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 2462518933 1327 CDFEFDLCSWKQEKDEDFDWNLKASSIPAAGTEPaaDHTLGNSSGHYIFINSLFPqQPMRAARISSPVIS-KRSKNCkII 1405
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSG-REGQKARLLSPLLPpPRSSHC-LS 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462518933 1406 FHYHMYGNGIGALTLMQVSVTNQTKVLL-NLTAEQGNFWRREELSLFG-DEDFQLKFEGRVGKGQRGDIALDDIVLTE 1481
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 2462518933 1749 CNFETSsgnwttACSLTQDSEDDLDWAIGSRIPAKALIPDSDHTPGSGQHFLYVNSSGSKEGSVARITTSKSFPASLGMC 1828
Cdd:cd06263      1 CDFEDG------LCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518933 1829 tVRFWFYMIDpRSMGILKVYTIEESG-LNILVWSVIGNKRTGWTYGSVPLSSNS-PFKVAFEADLDGNEDIFIALDDISF 1906
Cdd:cd06263     75 -LSFWYHMYG-SGVGTLNVYVREEGGgLGTLLWSASGGQGNQWQEAEVTLSASSkPFQVVFEGVRGSGSRGDIALDDISL 152

                   ....*
gi 2462518933 1907 TP-EC 1910
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 2462518933 1541 CTFEKGWCGWQNSQADNFDWVLGVGSHQSLRPPKDHTLGNENGHFMYLEATAvGLRGDKAHFRS-TMWRESSAACtMSFW 1619
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSpLLPPPRSSHC-LSFW 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462518933 1620 YFISAKATGSIQILIKTEKG--LSKVWQESkQNPGNHWQKADILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEFKN 1693
Cdd:cd06263     79 YHMYGSGVGTLNVYVREEGGglGTLLWSAS-GGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSP 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 2462518933  496 CDFESGFCGWEPFLTEDSHWKLMKGLNNgeHHFPAADHTANINHGSFIYLEA-QRSPG-VAKLGSPVLTklLTASTPCqV 573
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESsSGREGqKARLLSPLLP--PPRSSHC-L 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518933  574 QFWYHLS--QHSNLSVFTRTSLDGNLQKQGKIIRFSESQWSHAKIDLiaeaGESTLPFQLILEATVLSSNA-TVALDDIS 650
Cdd:cd06263     76 SFWYHMYgsGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTL----SASSKPFQVVFEGVRGSGSRgDIALDDIS 151

                   ..
gi 2462518933  651 VS 652
Cdd:cd06263    152 LS 153

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 2462518933  1283 KCTAHEFMCANKHCVAKDKLCDFVNDCADNSDE 1315
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.

                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462518933   454 CSADEFPCTSGQCIAKESVCDSRQDCSDESDE 485
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2462518933 1923 CEADQFSCiYTLQCVPLSGKCDGHEDCIDGSDEMDC 1958
Cdd:cd00112      1 CPPNEFRC-ANGRCIPSSWVCDGEDDCGDGSDEENC 35

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462518933 1503 CPLGYRECHNGKCYRLEQSCNFVDNCGDNTDENEC 1537
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 2462518933  847 DHFWCRHTRaCIEKLRLCDLVDDCGDRTDEVNC 879
Cdd:cd00112      4 NEFRCANGR-CIPSSWVCDGEDDCGDGSDEENC 35

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 2462518933  885 CNFETG-ICNWEQDAKDDFDWTRSQGPTPtlNTGPMKDNTLGTAKGHYLYIESSEPQAFQdSAALLSPILNATDTKGCtF 963
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTQGTGSGHFMYVDTSSGAPGQ-TARLLSPLLPPSRSPQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518933  964 RFYYHMFGKRIYRLAIYQRIWSDSRGQLLWQIFGNQGNRWIRKHLNISSR-QPFQILVEASVGDGFTGDIAIDDLSFM-- 1040
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSStQPFQVVFEGIRGGGSRGGIALDDISLSsg 156

                   ..
gi 2462518933 1041 DC 1042
Cdd:pfam00629  157 PC 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 2462518933 1110 CSFEKrSLCKWYQpipvhllQDSNTFRWGLGNGISIHHGeenhrPSVDHTQNTTDGWYLYADSSNGKFGDTADILTPIIS 1189
Cdd:cd06263      1 CDFED-GLCGWTQ-------DSTDDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLP 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518933 1190 LT-GPKCtLVFWTHMNGATVGSLQVLIKKDN--VTSKLWAQTGQQGAQWKRAEVFLG-IRSHTQIVFRAKRGISYIGDVA 1265
Cdd:cd06263     68 PPrSSHC-LSFWYHMYGSGVGTLNVYVREEGggLGTLLWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIA 146

                   ....*...
gi 2462518933 1266 VDDISFQD 1273
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 2462518933 1749 CNFETSsgnwttACSLTQDSEDDLDWAIGSRIPAKALIPDSDHTPGSGQHFLYVNSSGSKEGSVARITTSKSFPASLGMC 1828
Cdd:cd06263      1 CDFEDG------LCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518933 1829 tVRFWFYMIDpRSMGILKVYTIEESG-LNILVWSVIGNKRTGWTYGSVPLSSNS-PFKVAFEADLDGNEDIFIALDDISF 1906
Cdd:cd06263     75 -LSFWYHMYG-SGVGTLNVYVREEGGgLGTLLWSASGGQGNQWQEAEVTLSASSkPFQVVFEGVRGSGSRGDIALDDISL 152

                   ....*
gi 2462518933 1907 TP-EC 1910
Cdd:cd06263    153 SPgPC 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 2462518933 1749 CNFETSSgnwttACSLTQDSEDDLDWAIGSRIPAKAlIPDSDHTPGSGQ-HFLYVNSSGSKEGSVARITtSKSFPASLGM 1827
Cdd:pfam00629    1 CDFEDGN-----LCGWTQDSSDDFDWERVSGPSVKT-GPSSDHTQGTGSgHFMYVDTSSGAPGQTARLL-SPLLPPSRSP 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518933 1828 CTVRFWFYMIDPrSMGILKVYTIEESG-LNILVWSVIGNKRTGWTYGSVPLSSNS-PFKVAFEADLDGNEDIFIALDDIS 1905
Cdd:pfam00629   74 QCLRFWYHMSGS-GVGTLRVYVRENGGtLDTLLWSISGDQGPSWKEARVTLSSSTqPFQVVFEGIRGGGSRGGIALDDIS 152

                   ....
gi 2462518933 1906 FTPE 1909
Cdd:pfam00629  153 LSSG 156

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 2462518933 1541 CTFEKGWCGWQNSQADNFDWVLGVGSHQSLRPPKDHTLGNENGHFMYLEATAvGLRGDKAHFRS-TMWRESSAACtMSFW 1619
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSpLLPPPRSSHC-LSFW 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462518933 1620 YFISAKATGSIQILIKTEKG--LSKVWQESkQNPGNHWQKADILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEFKN 1693
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 2462518933 1541 CTFEKGW-CGWQNSQADNFDWVLGVGSHQSLRPPKDHTLGNENGHFMYLEATAvGLRGDKAHFRS-TMWRESSAACtMSF 1618
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPSVKTGPSSDHTQGTGSGHFMYVDTSS-GAPGQTARLLSpLLPPSRSPQC-LRF 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462518933 1619 WYFISAKATGSIQILIKTEKG--LSKVWQeSKQNPGNHWQKADILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEF 1691
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVRENGGtlDTLLWS-ISGDQGPSWKEARVTLSSSTQpFQVVFEGIRGGGSRGGIALDDISL 153

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 2462518933  1322 TSSGRCDFEFD-LCSWKQEKDEDFDWnlKASSIPAAGTEPAADHTLGNssGHYIFINSLFPQQPMRAARISSPVISKRSK 1400
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHW--ERVSSATGIPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518933  1401 NCkIIFHYHMYGNGIGALTL-MQVSVTNQTKVLLNLTAEQGNFWRREELSLFG-DEDFQLKFEGRVGKGQRGDIALDDIV 1478
Cdd:smart00137   77 HC-LTFWYYMYGSGSGTLNVyVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTRGKGHSGYIALDDIL 155

                    ...
gi 2462518933  1479 LTE 1481
Cdd:smart00137  156 LSN 158

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518933   93 CDFEDGLCHMTQDQSLQPSWTKRSGMIGLS-PPFYDHNGDVSAHFLSLVSRVDSISSS--LRSRVFLPTNDQHdCqITFY 169
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPgTPPDHTHGTGSGHYLYVESSSGREGQKarLLSPLLPPPRSSH-C-LSFW 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462518933  170 YF-SCQVSGKLMVGLQTACGGPIQHLWQNTAALPNQWERNVIKIQS-SQRFQVVFEGQMASTYEQDevIAIDDISFSSG 246
Cdd:cd06263     79 YHmYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGD--IALDDISLSPG 155

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 2462518933  1540 SCTFEKGW-CGWQNSQADNFDWVLGVGSHQSLRPPKDHTLGneNGHFMYLEATaVGLRGDKAHFRSTMWRESSAACTMSF 1618
Cdd:smart00137    5 NCDFEEGStCGWHQDSNDDGHWERVSSATGIPGPNRDHTTG--NGHFMFFETS-SGAEGQTARLLSPPLYENRSTHCLTF 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462518933  1619 WYFISAKATGSIQILIKTEKG--LSKVWqESKQNPGNHWQKADILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEFKN 1693
Cdd:smart00137   82 WYYMYGSGSGTLNVYVRENNGsqDTLLW-SRSGTQGGQWLQAEVALSSWPQpFQVVFEGTRGKGHSGYIALDDILLSN 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 2462518933  496 CDFESGFCGWEPFLTEDSHWKLMKGLNNgeHHFPAADHTANINHGSFIYLEA-QRSPG-VAKLGSPVLTklLTASTPCqV 573
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESsSGREGqKARLLSPLLP--PPRSSHC-L 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518933  574 QFWYHLS--QHSNLSVFTRTSLDGNLQKQGKIIRFSESQWSHAKIDLiaeaGESTLPFQLILEATVLSSNA-TVALDDIS 650
Cdd:cd06263     76 SFWYHMYgsGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTL----SASSKPFQVVFEGVRGSGSRgDIALDDIS 151

                   ..
gi 2462518933  651 VS 652
Cdd:cd06263    152 LS 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 2462518933   93 CDFEDG-LCHMTQDQSLQPSWTKRSGMIGLSPPFYDHNGDVSA-HFLSLVSRVDSISSS--LRSRVFLPTNDQHdCqITF 168
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPSVKTGPSSDHTQGTGSgHFMYVDTSSGAPGQTarLLSPLLPPSRSPQ-C-LRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518933  169 YYF-SCQVSGKLMVGLQTACGGPIQHLWQNTAALPNQWERNVIKIQSSQR-FQVVFEGQMASTYEQDevIAIDDISFSSG 246
Cdd:pfam00629   79 WYHmSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQpFQVVFEGIRGGGSRGG--IALDDISLSSG 156

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 2462518933  290 CGFEFDMCEWTSEASAGqISWMRTKAREIPafESTPQQDQGGDDEGYYVWVGAKHGftlnHLDSRAYLNSSVCH-CLGKS 368
Cdd:cd06263      1 CDFEDGLCGWTQDSTDD-FDWTRVSGSTPS--PGTPPDHTHGTGSGHYLYVESSSG----REGQKARLLSPLLPpPRSSH 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462518933  369 ChLQFYYAMESS---VLRV--RLYNNKEEEIFWTYNISTHSQWVKADVLIPEDLKTFKIIFEGTLLS-QRSFIALD 438
Cdd:cd06263     74 C-LSFWYHMYGSgvgTLNVyvREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSgSRGDIALD 148

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462518933   290 CGFEFD-MCEWtSEASAGQISWMRTKAREipaFESTPQQDQGGDDeGYYVWVGA---KHGftlnhldSRAYLNSSVCHCL 365
Cdd:smart00137    6 CDFEEGsTCGW-HQDSNDDGHWERVSSAT---GIPGPNRDHTTGN-GHFMFFETssgAEG-------QTARLLSPPLYEN 73