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 565671710  865 CNFETGICNWEQDAKDDFDWTRSQGPTPTLNTGPmkDNTLGTAKGHYLYIESSEPQaFQDSAALLSPILNATDTKGCtFR 944
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGR-EGQKARLLSPLLPPPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565671710  945 FYYHMFGKRIYRLAIYQRIWSDSRGQLLWQIFGNQGNRWIRKHLNISS-RQPFQILVEASVGDGFTGDIAIDDLSFMD 1021
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 565671710 1090 CSFEKrSLCKWYQpipvhllQDSNTFRWGLGNGISIHHGeenhrPSVDHTQNTTDGWYLYADSSNGKFGDTADILTPIIS 1169
Cdd:cd06263     1 CDFED-GLCGWTQ-------DSTDDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565671710 1170 LT-GPKCtLVFWTHMNGATVGSLQVLIKKDN--VTSKLWAQTGQQGAQWKRAEVFLG-IRSHTQIVFRAKRGISYIGDVA 1245
Cdd:cd06263    68 PPrSSHC-LSFWYHMYGSGVGTLNVYVREEGggLGTLLWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIA 146

                  ....*...
gi 565671710 1246 VDDISFQD 1253
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 565671710  654 CDFEANSCDWfEAISGDHFDWIRSSQSELSADfehqaPPRDHSLNASQGHFMFILKKSSSLWQVAKLQSPTFSQT-GPGC 732
Cdd:cd06263     1 CDFEDGLCGW-TQDSTDDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565671710  733 iLSFWFYNYGLSVGAAELQLHMENSHDSTVIWRVLYNQGKQWLEATIQLGRLSQPFHLSLDKVSLGIYDGVSAIDDIRFE 812
Cdd:cd06263    75 -LSFWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLS 153

                  .
gi 565671710  813 N 813
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 565671710   73 CDFEDGLCHMTQDQSLQPSWTKRSGMIGLS-PPFYDHNGDVSAHFLSLVSRVDSISSS--LRSRVFLPTNDQHdCqITFY 149
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPgTPPDHTHGTGSGHYLYVESSSGREGQKarLLSPLLPPPRSSH-C-LSFW 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565671710  150 YF-SCQVSGKLMVGLQTACGGPIQHLWQNTAALPNQWERNVIKIQS-SQRFQVVFEGQMASTYEQDevIAIDDISFSSG 226
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 565671710  270 CGFEFDMCEWTSEASAGqISWMRTKAREIPafESTPQQDQGGDDEGYYVWVGAKHGftlnHLDSRAYLNSSVCH-CLGKS 348
Cdd:cd06263     1 CDFEDGLCGWTQDSTDD-FDWTRVSGSTPS--PGTPPDHTHGTGSGHYLYVESSSG----REGQKARLLSPLLPpPRSSH 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565671710  349 ChLQFYYAMESS---VLRV--RLYNNKEEEIFWTYNISTHSQWVKADVLIPEDLKTFKIIFEGTLLS-QRSFIALD 418
Cdd:cd06263    74 C-LSFWYHMYGSgvgTLNVyvREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSgSRGDIALD 148

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 565671710 1050 CTDNEFICRsDGHCIEKMQKCDFKYDCPDKSDEASC 1085
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 565671710 1684 CPEiTDFLCRDKKCIASHLLCDYKPDCSDRSDEAHC 1719
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 565671710 1947 CSNMEFPCSTDECIPSLLLCDGVPDCHFNEDELIC 1981
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 565671710   38 FQCDNGVSLPPDSICDFTDQCGDSSDERHC 67
Cdd:cd00112     6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 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 565671710  827 DHFWCRHTRaCIEKLRLCDLVDDCGDRTDEVNC 859
Cdd:cd00112     4 NEFRCANGR-CIPSSWVCDGEDDCGDGSDEENC 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 565671710  865 CNFETGICNWEQDAKDDFDWTRSQGPTPTLNTGPmkDNTLGTAKGHYLYIESSEPQaFQDSAALLSPILNATDTKGCtFR 944
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGR-EGQKARLLSPLLPPPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565671710  945 FYYHMFGKRIYRLAIYQRIWSDSRGQLLWQIFGNQGNRWIRKHLNISS-RQPFQILVEASVGDGFTGDIAIDDLSFMD 1021
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 565671710 1307 CDFEFDLCSWKQEKDEDFDWNLKASSIPAAGTEPaaDHTLGNSSGHYIFIKSLFPqQPMRAARISSPVIS-KRSKNCkII 1385
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSG-REGQKARLLSPLLPpPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565671710 1386 FHYHMYGNGIGALTLMQVSVTNQTKVLL-NLTVEQGNFWRREELSLFG-DEDFQLKFEGRVGKGQRGDIALDDIVLTE 1461
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 565671710    860 APELQCNFETG-ICNWEQDAKDDFDWTRSQGPTPtlNTGPMKDNTLGTakGHYLYIESSEPQAFQdSAALLSPILNATDT 938
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSSGAEGQ-TARLLSPPLYENRS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565671710    939 KGCtFRFYYHMFGKRIYRLAIYQRIWSDSRGQLLWQIFGNQGNRWIRKHLNISS-RQPFQILVEASVGDGFTGDIAIDDL 1017
Cdd:smart00137   76 THC-LTFWYYMYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTRGKGHSGYIALDDI 154

                    ....
gi 565671710   1018 SFMD 1021
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 565671710  654 CDFEANSCDWfEAISGDHFDWIRSSQSELSADfehqaPPRDHSLNASQGHFMFILKKSSSLWQVAKLQSPTFSQT-GPGC 732
Cdd:cd06263     1 CDFEDGLCGW-TQDSTDDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565671710  733 iLSFWFYNYGLSVGAAELQLHMENSHDSTVIWRVLYNQGKQWLEATIQLGRLSQPFHLSLDKVSLGIYDGVSAIDDIRFE 812
Cdd:cd06263    75 -LSFWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLS 153

                  .
gi 565671710  813 N 813
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 565671710   654 CDFE-ANSCDWFEAISgDHFDWIRSSqselsADFEHQAPPRDHSLNASQGHFMFILKKSSSLWQVAKLQSPTFSQTGPGC 732
Cdd:pfam00629    1 CDFEdGNLCGWTQDSS-DDFDWERVS-----GPSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565671710   733 ILSFWFYNYGLSVGAAELQLHMENSHDSTVIWRVLYNQGKQWLEATIQLGRLSQPFHLSLDKVSLGIYDGVSAIDDIRF- 811
Cdd:pfam00629   75 CLRFWYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISLs 154

                   ....
gi 565671710   812 -ENC 814
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 565671710 1521 CTFEKGWCGWQNSQADNFDWVLGVGSHQSLRPPKDHTLGNENGHFMYLEATAvGLRGDKAHFRS-TMWRESSAACtMSFW 1599
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSpLLPPPRSSHC-LSFW 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565671710 1600 YFVSAKATGSIQILIKTEKG--LSKVWQESkQNPGNHWQKADILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEFKN 1673
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 565671710  1307 CDFEFD-LCSWKQEKDEDFDWnlKASSIPAAGTEPAADHTLGNSSGHYIFIKSLFPQqPMRAARISSPVISKRSKNCKII 1385
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDW--ERVSGPSVKTGPSSDHTQGTGSGHFMYVDTSSGA-PGQTARLLSPLLPPSRSPQCLR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565671710  1386 FHYHMYGNGIGALTL-MQVSVTNQTKVLLNLTVEQGNFWRREELSL-FGDEDFQLKFEGRVGKGQRGDIALDDIVLTE-N 1462
Cdd:pfam00629   78 FWYHMSGSGVGTLRVyVRENGGTLDTLLWSISGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDISLSSgP 157

                   .
gi 565671710  1463 C 1463
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 565671710   1090 CSFEKRSLCKWyqpipVHLLQDSNTFRWGLGNgisihhgEENHRPSVDHTQNttDGWYLYADSSNGKFGDTADILTPIIS 1169
Cdd:smart00137    6 CDFEEGSTCGW-----HQDSNDDGHWERVSSA-------TGIPGPNRDHTTG--NGHFMFFETSSGAEGQTARLLSPPLY 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565671710   1170 LTGPKCTLVFWTHMNGATVGSLQVLIKKDN--VTSKLWAQTGQQGAQWKRAEVFLGIRSHT-QIVFRAKRGISYIGDVAV 1246
Cdd:smart00137   72 ENRSTHCLTFWYYMYGSGSGTLNVYVRENNgsQDTLLWSRSGTQGGQWLQAEVALSSWPQPfQVVFEGTRGKGHSGYIAL 151

                    ....*..
gi 565671710   1247 DDISFQD 1253
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 565671710   1727 GSCNFEtssgnWTTACSLTQDSEDDLDWAIGSRIPAKALiPDSDHTPGSGqHFLYVNSSGSKEGSVARITtSKSFPASLG 1806
Cdd:smart00137    4 GNCDFE-----EGSTCGWHQDSNDDGHWERVSSATGIPG-PNRDHTTGNG-HFMFFETSSGAEGQTARLL-SPPLYENRS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565671710   1807 MCTVRFWFYMIDPRSmGILKVYTIEESGLNI-LVWSVIGNKRTGWTYGSVPLSSNS-PFKVAFEADLDGNEDIFIALDDI 1884
Cdd:smart00137   76 THCLTFWYYMYGSGS-GTLNVYVRENNGSQDtLLWSRSGTQGGQWLQAEVALSSWPqPFQVVFEGTRGKGHSGYIALDDI 154

                    ....
gi 565671710   1885 SFTP 1888
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 565671710    654 CDFE-ANSCDWfEAISGDHFDWIRSSQSELSAdfehqAPPRDHSLNasQGHFMFILKKSSSLWQVAKLQSPTFSQTGPGC 732
Cdd:smart00137    6 CDFEeGSTCGW-HQDSNDDGHWERVSSATGIP-----GPNRDHTTG--NGHFMFFETSSGAEGQTARLLSPPLYENRSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565671710    733 ILSFWFYNYGLSVGAaeLQLHMENSHDS--TVIWRVLYNQGKQWLEATIQLGRLSQPFHLSLDKVSLGIYDGVSAIDDIR 810
Cdd:smart00137   78 CLTFWYYMYGSGSGT--LNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDIL 155

                    ...
gi 565671710    811 FEN 813
Cdd:smart00137  156 LSN 158

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 565671710   476 CDFESG-FCGWEPFLTEDSHWKLMKGLNngEHHFPAADHTANINHGSFIYLEAQRSPG--VAKLGSPVLTklLTASTPCq 552
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPS--VKTGPSSDHTQGTGSGHFMYVDTSSGAPgqTARLLSPLLP--PSRSPQC- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565671710   553 VQFWYHLSQHS--NLSVFTRTSLDGNLQKQGKIIRFSESQWSHAKIDLiaeaGESTLPFQLILEATVLSSNA-TVALDDI 629
Cdd:pfam00629   76 LRFWYHMSGSGvgTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTL----SSSTQPFQVVFEGIRGGGSRgGIALDDI 151

                   ....*
gi 565671710   630 SVSQE 634
Cdd:pfam00629  152 SLSSG 156

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 565671710    474 LTCDFESG-FCGWEPFLTEDSHWKLMKGLNNGEHhfPAADHTanINHGSFIYLEAQ-RSPG-VAKLGSPVLTklLTASTP 550
Cdd:smart00137    4 GNCDFEEGsTCGWHQDSNDDGHWERVSSATGIPG--PNRDHT--TGNGHFMFFETSsGAEGqTARLLSPPLY--ENRSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565671710    551 CqVQFWYHL--SQHSNLSVFTRtslDGNLQKQGKIIRFSE---SQWSHAKIDLIAEAGestlPFQLILEATVLSSNA-TV 624
Cdd:smart00137   78 C-LTFWYYMygSGSGTLNVYVR---ENNGSQDTLLWSRSGtqgGQWLQAEVALSSWPQ----PFQVVFEGTRGKGHSgYI 149

                    ....*...
gi 565671710    625 ALDDISVS 632
Cdd:smart00137  150 ALDDILLS 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 565671710     73 CDFEDG-LCHMTQDQSLQPSWTKRSGMIGLSPPFYDH-NGDVSAHFLSLVSRVDSISSSLRSRVFLPTNDQHdCqITFYY 150
Cdd:smart00137    6 CDFEEGsTCGWHQDSNDDGHWERVSSATGIPGPNRDHtTGNGHFMFFETSSGAEGQTARLLSPPLYENRSTH-C-LTFWY 83

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565671710    151 F-SCQVSGKLMVGLQTACGGPIQHLWQNTAALPNQWERNVIKIQSSQR-FQVVFEGQMASTYEQDevIAIDDISFSSG 226
Cdd:smart00137   84 YmYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQpFQVVFEGTRGKGHSGY--IALDDILLSNG 159