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Conserved domains on  [gi|1622869763|ref|XP_028690410|]
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apical endosomal glycoprotein isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 677-833 3.60e-45

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.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 160.59  E-value: 3.60e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   677 DREVSCNFERD-TCSWYPGHLSDTHWRWVES----RGPDHDHTTGQGHFVLLDpTDPLAWGHSAHLLSRPQVPAAPTECL 751
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSatgiPGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   752 SFWYYLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGsraQYQLLFEGLR-DGYHGTMALDDVAV 828
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 1622869763   829 RPGPC 833
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 839-1018 5.87e-37

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.


:

Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 136.72  E-value: 5.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  839 CSFEDSD-CGFS--SGGRGLWRRQANASGHTawGPPTDHTTETAQGmgawqgqglggwpgagrlmlappgHYMVVDTSpd 915
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSG------------------------HFMYVDTS-- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  916 ALPRGQTASLTSKEYSPPAQPACLTFWYHGSLHNPGTLRVHLE---KGRKHQVLSLSAHGGLAWRLGSVDVQA-EQAWRV 991
Cdd:pfam00629   53 SGAPGQTARLLSPLLPPSRSPQCLRFWYHMSGSGVGTLRVYVRengGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQV 132

                          170       180
                   ....*....|....*....|....*..
gi 1622869763  992 VFEAVAAGVAHSYVALDDLLLQDGPCP 1018
Cdd:pfam00629  133 VFEGIRGGGSRGGIALDDISLSSGPCP 159
MAM super family cl42956
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 62-219 4.38e-36

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.


The actual alignment was detected with superfamily member smart00137:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 134.39  E-value: 4.38e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763    62 TPFACDFEQDS-CGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTdlGWYMAVGTHRGKEASTAALRSPTLREAAPSC 140
Cdd:smart00137    2 SPGNCDFEEGStCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   141 KLRLWYHAASGDVAELRLEVT--HGSETLTLWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAFW 218
Cdd:smart00137   78 CLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILLS 157


                    .
gi 1622869763   219 D 219
Cdd:smart00137  158 N 158
MAM super family cl42956
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 1018-1244 1.43e-32

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.


The actual alignment was detected with superfamily member smart00137:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 124.38  E-value: 1.43e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  1018 PRPGSCDFESG-LCGWSHLAWPslgGYSWDWGGGATpsRYPQPPVDHTLGTkagtcplepggeatqrphtatwlpaahrv 1096
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSND---DGHWERVSSAT--GIPGPNRDHTTGN----------------------------- 46

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  1097 hapsrggpahsasaralragsahqpginlllfpGHFAFFETGVLGPGgRAAWLRSEPLPAT-PASCLRFWYHMGFPEHfy 1175
Cdd:smart00137   47 ---------------------------------GHFMFFETSSGAEG-QTARLLSPPLYENrSTHCLTFWYYMYGSGS-- 90

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622869763  1176 kGELRVLLRSTQGQLA--VWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGqPALGPIALDDVEYLAGQ 1244
Cdd:smart00137   91 -GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGK-GHSGYIALDDILLSNGP 160
MAM super family cl47572
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 271-450 7.51e-25

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.


The actual alignment was detected with superfamily member pfam00629:

Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 102.06  E-value: 7.51e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  271 TDFETG-LGPWNRSE----GWSRNHsagGPERPSWPRRDHSRNSAQGSFLV---SVAEPGTPAILSSPAFQASGASNCsv 342
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERVS---GPSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  343 rwvgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRGELGTAWVRDRVDIQS-A 421
Cdd:pfam00629   76 -------------------------LRFWYHMSGSGVGTLRVYVRENGGTLDT---LLWSISGDQGPSWKEARVTLSSsT 127

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622869763  422 HPFQILLAGQ--TGPGGVVGLDD-LILSDHCR 450
Cdd:pfam00629  128 QPFQVVFEGIrgGGSRGGIALDDiSLSSGPCP 159
MAM super family cl47572
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 519-669 7.88e-25

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.


The actual alignment was detected with superfamily member pfam00629:

Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 102.06  E-value: 7.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  519 TDFESLEAGGWEDASVGRLQWRRLSA-QESQGSSA-----AAAGHFLSLQRAWGQLSTEARVLTPLLGPSGPSCELHLAY 592
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSdhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRFWY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  593 YLQSQPRGFLALVVVDNGSR--ELAWQALSSSAGGWKVDKVLLGARRRPFQLEFVGLVdlDGPDQQGAGVDNVTL--RDC 668
Cdd:pfam00629   81 HMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGPC 158


                   .
gi 1622869763  669 S 669
Cdd:pfam00629  159 P 159
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-261 3.40e-08

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


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.67  E-value: 3.40e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622869763  229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDED 261
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 483-516 1.48e-06

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


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 45.66  E-value: 1.48e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622869763  483 CKQGHFACGD-LCVPPEQLCDFEEQCAGGEDEQAC 516
Cdd:cd00112      1 CPPNEFRCANgRCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 677-833 3.60e-45

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.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 160.59  E-value: 3.60e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   677 DREVSCNFERD-TCSWYPGHLSDTHWRWVES----RGPDHDHTTGQGHFVLLDpTDPLAWGHSAHLLSRPQVPAAPTECL 751
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSatgiPGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   752 SFWYYLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGsraQYQLLFEGLR-DGYHGTMALDDVAV 828
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 1622869763   829 RPGPC 833
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 682-834 8.79e-45

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 159.06  E-value: 8.79e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  682 CNFERDT-CSWYPGHLSDTHWRWV----ESRGPDHDHT--TGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFW 754
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVsgpsVKTGPSSDHTqgTGSGHFMYVDTSSG-APGQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  755 YYLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGsraQYQLLFEGLRD-GYHGTMALDDVAVRPG 831
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQ---PFQVVFEGIRGgGSRGGIALDDISLSSG 156


                   ...
gi 1622869763  832 PCW 834
Cdd:pfam00629  157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 682-833 4.90e-44

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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 157.15  E-value: 4.90e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  682 CNFERDTCSWYPGHLSDTHWRWVES------RGPDHDHTTGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFWY 755
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGstpspgTPPDHTHGTGSGHYLYVESSSG-REGQKARLLSPLLPPPRSSHCLSFWY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  756 YLHGPQIGTLRLAMRREGE--ETHLWSRSGTQGNRWHEAWATLSHqpgSRAQYQLLFEGLRD-GYHGTMALDDVAVRPGP 832
Cdd:cd06263     80 HMYGSGVGTLNVYVREEGGglGTLLWSASGGQGNQWQEAEVTLSA---SSKPFQVVFEGVRGsGSRGDIALDDISLSPGP 156


                   .
gi 1622869763  833 C 833
Cdd:cd06263    157 C 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 839-1018 5.87e-37

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 136.72  E-value: 5.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  839 CSFEDSD-CGFS--SGGRGLWRRQANASGHTawGPPTDHTTETAQGmgawqgqglggwpgagrlmlappgHYMVVDTSpd 915
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSG------------------------HFMYVDTS-- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  916 ALPRGQTASLTSKEYSPPAQPACLTFWYHGSLHNPGTLRVHLE---KGRKHQVLSLSAHGGLAWRLGSVDVQA-EQAWRV 991
Cdd:pfam00629   53 SGAPGQTARLLSPLLPPSRSPQCLRFWYHMSGSGVGTLRVYVRengGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQV 132

                          170       180
                   ....*....|....*....|....*..
gi 1622869763  992 VFEAVAAGVAHSYVALDDLLLQDGPCP 1018
Cdd:pfam00629  133 VFEGIRGGGSRGGIALDDISLSSGPCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 62-219 4.38e-36

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.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 134.39  E-value: 4.38e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763    62 TPFACDFEQDS-CGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTdlGWYMAVGTHRGKEASTAALRSPTLREAAPSC 140
Cdd:smart00137    2 SPGNCDFEEGStCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   141 KLRLWYHAASGDVAELRLEVT--HGSETLTLWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAFW 218
Cdd:smart00137   78 CLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILLS 157


                    .
gi 1622869763   219 D 219
Cdd:smart00137  158 N 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 66-219 9.87e-36

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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 133.27  E-value: 9.87e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   66 CDFEQDSCGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAA-PSCkLRL 144
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRsSHC-LSF 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622869763  145 WYHAASGDVAELRLEVTHGSETLT--LWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAFWD 219
Cdd:cd06263     78 WYHMYGSGVGTLNVYVREEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 839-1017 5.33e-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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 128.26  E-value: 5.33e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  839 CSFEDSDCGFS--SGGRGLWRRQANASGHTawGPPTDHTTETAQGmgawqgqglggwpgagrlmlappgHYMVVDTSPDa 916
Cdd:cd06263      1 CDFEDGLCGWTqdSTDDFDWTRVSGSTPSP--GTPPDHTHGTGSG------------------------HYLYVESSSG- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  917 lPRGQTASLTSKEYSPPAQPACLTFWYHGSLHNPGTLRVHL-EKGRKHQ--VLSLSAHGGLAWRLGSVDVQAEQA-WRVV 992
Cdd:cd06263     54 -REGQKARLLSPLLPPPRSSHCLSFWYHMYGSGVGTLNVYVrEEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKpFQVV 132

                          170       180
                   ....*....|....*....|....*
gi 1622869763  993 FEAVAAGVAHSYVALDDLLLQDGPC 1017
Cdd:cd06263    133 FEGVRGSGSRGDIALDDISLSPGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 66-217 5.95e-34

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 128.25  E-value: 5.95e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   66 CDFEQDS-CGWRDISTSGYSWLRDRAGAalEGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAAPSCKLRL 144
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPS--VKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622869763  145 WYHAASGDVAELRLEVTHGSETL--TLWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAF 217
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISL 153
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 1018-1244 1.43e-32

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.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 124.38  E-value: 1.43e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  1018 PRPGSCDFESG-LCGWSHLAWPslgGYSWDWGGGATpsRYPQPPVDHTLGTkagtcplepggeatqrphtatwlpaahrv 1096
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSND---DGHWERVSSAT--GIPGPNRDHTTGN----------------------------- 46

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  1097 hapsrggpahsasaralragsahqpginlllfpGHFAFFETGVLGPGgRAAWLRSEPLPAT-PASCLRFWYHMGFPEHfy 1175
Cdd:smart00137   47 ---------------------------------GHFMFFETSSGAEG-QTARLLSPPLYENrSTHCLTFWYYMYGSGS-- 90

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622869763  1176 kGELRVLLRSTQGQLA--VWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGqPALGPIALDDVEYLAGQ 1244
Cdd:smart00137   91 -GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGK-GHSGYIALDDILLSNGP 160
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1023-1244 3.85e-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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 114.40  E-value: 3.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763 1023 CDFESGLCGWSHLawpSLGGYSWDWGGGATPSryPQPPVDHTLGTKAGtcplepggeatqrphtatwlpaahrvhapsrg 1102
Cdd:cd06263      1 CDFEDGLCGWTQD---STDDFDWTRVSGSTPS--PGTPPDHTHGTGSG-------------------------------- 43

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763 1103 gpahsasaralragsahqpginlllfpgHFAFFETGVlGPGGRAAWLRSEPLPAT-PASCLRFWYHMGFPEHfykGELRV 1181
Cdd:cd06263     44 ----------------------------HYLYVESSS-GREGQKARLLSPLLPPPrSSHCLSFWYHMYGSGV---GTLNV 91

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622869763 1182 LLRSTQGQL--AVWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGQPAlGPIALDDVEYLAGQ 1244
Cdd:cd06263     92 YVREEGGGLgtLLWSASGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSR-GDIALDDISLSPGP 156
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 1023-1246 3.89e-27

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 108.60  E-value: 3.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763 1023 CDFESG-LCGWSHlawPSLGGYSWDWGGGatPSRYPQPPVDHTLGTKAGtcplepggeatqrphtatwlpaahrvhapsr 1101
Cdd:pfam00629    1 CDFEDGnLCGWTQ---DSSDDFDWERVSG--PSVKTGPSSDHTQGTGSG------------------------------- 44

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763 1102 ggpahsasaralragsahqpginlllfpgHFAFFETgVLGPGGRAAWLRSEPLPATPAS-CLRFWYHMGFPehfYKGELR 1180
Cdd:pfam00629   45 -----------------------------HFMYVDT-SSGAPGQTARLLSPLLPPSRSPqCLRFWYHMSGS---GVGTLR 91

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622869763 1181 VLLRSTQGQL--AVWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGqPALGPIALDDVEyLAGQRC 1246
Cdd:pfam00629   92 VYVRENGGTLdtLLWSISGDQGPSWKEARVTLsSSTQPFQVVFEGIRGG-GSRGGIALDDIS-LSSGPC 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 271-450 7.51e-25

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 102.06  E-value: 7.51e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  271 TDFETG-LGPWNRSE----GWSRNHsagGPERPSWPRRDHSRNSAQGSFLV---SVAEPGTPAILSSPAFQASGASNCsv 342
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERVS---GPSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  343 rwvgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRGELGTAWVRDRVDIQS-A 421
Cdd:pfam00629   76 -------------------------LRFWYHMSGSGVGTLRVYVRENGGTLDT---LLWSISGDQGPSWKEARVTLSSsT 127

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622869763  422 HPFQILLAGQ--TGPGGVVGLDD-LILSDHCR 450
Cdd:pfam00629  128 QPFQVVFEGIrgGGSRGGIALDDiSLSSGPCP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 519-669 7.88e-25

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 102.06  E-value: 7.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  519 TDFESLEAGGWEDASVGRLQWRRLSA-QESQGSSA-----AAAGHFLSLQRAWGQLSTEARVLTPLLGPSGPSCELHLAY 592
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSdhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRFWY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  593 YLQSQPRGFLALVVVDNGSR--ELAWQALSSSAGGWKVDKVLLGARRRPFQLEFVGLVdlDGPDQQGAGVDNVTL--RDC 668
Cdd:pfam00629   81 HMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGPC 158


                   .
gi 1622869763  669 S 669
Cdd:pfam00629  159 P 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 836-1017 4.14e-22

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.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 94.33  E-value: 4.14e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   836 PHHCSFED-SDCGF--SSGGRGLWRRQanaSGHTAW-GPPTDHTTetaqgmgawqgqglggwpgagrlmlaPPGHYMVVD 911
Cdd:smart00137    3 PGNCDFEEgSTCGWhqDSNDDGHWERV---SSATGIpGPNRDHTT--------------------------GNGHFMFFE 53

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   912 TSPdaLPRGQTASLTSKEYSPPAQPACLTFWYHGSLHNPGTLRVHLeKGRKHQ----VLSLSAHGGLAWRLGSVDVQAE- 986
Cdd:smart00137   54 TSS--GAEGQTARLLSPPLYENRSTHCLTFWYYMYGSGSGTLNVYV-RENNGSqdtlLWSRSGTQGGQWLQAEVALSSWp 130

                           170       180       190
                    ....*....|....*....|....*....|.
gi 1622869763   987 QAWRVVFEAVAAGVAHSYVALDDLLLQDGPC 1017
Cdd:smart00137  131 QPFQVVFEGTRGKGHSGYIALDDILLSNGPC 161
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 249-448 1.45e-21

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.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 92.79  E-value: 1.45e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   249 DGEDNCGDlsdEDPLTCGRHTATDFEtglGPWNRSEGWsrnhsaggpERPSWPRRDHSRNSaqGSFL---VSVAEPGTPA 325
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSA---------TGIPGPNRDHTTGN--GHFMffeTSSGAEGQTA 63

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   326 ILSSPAFQASGASNCsvrwvgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRG 405
Cdd:smart00137   64 RLLSPPLYENRSTHC---------------------------LTFWYYMYGSGSGTLNVYVRENNGSQDT---LLWSRSG 113

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*.
gi 1622869763   406 ELGTAWVRDRVDIQS-AHPFQILLAGQTGPG--GVVGLDDLILSDH 448
Cdd:smart00137  114 TQGGQWLQAEVALSSwPQPFQVVFEGTRGKGhsGYIALDDILLSNG 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 501-667 1.26e-18

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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 84.35  E-value: 1.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  501 CDFEEQcaggedeqACGttdfesleaggWEDASVGRLQWRRLSAQESQ------GSSAAAAGHFLSLQRAWGQLSTEARV 574
Cdd:cd06263      1 CDFEDG--------LCG-----------WTQDSTDDFDWTRVSGSTPSpgtppdHTHGTGSGHYLYVESSSGREGQKARL 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  575 LTPLL-GPSGPSCeLHLAYYLQSQPRGFLALVVVDNGS--RELAWQALSSSAGGWKVDKVLLGARRRPFQLEFVGLVdld 651
Cdd:cd06263     62 LSPLLpPPRSSHC-LSFWYHMYGSGVGTLNVYVREEGGglGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVR--- 137

                          170
                   ....*....|....*..
gi 1622869763  652 GPDQQGA-GVDNVTLRD 667
Cdd:cd06263    138 GSGSRGDiALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 272-448 4.83e-14

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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 70.87  E-value: 4.83e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  272 DFETGLGPWNRSEG----WSRNHSAGGPERPSwprRDHSRNSAQGSFLV---SVAEPGTPAILSSPAFQASGASNCsvrw 344
Cdd:cd06263      2 DFEDGLCGWTQDSTddfdWTRVSGSTPSPGTP---PDHTHGTGSGHYLYvesSSGREGQKARLLSPLLPPPRSSHC---- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  345 vgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRGELGTAWVRDRVDIQSAH-P 423
Cdd:cd06263     75 -----------------------LSFWYHMYGSGVGTLNVYVREEGGGLGT---LLWSASGGQGNQWQEAEVTLSASSkP 128

                          170       180
                   ....*....|....*....|....*..
gi 1622869763  424 FQILLAGQTGPG--GVVGLDDLILSDH 448
Cdd:cd06263    129 FQVVFEGVRGSGsrGDIALDDISLSPG 155
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-261 3.40e-08

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.67  E-value: 3.40e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622869763  229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDED 261
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 229-260 6.90e-08

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.55  E-value: 6.90e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622869763   229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 483-516 1.48e-06

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 45.66  E-value: 1.48e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622869763  483 CKQGHFACGD-LCVPPEQLCDFEEQCAGGEDEQAC 516
Cdd:cd00112      1 CPPNEFRCANgRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 483-513 3.51e-05

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 41.85  E-value: 3.51e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622869763   483 CKQGHFACGD-LCVPPEQLCDFEEQCAGGEDE 513
Cdd:smart00192    2 CPPGEFQCDNgRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
229-260 4.23e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 39.15  E-value: 4.23e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622869763  229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
 
Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 677-833 3.60e-45

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.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 160.59  E-value: 3.60e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   677 DREVSCNFERD-TCSWYPGHLSDTHWRWVES----RGPDHDHTTGQGHFVLLDpTDPLAWGHSAHLLSRPQVPAAPTECL 751
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSatgiPGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   752 SFWYYLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGsraQYQLLFEGLR-DGYHGTMALDDVAV 828
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 1622869763   829 RPGPC 833
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 682-834 8.79e-45

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 159.06  E-value: 8.79e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  682 CNFERDT-CSWYPGHLSDTHWRWV----ESRGPDHDHT--TGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFW 754
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVsgpsVKTGPSSDHTqgTGSGHFMYVDTSSG-APGQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  755 YYLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGsraQYQLLFEGLRD-GYHGTMALDDVAVRPG 831
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQ---PFQVVFEGIRGgGSRGGIALDDISLSSG 156


                   ...
gi 1622869763  832 PCW 834
Cdd:pfam00629  157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 682-833 4.90e-44

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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 157.15  E-value: 4.90e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  682 CNFERDTCSWYPGHLSDTHWRWVES------RGPDHDHTTGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFWY 755
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGstpspgTPPDHTHGTGSGHYLYVESSSG-REGQKARLLSPLLPPPRSSHCLSFWY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  756 YLHGPQIGTLRLAMRREGE--ETHLWSRSGTQGNRWHEAWATLSHqpgSRAQYQLLFEGLRD-GYHGTMALDDVAVRPGP 832
Cdd:cd06263     80 HMYGSGVGTLNVYVREEGGglGTLLWSASGGQGNQWQEAEVTLSA---SSKPFQVVFEGVRGsGSRGDIALDDISLSPGP 156


                   .
gi 1622869763  833 C 833
Cdd:cd06263    157 C 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 839-1018 5.87e-37

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 136.72  E-value: 5.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  839 CSFEDSD-CGFS--SGGRGLWRRQANASGHTawGPPTDHTTETAQGmgawqgqglggwpgagrlmlappgHYMVVDTSpd 915
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSG------------------------HFMYVDTS-- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  916 ALPRGQTASLTSKEYSPPAQPACLTFWYHGSLHNPGTLRVHLE---KGRKHQVLSLSAHGGLAWRLGSVDVQA-EQAWRV 991
Cdd:pfam00629   53 SGAPGQTARLLSPLLPPSRSPQCLRFWYHMSGSGVGTLRVYVRengGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQV 132

                          170       180
                   ....*....|....*....|....*..
gi 1622869763  992 VFEAVAAGVAHSYVALDDLLLQDGPCP 1018
Cdd:pfam00629  133 VFEGIRGGGSRGGIALDDISLSSGPCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 62-219 4.38e-36

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.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 134.39  E-value: 4.38e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763    62 TPFACDFEQDS-CGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTdlGWYMAVGTHRGKEASTAALRSPTLREAAPSC 140
Cdd:smart00137    2 SPGNCDFEEGStCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   141 KLRLWYHAASGDVAELRLEVT--HGSETLTLWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAFW 218
Cdd:smart00137   78 CLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILLS 157


                    .
gi 1622869763   219 D 219
Cdd:smart00137  158 N 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 66-219 9.87e-36

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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 133.27  E-value: 9.87e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   66 CDFEQDSCGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAA-PSCkLRL 144
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRsSHC-LSF 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622869763  145 WYHAASGDVAELRLEVTHGSETLT--LWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAFWD 219
Cdd:cd06263     78 WYHMYGSGVGTLNVYVREEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 839-1017 5.33e-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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 128.26  E-value: 5.33e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  839 CSFEDSDCGFS--SGGRGLWRRQANASGHTawGPPTDHTTETAQGmgawqgqglggwpgagrlmlappgHYMVVDTSPDa 916
Cdd:cd06263      1 CDFEDGLCGWTqdSTDDFDWTRVSGSTPSP--GTPPDHTHGTGSG------------------------HYLYVESSSG- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  917 lPRGQTASLTSKEYSPPAQPACLTFWYHGSLHNPGTLRVHL-EKGRKHQ--VLSLSAHGGLAWRLGSVDVQAEQA-WRVV 992
Cdd:cd06263     54 -REGQKARLLSPLLPPPRSSHCLSFWYHMYGSGVGTLNVYVrEEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKpFQVV 132

                          170       180
                   ....*....|....*....|....*
gi 1622869763  993 FEAVAAGVAHSYVALDDLLLQDGPC 1017
Cdd:cd06263    133 FEGVRGSGSRGDIALDDISLSPGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 66-217 5.95e-34

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 128.25  E-value: 5.95e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   66 CDFEQDS-CGWRDISTSGYSWLRDRAGAalEGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAAPSCKLRL 144
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPS--VKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622869763  145 WYHAASGDVAELRLEVTHGSETL--TLWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAF 217
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISL 153
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 1018-1244 1.43e-32

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.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 124.38  E-value: 1.43e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  1018 PRPGSCDFESG-LCGWSHLAWPslgGYSWDWGGGATpsRYPQPPVDHTLGTkagtcplepggeatqrphtatwlpaahrv 1096
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSND---DGHWERVSSAT--GIPGPNRDHTTGN----------------------------- 46

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  1097 hapsrggpahsasaralragsahqpginlllfpGHFAFFETGVLGPGgRAAWLRSEPLPAT-PASCLRFWYHMGFPEHfy 1175
Cdd:smart00137   47 ---------------------------------GHFMFFETSSGAEG-QTARLLSPPLYENrSTHCLTFWYYMYGSGS-- 90

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622869763  1176 kGELRVLLRSTQGQLA--VWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGqPALGPIALDDVEYLAGQ 1244
Cdd:smart00137   91 -GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGK-GHSGYIALDDILLSNGP 160
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1023-1244 3.85e-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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 114.40  E-value: 3.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763 1023 CDFESGLCGWSHLawpSLGGYSWDWGGGATPSryPQPPVDHTLGTKAGtcplepggeatqrphtatwlpaahrvhapsrg 1102
Cdd:cd06263      1 CDFEDGLCGWTQD---STDDFDWTRVSGSTPS--PGTPPDHTHGTGSG-------------------------------- 43

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763 1103 gpahsasaralragsahqpginlllfpgHFAFFETGVlGPGGRAAWLRSEPLPAT-PASCLRFWYHMGFPEHfykGELRV 1181
Cdd:cd06263     44 ----------------------------HYLYVESSS-GREGQKARLLSPLLPPPrSSHCLSFWYHMYGSGV---GTLNV 91

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622869763 1182 LLRSTQGQL--AVWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGQPAlGPIALDDVEYLAGQ 1244
Cdd:cd06263     92 YVREEGGGLgtLLWSASGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSR-GDIALDDISLSPGP 156
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 1023-1246 3.89e-27

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 108.60  E-value: 3.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763 1023 CDFESG-LCGWSHlawPSLGGYSWDWGGGatPSRYPQPPVDHTLGTKAGtcplepggeatqrphtatwlpaahrvhapsr 1101
Cdd:pfam00629    1 CDFEDGnLCGWTQ---DSSDDFDWERVSG--PSVKTGPSSDHTQGTGSG------------------------------- 44

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763 1102 ggpahsasaralragsahqpginlllfpgHFAFFETgVLGPGGRAAWLRSEPLPATPAS-CLRFWYHMGFPehfYKGELR 1180
Cdd:pfam00629   45 -----------------------------HFMYVDT-SSGAPGQTARLLSPLLPPSRSPqCLRFWYHMSGS---GVGTLR 91

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622869763 1181 VLLRSTQGQL--AVWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGqPALGPIALDDVEyLAGQRC 1246
Cdd:pfam00629   92 VYVRENGGTLdtLLWSISGDQGPSWKEARVTLsSSTQPFQVVFEGIRGG-GSRGGIALDDIS-LSSGPC 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 271-450 7.51e-25

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 102.06  E-value: 7.51e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  271 TDFETG-LGPWNRSE----GWSRNHsagGPERPSWPRRDHSRNSAQGSFLV---SVAEPGTPAILSSPAFQASGASNCsv 342
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERVS---GPSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  343 rwvgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRGELGTAWVRDRVDIQS-A 421
Cdd:pfam00629   76 -------------------------LRFWYHMSGSGVGTLRVYVRENGGTLDT---LLWSISGDQGPSWKEARVTLSSsT 127

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622869763  422 HPFQILLAGQ--TGPGGVVGLDD-LILSDHCR 450
Cdd:pfam00629  128 QPFQVVFEGIrgGGSRGGIALDDiSLSSGPCP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 519-669 7.88e-25

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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 102.06  E-value: 7.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  519 TDFESLEAGGWEDASVGRLQWRRLSA-QESQGSSA-----AAAGHFLSLQRAWGQLSTEARVLTPLLGPSGPSCELHLAY 592
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSdhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRFWY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  593 YLQSQPRGFLALVVVDNGSR--ELAWQALSSSAGGWKVDKVLLGARRRPFQLEFVGLVdlDGPDQQGAGVDNVTL--RDC 668
Cdd:pfam00629   81 HMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGPC 158


                   .
gi 1622869763  669 S 669
Cdd:pfam00629  159 P 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 836-1017 4.14e-22

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.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 94.33  E-value: 4.14e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   836 PHHCSFED-SDCGF--SSGGRGLWRRQanaSGHTAW-GPPTDHTTetaqgmgawqgqglggwpgagrlmlaPPGHYMVVD 911
Cdd:smart00137    3 PGNCDFEEgSTCGWhqDSNDDGHWERV---SSATGIpGPNRDHTT--------------------------GNGHFMFFE 53

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   912 TSPdaLPRGQTASLTSKEYSPPAQPACLTFWYHGSLHNPGTLRVHLeKGRKHQ----VLSLSAHGGLAWRLGSVDVQAE- 986
Cdd:smart00137   54 TSS--GAEGQTARLLSPPLYENRSTHCLTFWYYMYGSGSGTLNVYV-RENNGSqdtlLWSRSGTQGGQWLQAEVALSSWp 130

                           170       180       190
                    ....*....|....*....|....*....|.
gi 1622869763   987 QAWRVVFEAVAAGVAHSYVALDDLLLQDGPC 1017
Cdd:smart00137  131 QPFQVVFEGTRGKGHSGYIALDDILLSNGPC 161
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 249-448 1.45e-21

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.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 92.79  E-value: 1.45e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   249 DGEDNCGDlsdEDPLTCGRHTATDFEtglGPWNRSEGWsrnhsaggpERPSWPRRDHSRNSaqGSFL---VSVAEPGTPA 325
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSA---------TGIPGPNRDHTTGN--GHFMffeTSSGAEGQTA 63

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763   326 ILSSPAFQASGASNCsvrwvgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRG 405
Cdd:smart00137   64 RLLSPPLYENRSTHC---------------------------LTFWYYMYGSGSGTLNVYVRENNGSQDT---LLWSRSG 113

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*.
gi 1622869763   406 ELGTAWVRDRVDIQS-AHPFQILLAGQTGPG--GVVGLDDLILSDH 448
Cdd:smart00137  114 TQGGQWLQAEVALSSwPQPFQVVFEGTRGKGhsGYIALDDILLSNG 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 501-667 1.26e-18

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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 84.35  E-value: 1.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  501 CDFEEQcaggedeqACGttdfesleaggWEDASVGRLQWRRLSAQESQ------GSSAAAAGHFLSLQRAWGQLSTEARV 574
Cdd:cd06263      1 CDFEDG--------LCG-----------WTQDSTDDFDWTRVSGSTPSpgtppdHTHGTGSGHYLYVESSSGREGQKARL 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  575 LTPLL-GPSGPSCeLHLAYYLQSQPRGFLALVVVDNGS--RELAWQALSSSAGGWKVDKVLLGARRRPFQLEFVGLVdld 651
Cdd:cd06263     62 LSPLLpPPRSSHC-LSFWYHMYGSGVGTLNVYVREEGGglGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVR--- 137

                          170
                   ....*....|....*..
gi 1622869763  652 GPDQQGA-GVDNVTLRD 667
Cdd:cd06263    138 GSGSRGDiALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 272-448 4.83e-14

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.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 70.87  E-value: 4.83e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  272 DFETGLGPWNRSEG----WSRNHSAGGPERPSwprRDHSRNSAQGSFLV---SVAEPGTPAILSSPAFQASGASNCsvrw 344
Cdd:cd06263      2 DFEDGLCGWTQDSTddfdWTRVSGSTPSPGTP---PDHTHGTGSGHYLYvesSSGREGQKARLLSPLLPPPRSSHC---- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869763  345 vgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRGELGTAWVRDRVDIQSAH-P 423
Cdd:cd06263     75 -----------------------LSFWYHMYGSGVGTLNVYVREEGGGLGT---LLWSASGGQGNQWQEAEVTLSASSkP 128

                          170       180
                   ....*....|....*....|....*..
gi 1622869763  424 FQILLAGQTGPG--GVVGLDDLILSDH 448
Cdd:cd06263    129 FQVVFEGVRGSGsrGDIALDDISLSPG 155
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-261 3.40e-08

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.67  E-value: 3.40e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622869763  229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDED 261
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 229-260 6.90e-08

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.55  E-value: 6.90e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622869763   229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 483-516 1.48e-06

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 45.66  E-value: 1.48e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622869763  483 CKQGHFACGD-LCVPPEQLCDFEEQCAGGEDEQAC 516
Cdd:cd00112      1 CPPNEFRCANgRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 483-513 3.51e-05

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 41.85  E-value: 3.51e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622869763   483 CKQGHFACGD-LCVPPEQLCDFEEQCAGGEDE 513
Cdd:smart00192    2 CPPGEFQCDNgRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
229-260 4.23e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 39.15  E-value: 4.23e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622869763  229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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