTGDIAIDDLSFMD 983
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGDIALDDISLSP 154

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011 1269 CDFEFDLCSWKQEKDEDFDWNLKASSIPAAGTEPaaDHTLGNSSGHYIFIKSLFPqQPMRAARISSPVIS-KRSKNCkII 1347
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSG-REGQKARLLSPLLPpPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960011 1348 FHYHMYGNGIGALTLMQVSVTNQTKVLL-NLTVEQGNFWRREELSLFG-DEDFQLKFEGRVGKGQRGDIALDDIVLTE 1423
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVREEGGGLGTLLwSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGDIALDDISLSP 154

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011    822 APELQCNFETG-ICNWEQDAKDDFDWTRSQGPTPtlNTGPMKDNTLGTakGHYLYIESSEPQAFQdSAALLSPILNATDT 900
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSSGAEGQ-TARLLSPPLYENRS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011    901 KGCtFRFYYHMFGKRIYRLAIYQRIWSDSRGQLLWQIFGNQGNRWIRKHLNISS-RQPFQILVEASVGDGFTGDIAIDDL 979
Cdd:smart00137   76 THC-LTFWYYMYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTRGKGHSGYIALDDI 154

                    ....
gi 767960011    980 SFMD 983
Cdd:smart00137  155 LLSN 158

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011  616 CDFEANSCDWfEAISGDHFDWIRSSQSELSADfehqaPPRDHSLNASQGHFMFILKKSSSLWQVAKLQSPTFSQT-GPGC 694
Cdd:cd06263     1 CDFEDGLCGW-TQDSTDDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011  695 iLSFWFYNYGLSVGAAELQLHMENSHDSTVIWRVLYNQGKQWLEATIQLGRLSQPFHLSLDKVSLGIYDGVSAIDDIRFE 774
Cdd:cd06263    75 -LSFWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLS 153

                  .
gi 767960011  775 N 775
Cdd:cd06263   154 P 154

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011   616 CDFE-ANSCDWFEAISgDHFDWIRSSqselsADFEHQAPPRDHSLNASQGHFMFILKKSSSLWQVAKLQSPTFSQTGPGC 694
Cdd:pfam00629    1 CDFEdGNLCGWTQDSS-DDFDWERVS-----GPSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011   695 ILSFWFYNYGLSVGAAELQLHMENSHDSTVIWRVLYNQGKQWLEATIQLGRLSQPFHLSLDKVSLGIYDGVSAIDDIRF- 773
Cdd:pfam00629   75 CLRFWYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISLs 154

                   ....
gi 767960011   774 -ENC 776
Cdd:pfam00629  155 sGPC 158

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011 1483 CTFEKGWCGWQNSQADNFDWVLGVGSHQSLRPPKDHTLGNENGHFMYLEATAvGLRGDKAHFRS-TMWRESSAACtMSFW 1561
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSpLLPPPRSSHC-LSFW 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960011 1562 YFVSAKATGSIQILIKTEKG--LSKVWQESkQNPGNHWQKADILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEFKN 1635
Cdd:cd06263    79 YHMYGSGVGTLNVYVREEGGglGTLLWSAS-GGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSP 154

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011  1269 CDFEFD-LCSWKQEKDEDFDWnlKASSIPAAGTEPAADHTLGNSSGHYIFIKSLFPQqPMRAARISSPVISKRSKNCKII 1347
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDW--ERVSGPSVKTGPSSDHTQGTGSGHFMYVDTSSGA-PGQTARLLSPLLPPSRSPQCLR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011  1348 FHYHMYGNGIGALTL-MQVSVTNQTKVLLNLTVEQGNFWRREELSL-FGDEDFQLKFEGRVGKGQRGDIALDDIVLTE-N 1424
Cdd:pfam00629   78 FWYHMSGSGVGTLRVyVRENGGTLDTLLWSISGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDISLSSgP 157

                   .
gi 767960011  1425 C 1425
Cdd:pfam00629  158 C 158

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011   1052 CSFEKRSLCKWyqpipVHLLQDSNTFRWGLGNgisihhgEENHRPSVDHTQNttDGWYLYADSSNGKFGDTADILTPIIS 1131
Cdd:smart00137    6 CDFEEGSTCGW-----HQDSNDDGHWERVSSA-------TGIPGPNRDHTTG--NGHFMFFETSSGAEGQTARLLSPPLY 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011   1132 LTGPKCTLVFWTHMNGATVGSLQVLIKKDN--VTSKLWAQTGQQGAQWKRAEVFLGIRSHT-QIVFRAKRGISYIGDVAV 1208
Cdd:smart00137   72 ENRSTHCLTFWYYMYGSGSGTLNVYVRENNgsQDTLLWSRSGTQGGQWLQAEVALSSWPQPfQVVFEGTRGKGHSGYIAL 151

                    ....*..
gi 767960011   1209 DDISFQD 1215
Cdd:smart00137  152 DDILLSN 158

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011   1689 GSCNFEtssgnWTTACSLTQDSEDDLDWAIGSRIPAKALiPDSDHTPGSGqHFLYVNSSGSKEGSVARITtSKSFPASLG 1768
Cdd:smart00137    4 GNCDFE-----EGSTCGWHQDSNDDGHWERVSSATGIPG-PNRDHTTGNG-HFMFFETSSGAEGQTARLL-SPPLYENRS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011   1769 MCTVRFWFYMIDPRSmGILKVYTIEESGLNI-LVWSVIGNKRTGWTYGSVPLSSNS-PFKVAFEADLDGNEDIFIALDDI 1846
Cdd:smart00137   76 THCLTFWYYMYGSGS-GTLNVYVRENNGSQDtLLWSRSGTQGGQWLQAEVALSSWPqPFQVVFEGTRGKGHSGYIALDDI 154

                    ....
gi 767960011   1847 SFTP 1850
Cdd:smart00137  155 LLSN 158

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011    616 CDFE-ANSCDWfEAISGDHFDWIRSSQSELSAdfehqAPPRDHSLNasQGHFMFILKKSSSLWQVAKLQSPTFSQTGPGC 694
Cdd:smart00137    6 CDFEeGSTCGW-HQDSNDDGHWERVSSATGIP-----GPNRDHTTG--NGHFMFFETSSGAEGQTARLLSPPLYENRSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011    695 ILSFWFYNYGLSVGAaeLQLHMENSHDS--TVIWRVLYNQGKQWLEATIQLGRLSQPFHLSLDKVSLGIYDGVSAIDDIR 772
Cdd:smart00137   78 CLTFWYYMYGSGSGT--LNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDIL 155

                    ...
gi 767960011    773 FEN 775
Cdd:smart00137  156 LSN 158

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011  290 CGFEFDMCEWTSEASAGqISWMRTKAREIPafESTPQQDQGGDDEGYYVWVGAKHGftlnHLDSRAYLNSSVCH-CLGKS 368
Cdd:cd06263     1 CDFEDGLCGWTQDSTDD-FDWTRVSGSTPS--PGTPPDHTHGTGSGHYLYVESSSG----REGQKARLLSPLLPpPRSSH 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767960011  369 ChLQFYYAMESS---VLRV--RLYNNKEEEIFWTYNISTHSQWVKADVLIPEDLKTFKIIFEGTLLS-QRSFIALD 438
Cdd:cd06263    74 C-LSFWYHMYGSgvgTLNVyvREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSgSRGDIALD 148

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960011    290 CGFEFD-MCEWtSEASAGQISWMRTKAREipaFESTPQQDQGGDDeGYYVWVGA---KHGftlnhldSRAYLNSSVCHCL 365
Cdd:smart00137    6 CDFEEGsTCGW-HQDSNDDGHWERVSSAT---GIPGPNRDHTTGN-GHFMFFETssgAEG-------QTARLLSPPLYEN 73

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960011    366 GKSCHLQFYYAM---ESSVLRVRLYNNKEEEIFWTYNISTH--SQWVKADVLIPEDLKTFKIIFEGTLLS-QRSFIALD 438
Cdd:smart00137   74 RSTHCLTFWYYMygsGSGTLNVYVRENNGSQDTLLWSRSGTqgGQWLQAEVALSSWPQPFQVVFEGTRGKgHSGYIALD 152

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.

                            10        20        30
                    ....*....|....*....|....*....|...
gi 767960011   1225 KCTDHEFMCANKHCIAKDKLCDFVNDCADNSDE 1257
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33

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

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 767960011 1012 CTDNEFICRsDGHCIEKMQKCDFKYDCPDKSDEASC 1047
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35

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

                          10        20        30
                  ....*....|....*....|....*....|...
gi 767960011  454 CSADEFPCTSGQCIAKESVCDSRQDCSDESDED 486
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33

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

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 767960011 1865 CEADQFSCiYTLQCVPLSGKCDGHEDCIDGSDEMDC 1900
Cdd:cd00112     1 CPPNEFRC-ANGRCIPSSWVCDGEDDCGDGSDEENC 35