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 1799935035  816 CNFENGLCNWEQDVEDDFDWIRIQGPTPTVNTGPlkDHTTGTARGHYLYLESSePRQFQDKAVLLSPLFNPSGNGTCvFR 895
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESS-SGREGQKARLLSPLLPPPRSSHC-LS 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799935035  896 FHYHMFGKEVYKLSVFQRTVNNTKGWLLWYKFGNQENRWIRQTLFISS-SKPFQILMKGTVGDGFTGDIGLDDVSFL 971
Cdd:cd06263     77 FWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGDIALDDISLS 153

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 1799935035 1041 CDFEDkGLCGWHQPAleqmsrnysihiTNTFKWQLGRGAnlypeQEQHCPLTDHTTCTEEGWYIFADSSNGEFGHTADIA 1120
Cdd:cd06263      1 CDFED-GLCGWTQDS------------TDDFDWTRVSGS-----TPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLL 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935035 1121 TPVISLT-GPRCkIIFWNHMNGSTVGSLEVLCKSSN--KTSKLWTQSGSQGPQWNRAEVFLGIRSN-FQVIFRAKRGVSY 1196
Cdd:cd06263     63 SPLLPPPrSSHC-LSFWYHMYGSGVGTLNVYVREEGggLGTLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGS 141

                          170
                   ....*....|.
gi 1799935035 1197 MGDVAVDDITF 1207
Cdd:cd06263    142 RGDIALDDISL 152

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 1799935035 1686 CNFEIQDqewttvCGLIQDTTDDFDWSISNSAAQTS-PHTDHTPGKGQ-SFLYVNSSAQKEGDSARITTSKFFPASLGVC 1763
Cdd:cd06263      1 CDFEDGL------CGWTQDSTDDFDWTRVSGSTPSPgTPPDHTHGTGSgHYLYVESSSGREGQKARLLSPLLPPPRSSHC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935035 1764 rVRFWFWMFaSRQTGVLKVYTVEE-HGMDILMWSSSRNEENKWMYGSVVLSSNS-PFRVAFEAEVGWSQPTEFALDDISF 1841
Cdd:cd06263     75 -LSFWYHMY-GSGVGTLNVYVREEgGGLGTLLWSASGGQGNQWQEAEVTLSASSkPFQVVFEGVRGSGSRGDIALDDISL 152

                   ....*
gi 1799935035 1842 TP-EC 1845
Cdd:cd06263    153 SPgPC 157

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 1799935035   61 CDFETNLCKALPEFNLHPVWTRRNGQSGMGPPYSDHS-GNESAYFL--SLSSEMQSSSATLRTNVFLPTDEEHiCqIRFH 137
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHThGTGSGHYLyvESSSGREGQKARLLSPLLPPPRSSH-C-LSFW 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799935035  138 YWVSQMS-GALMVGLQKHSEDTITNIWQVSGELRNQWNVNNITINST-EKYQVIFWGMVETQTKGEtVAIDDITFSEG 213
Cdd:cd06263     79 YHMYGSGvGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASsKPFQVVFEGVRGSGSRGD-IALDDISLSPG 155

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 1799935035 1220 CTSEEFICANKYCIPKNNLCDFVNDCADNSDE 1251
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDE 32

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 1799935035 1641 CPAlTDFVCGNGNCIESQFICDYKPDCEDLSDEADC 1676
Cdd:cd00112      1 CPP-NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 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 1799935035 1906 CKETEFLCPSQGCVPSLLRCDGVPDCHLSEDEVGC 1940
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 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 1799935035 1441 CSHGHRQCQNGKCYRPEQSCDFEDNCGDNTDESKC 1475
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 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 1799935035 1945 CSNGSLLCAStNQCIAFSQRCDGIVDCIDSSlDESGC 1981
Cdd:cd00112      1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGS-DEENC 35

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935035  816 CNFENGLCNWEQDVEDDFDWIRIQGPTPTVNTGPlkDHTTGTARGHYLYLESSePRQFQDKAVLLSPLFNPSGNGTCvFR 895
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESS-SGREGQKARLLSPLLPPPRSSHC-LS 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799935035  896 FHYHMFGKEVYKLSVFQRTVNNTKGWLLWYKFGNQENRWIRQTLFISS-SKPFQILMKGTVGDGFTGDIGLDDVSFL 971
Cdd:cd06263     77 FWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGDIALDDISLS 153

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 1799935035  816 CNFENG-LCNWEQDVEDDFDWIRIQGPTPtvNTGPLKDHTTGTARGHYLYLESSEPrQFQDKAVLLSPLFNPSGNGTCvF 894
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTQGTGSGHFMYVDTSSG-APGQTARLLSPLLPPSRSPQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935035  895 RFHYHMFGKEVYKLSVFQRTVNNTKGWLLWYKFGNQENRWIRQTLFISS-SKPFQILMKGTVGDGFTGDIGLDDVSFLGC 973
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156

                   .
gi 1799935035  974 T 974
Cdd:pfam00629  157 P 157

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 1799935035   811 NPDLQCNFE-NGLCNWEQDVEDDFDWIRIQGPTPtvNTGPLKDHTTGTarGHYLYLESSEPRQFQdKAVLLSPLFNPSgN 889
Cdd:smart00137    1 TSPGNCDFEeGSTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSSGAEGQ-TARLLSPPLYEN-R 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935035   890 GTCVFRFHYHMFGKEVYKLSVFQRTVNNTKGWLLWYKFGNQENRWIRQTLFISSS-KPFQILMKGTVGDGFTGDIGLDDV 968
Cdd:smart00137   75 STHCLTFWYYMYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGKGHSGYIALDDI 154

                    ...
gi 1799935035   969 SFL 971
Cdd:smart00137  155 LLS 157

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 1799935035  605 CDFERES-CGWIETvNADEFDWVRSSSSAlppafQKQAPPWDHTYNKPEGHFMFILKNSSSISQIARLRSPKFRQTGSNC 683
Cdd:pfam00629    1 CDFEDGNlCGWTQD-SSDDFDWERVSGPS-----VKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935035  684 TLSFWYYNYGQSVGAAELQLIVDGLKQPTVLWRTYYNEGNQWLKAVIQLGRLPHPFQFSLDKISLGFYEGVSAIDDIRF- 762
Cdd:pfam00629   75 CLRFWYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISLs 154

                   ....*
gi 1799935035  763 -ENCA 766
Cdd:pfam00629  155 sGPCP 159

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 1799935035  1258 TSIGHCNFEFE-LCGWKQDEDDDFDWHlRTSSTTKlGTGPATDHTLqePSGHYIFIKSSFFQlPGQKARISSPVLSRRNK 1336
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWE-RVSSATG-IPGPNRDHTT--GNGHFMFFETSSGA-EGQTARLLSPPLYENRS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935035  1337 NCKIIFYYHMYGADIGSLIIYQRtTLKHE--KILLNLTGNQGNFWQRKALTLSGDgDEDFQVVFEGIAGKGPKDGIALDD 1414
Cdd:smart00137   76 THCLTFWYYMYGSGSGTLNVYVR-ENNGSqdTLLWSRSGTQGGQWLQAEVALSSW-PQPFQVVFEGTRGKGHSGYIALDD 153

                    ....
gi 1799935035  1415 LTFS 1418
Cdd:smart00137  154 ILLS 157

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 1799935035  605 CDFERESCGWIEtVNADEFDWVRSSSSALPPAfqkqaPPWDHTYNKPEGHFMFILKNSSSISQIARLRSPKFRQT-GSNC 683
Cdd:cd06263      1 CDFEDGLCGWTQ-DSTDDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935035  684 tLSFWYYNYGQSVGAAELQLIVDGLKQPTVLWRTYYNEGNQWLKAVIQLGRLPHPFQFSLDKISLGFYEGVSAIDDIRFE 763
Cdd:cd06263     75 -LSFWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLS 153

                   .
gi 1799935035  764 N 764
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 1799935035 1479 CTFENGKCGWQNSLADNFNWVLGVGSPQSLRPPGDHTLGNRTGHFLYLEATAtGLINEKAHVKSSIWKESSRTCVMSFWY 1558
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPRSSHCLSFWY 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799935035 1559 FKLSKAMGHIQVLIKTDDGIV--KIWSESGNHGDKWNNVKLHLGKLRN-FEIIFEGIRTRDLGGGAAIDDIEFNN 1630
Cdd:cd06263     80 HMYGSGVGTLNVYVREEGGGLgtLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSP 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 1799935035 1479 CTFENGK-CGWQNSLADNFNWVLGVGSPQSLRPPGDHTLGNRTGHFLYLEATAtGLINEKAHVKSSIWKESSRTCVMSFW 1557
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPSVKTGPSSDHTQGTGSGHFMYVDTSS-GAPGQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935035 1558 YFKLSKAMGHIQVLIKTDDGIV--KIWSESGNHGDKWNNVKLHLGKLRN-FEIIFEGIRTRDLGGGAAIDDIEFN--NCS 1632
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQpFQVVFEGIRGGGSRGGIALDDISLSsgPCP 159

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 1799935035  1478 SCTFENGK-CGWQNSLADNFNWVLGVGSPQSLRPPGDHTLGNrtGHFLYLEATAtGLINEKAHVKSSIWKESSRTCVMSF 1556
Cdd:smart00137    5 NCDFEEGStCGWHQDSNDDGHWERVSSATGIPGPNRDHTTGN--GHFMFFETSS-GAEGQTARLLSPPLYENRSTHCLTF 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799935035  1557 WYFKLSKAMGHIQVLIKTDDGIV--KIWSESGNHGDKWNNVKLHLGKLRN-FEIIFEGIRTRDLGGGAAIDDIEFNN 1630
Cdd:smart00137   82 WYYMYGSGSGTLNVYVRENNGSQdtLLWSRSGTQGGQWLQAEVALSSWPQpFQVVFEGTRGKGHSGYIALDDILLSN 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 1799935035   61 CDFETNLCKALPEFNLHPVWTRRNGQSGMGPPYSDHS-GNESAYFL--SLSSEMQSSSATLRTNVFLPTDEEHiCqIRFH 137
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHThGTGSGHYLyvESSSGREGQKARLLSPLLPPPRSSH-C-LSFW 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799935035  138 YWVSQMS-GALMVGLQKHSEDTITNIWQVSGELRNQWNVNNITINST-EKYQVIFWGMVETQTKGEtVAIDDITFSEG 213
Cdd:cd06263     79 YHMYGSGvGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASsKPFQVVFEGVRGSGSRGD-IALDDISLSPG 155

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 1799935035  425 CDFETDLCGWKPLSKGDADWNIKKEQAPLDrkLPGRGHTNNMGHGTFIYFSGSHQMNTKTAmcHLESPfLVKLSPGLTCc 504
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSP--GTPPDHTHGTGSGHYLYVESSSGREGQKA--RLLSP-LLPPPRSSHC- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935035  505 qVRFWYWLSQDS--QLSVFRRTALNGSLEKLRDISGLPEMNWTKVNIPVESAAEelPFQIVLQGTVLTTHAA-VAIDDIG 581
Cdd:cd06263     75 -LSFWYHMYGSGvgTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK--PFQVVFEGVRGSGSRGdIALDDIS 151

                   ....*.
gi 1799935035  582 ISE-EC 586
Cdd:cd06263    152 LSPgPC 157

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 1799935035    59 DKCDFETN-LC--KALPEFNLHpvWTRRNGQSGMGPPYSDHSGNESAY-FLSLSSEMQSSSATLRTNVFLPTDEEHiCqI 134
Cdd:smart00137    4 GNCDFEEGsTCgwHQDSNDDGH--WERVSSATGIPGPNRDHTTGNGHFmFFETSSGAEGQTARLLSPPLYENRSTH-C-L 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799935035   135 RFHYwvsQMSG----ALMVGLQKHSEDTITNIWQVSGELRNQWNVNNITINS-TEKYQVIFWGMVETQTKGEtVAIDDIT 209
Cdd:smart00137   80 TFWY---YMYGsgsgTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTRGKGHSGY-IALDDIL 155

                    ....
gi 1799935035   210 FSEG 213
Cdd:smart00137  156 LSNG 159

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 1799935035  1220 CTSEEFICANKYCIPKNNLCDFVNDCADNSDE 1251
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 1799935035 1641 CPAlTDFVCGNGNCIESQFICDYKPDCEDLSDEADC 1676
Cdd:cd00112      1 CPP-NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 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 1799935035 1906 CKETEFLCPSQGCVPSLLRCDGVPDCHLSEDEVGC 1940
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

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 1799935035  1001 CTEKEFVCrASGHCIQMIQKCDFRPDCSDKSDE 1033
Cdd:smart00192    2 CPPGEFQC-DNGRCIPSSWVCDGVDDCGDGSDE 33