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 9506563  399 CSFDLGVCDWKQDREDDFDW-----------HPADRD--NDVGYYMAVPALAGHKKNIGRLKLLLPNLtPQSNFCLLFDY 465
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWtrvsgstpspgTPPDHThgTGSGHYLYVESSSGREGQKARLLSPLLPP-PRSSHCLSFWY 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506563  466 RLAGDKVGKLRVFVKNSN---NALAWEETKNEDGRWRTGKIQLYQGIDTTKsVIFEAERGKGKTGEIAVDGVLLVSGLC 541
Cdd:cd06263  80 HMYGSGVGTLNVYVREEGgglGTLLWSASGGQGNQWQEAEVTLSASSKPFQ-VVFEGVRGSGSRGDIALDDISLSPGPC 157

Calcium-binding EGF domain;

                          10        20
                  ....*....|....*....|....*....
gi 9506563    172 DIDECASSKAVCPSNRRCVNTFGSYYCKC 200
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRC 29

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 9506563  399 CSFDLGVCDWKQDREDDFDW-----------HPADRD--NDVGYYMAVPALAGHKKNIGRLKLLLPNLtPQSNFCLLFDY 465
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWtrvsgstpspgTPPDHThgTGSGHYLYVESSSGREGQKARLLSPLLPP-PRSSHCLSFWY 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506563  466 RLAGDKVGKLRVFVKNSN---NALAWEETKNEDGRWRTGKIQLYQGIDTTKsVIFEAERGKGKTGEIAVDGVLLVSGLC 541
Cdd:cd06263  80 HMYGSGVGTLNVYVREEGgglGTLLWSASGGQGNQWQEAEVTLSASSKPFQ-VVFEGVRGSGSRGDIALDDISLSPGPC 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 9506563     399 CSFDLG-VCDWKQDREDDFDWH-----------PADRDNDVGYYMAVPALAGHKKNIGRLklLLPNLTPQ-SNFCLLFDY 465
Cdd:smart00137   6 CDFEEGsTCGWHQDSNDDGHWErvssatgipgpNRDHTTGNGHFMFFETSSGAEGQTARL--LSPPLYENrSTHCLTFWY 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506563     466 RLAGDKVGKLRVFVKNSNNALA---WEETKNEDGRWRTGKI------QLYQgidttksVIFEAERGKGKTGEIAVDGVLL 536
Cdd:smart00137  84 YMYGSGSGTLNVYVRENNGSQDtllWSRSGTQGGQWLQAEValsswpQPFQ-------VVFEGTRGKGHSGYIALDDILL 156

                   ....*
gi 9506563     537 VSGLC 541
Cdd:smart00137 157 SNGPC 161

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 9506563     217 DINECALNtHPCSPHANCLNTRGSFKCKCKQGYRgNGLQC 256
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNC 38

Calcium-binding EGF domain;

                          10        20
                  ....*....|....*....|....*....
gi 9506563    172 DIDECASSKAVCPSNRRCVNTFGSYYCKC 200
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRC 29

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                        10        20        30
                ....*....|....*....|....*....|....*..
gi 9506563  172 DIDECASSkAVCPSNRRCVNTFGSYYCKCHIGFELKY 208
Cdd:cd00054   1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGRN 36

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                        10        20        30
                ....*....|....*....|....*....|....*
gi 9506563   92 DVNECgVKPRPCQH--RCVNTHGSYKCFCLSGHML 124
Cdd:cd00054   1 DIDEC-ASGNPCQNggTCVNTVGSYRCSCPPGYTG 34

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506563  399 CSFDLGVCDWKQDREDDFDW-----------HPADRD--NDVGYYMAVPALAGHKKNIGRLKLLLPNLtPQSNFCLLFDY 465
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWtrvsgstpspgTPPDHThgTGSGHYLYVESSSGREGQKARLLSPLLPP-PRSSHCLSFWY 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506563  466 RLAGDKVGKLRVFVKNSN---NALAWEETKNEDGRWRTGKIQLYQGIDTTKsVIFEAERGKGKTGEIAVDGVLLVSGLC 541
Cdd:cd06263  80 HMYGSGVGTLNVYVREEGgglGTLLWSASGGQGNQWQEAEVTLSASSKPFQ-VVFEGVRGSGSRGDIALDDISLSPGPC 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 9506563     399 CSFDLG-VCDWKQDREDDFDWH-----------PADRDNDVGYYMAVPALAGHKKNIGRLklLLPNLTPQ-SNFCLLFDY 465
Cdd:smart00137   6 CDFEEGsTCGWHQDSNDDGHWErvssatgipgpNRDHTTGNGHFMFFETSSGAEGQTARL--LSPPLYENrSTHCLTFWY 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506563     466 RLAGDKVGKLRVFVKNSNNALA---WEETKNEDGRWRTGKI------QLYQgidttksVIFEAERGKGKTGEIAVDGVLL 536
Cdd:smart00137  84 YMYGSGSGTLNVYVRENNGSQDtllWSRSGTQGGQWLQAEValsswpQPFQ-------VVFEGTRGKGHSGYIALDDILL 156

                   ....*
gi 9506563     537 VSGLC 541
Cdd:smart00137 157 SNGPC 161

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 9506563     217 DINECALNtHPCSPHANCLNTRGSFKCKCKQGYRgNGLQC 256
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNC 38

Calcium-binding EGF domain;

                          10        20
                  ....*....|....*....|....*....
gi 9506563    172 DIDECASSKAVCPSNRRCVNTFGSYYCKC 200
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRC 29

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....
gi 9506563     172 DIDECASsKAVCPSNRRCVNTFGSYYCKCHIGFE 205
Cdd:smart00179   1 DIDECAS-GNPCQNGGTCVNTVGSYRCECPPGYT 33

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.

                        10        20        30
                ....*....|....*....|....*....|....
gi 9506563  220 ECALNtHPCSPHANCLNTRGSFKCKCKQGYRGNG 253
Cdd:cd00053   1 ECAAS-NPCSNGGTCVNTPGSYRCVCPPGYTGDR 33

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                        10        20        30
                ....*....|....*....|....*....|....*
gi 9506563   92 DVNECgVKPRPCQH--RCVNTHGSYKCFCLSGHML 124
Cdd:cd00054   1 DIDEC-ASGNPCQNggTCVNTVGSYRCSCPPGYTG 34

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 9506563     96 CGVKPRPCQHRCVNTHGSYKCFCLSGHMLLPDatcsnSRTC 136
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDD-----GRTC 36