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 75709198 422 CNFDHGLCGWIREKDNDLHWEPIR--------------DPAGGQYLTVSAAKAPGGKAARLVLPLGRLMhSGDLCLSFRH 487
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWTRVSgstpspgtppdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPP-RSSHCLSFWY 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75709198 488 KVTGLHSGTLQVFVRKHGA-HGAALWGRNG--GHGWRQTQITL-RGADIKSVVFKGEKRRGHTGEIGLDDVSLKKGHC 561
Cdd:cd06263  80 HMYGSGVGTLNVYVREEGGgLGTLLWSASGgqGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157

Calcium-binding EGF domain;

                          10        20
                  ....*....|....*....|....*....
gi 75709198   169 DVDECATGRASCPRFRQCVNTFGSYICKC 197
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRC 29

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.

                          10        20
                  ....*....|....*....|...
gi 75709198   150 RCQCPsPGLQLAPDGRTCVDVDE 172
Cdd:pfam12662   1 TCSCP-PGYQLDPDGRTCVDIDE 22

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 75709198 422 CNFDHGLCGWIREKDNDLHWEPIR--------------DPAGGQYLTVSAAKAPGGKAARLVLPLGRLMhSGDLCLSFRH 487
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWTRVSgstpspgtppdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPP-RSSHCLSFWY 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75709198 488 KVTGLHSGTLQVFVRKHGA-HGAALWGRNG--GHGWRQTQITL-RGADIKSVVFKGEKRRGHTGEIGLDDVSLKKGHC 561
Cdd:cd06263  80 HMYGSGVGTLNVYVREEGGgLGTLLWSASGgqGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 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 75709198    420 HSCNF-DHGLCGWIREKDNDLHWE----------PIRDPAGGQ--YLTVSAAKAPGGKAARLVLPLGRLMHSGDlCLSFR 486
Cdd:smart00137   4 GNCDFeEGSTCGWHQDSNDDGHWErvssatgipgPNRDHTTGNghFMFFETSSGAEGQTARLLSPPLYENRSTH-CLTFW 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75709198    487 HKVTGLHSGTLQVFVR-KHGAHGAALWGRNG--GHGWRQTQITLRGADIK-SVVFKGEKRRGHTGEIGLDDVSLKKGHC 561
Cdd:smart00137  83 YYMYGSGSGTLNVYVReNNGSQDTLLWSRSGtqGGQWLQAEVALSSWPQPfQVVFEGTRGKGHSGYIALDDILLSNGPC 161

Calcium-binding EGF domain;

                          10        20
                  ....*....|....*....|....*....
gi 75709198   169 DVDECATGRASCPRFRQCVNTFGSYICKC 197
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 75709198 214 DIDECSLGQyQCSSFARCYNIRGSYKCKCKEGYQGD 249
Cdd:cd00054   1 DIDECASGN-PCQNGGTCVNTVGSYRCSCPPGYTGR 35

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|...
gi 75709198    169 DVDECATGrASCPRFRQCVNTFGSYICKCHKGF 201
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGY 32

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.

                          10        20
                  ....*....|....*....|...
gi 75709198   150 RCQCPsPGLQLAPDGRTCVDVDE 172
Cdd:pfam12662   1 TCSCP-PGYQLDPDGRTCVDIDE 22

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....
gi 75709198     89 DLNECgLKPRPCKH--RCMNTYGSYKCYCLNGYM 120
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGYT 33

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 75709198 422 CNFDHGLCGWIREKDNDLHWEPIR--------------DPAGGQYLTVSAAKAPGGKAARLVLPLGRLMhSGDLCLSFRH 487
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWTRVSgstpspgtppdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPP-RSSHCLSFWY 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75709198 488 KVTGLHSGTLQVFVRKHGA-HGAALWGRNG--GHGWRQTQITL-RGADIKSVVFKGEKRRGHTGEIGLDDVSLKKGHC 561
Cdd:cd06263  80 HMYGSGVGTLNVYVREEGGgLGTLLWSASGgqGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 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 75709198    420 HSCNF-DHGLCGWIREKDNDLHWE----------PIRDPAGGQ--YLTVSAAKAPGGKAARLVLPLGRLMHSGDlCLSFR 486
Cdd:smart00137   4 GNCDFeEGSTCGWHQDSNDDGHWErvssatgipgPNRDHTTGNghFMFFETSSGAEGQTARLLSPPLYENRSTH-CLTFW 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75709198    487 HKVTGLHSGTLQVFVR-KHGAHGAALWGRNG--GHGWRQTQITLRGADIK-SVVFKGEKRRGHTGEIGLDDVSLKKGHC 561
Cdd:smart00137  83 YYMYGSGSGTLNVYVReNNGSQDTLLWSRSGtqGGQWLQAEVALSSWPQPfQVVFEGTRGKGHSGYIALDDILLSNGPC 161

Calcium-binding EGF domain;

                          10        20
                  ....*....|....*....|....*....
gi 75709198   169 DVDECATGRASCPRFRQCVNTFGSYICKC 197
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 75709198 214 DIDECSLGQyQCSSFARCYNIRGSYKCKCKEGYQGD 249
Cdd:cd00054   1 DIDECASGN-PCQNGGTCVNTVGSYRCSCPPGYTGR 35

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 75709198   214 DIDECSLGQYQCSSFARCYNIRGSYKCKCKEG 245
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32

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
                  ....*....|....*....|....*....|....*.
gi 75709198    93 CGLKPRPCKHRCMNTYGSYKCYCLNGYMLMPDG-SC 127
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGrTC 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 75709198 169 DVDECATGrASCPRFRQCVNTFGSYICKCHKGF 201
Cdd:cd00054   1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGY 32

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 75709198  89 DLNECgLKPRPCKH--RCMNTYGSYKCYCLNGYML 121
Cdd:cd00054   1 DIDEC-ASGNPCQNggTCVNTVGSYRCSCPPGYTG 34