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Conserved domains on  [gi|119220585|ref|NP_996803|]
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apical endosomal glycoprotein precursor [Homo sapiens]

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 ...
 572-728 1.72e-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: 160.97  E-value: 1.72e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    572 PREVSCNFERD-TCSWYPGHLSDTHWRWVES----RGPDHDHTTGQGHFVLLDpTDPLAWGHSAHLLSRPQVPAAPTECL 646
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSatgiPGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    647 SFWYHLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGshaQYQLLFEGLR-DGYHGTMALDDVAV 723
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 119220585    724 RPGPC 728
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 734-889 3.96e-40

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: 145.58  E-value: 3.96e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   734 CSFEDSD-CGFS--PGGQGLWRRQANASGHAawGPPTDHTTETAQGHYMVVDTSpdALPRGQTASLTSKEHRPLAQPACL 810
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   811 TFWYHGSLRSPGTLRVYLEERGRHQ---VLSLSAHGGLAWRLGSMDVQA-ERAWRVVFEAVAAGVAHSYVALDDLLLQDG 886
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLdtlLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 119220585   887 PCP 889
Cdd:pfam00629  157 PCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 889-1055 2.11e-39

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: 143.64  E-value: 2.11e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    889 PQPGSCDFESG-LCGWSHLAWPGlggYSWDWGGGATpsRYPQPPVDHTLGTeaGHFAFFETGVLGPGgRAAWLRSEPLPA 967
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDD---GHWERVSSAT--GIPGPNRDHTTGN--GHFMFFETSSGAEG-QTARLLSPPLYE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    968 T-PASCLRFWYHMGFPEHfykGELKVLLHSAQGQLA--VWGAGGHRRHQWLEAQVEV-ASAKEFQIVFEATLGGqPALGP 1043
Cdd:smart00137   73 NrSTHCLTFWYYMYGSGS---GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGK-GHSGY 148

                           170
                    ....*....|..
gi 119220585   1044 IALDDVEYLAGQ 1055
Cdd:smart00137  149 IALDDILLSNGP 160
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 66-219 8.43e-37

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: 135.97  E-value: 8.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   66 CDFEQDPCGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAASS-CkLRL 144
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSShC-LSF 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119220585  145 WYHAASGDVAELRVELTHGAETLT--LWQSTGPWGPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLEFWD 219
Cdd:cd06263    78 WYHMYGSGVGTLNVYVREEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 271-424 8.27e-30

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: 116.31  E-value: 8.27e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   271 TDFETG-LGPWNRSE----GWSRNHragGPERPSWPRRDHSRNSAQGSFLV---SVAEPGTPAILSSPEFQASGTSNCsL 342
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERVS---GPSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   343 VFYQYLSGSEAGCLQLFLQTLGPGAPRapvLLRRRRGELGTAWVRDRVDIQS-AYPFQILLAGQ--TGPGGVVGLDD-LI 418
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDT---LLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIrgGGSRGGIALDDiSL 153


                   ....*.
gi 119220585   419 LSDHCR 424
Cdd:pfam00629  154 SSGPCP 159
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-261 1.02e-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: 51.82  E-value: 1.02e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 119220585  229 CPPGHHHCQNKVCVEPQQLCDGEDNCGDLSDEN 261
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 457-490 4.13e-05

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: 41.42  E-value: 4.13e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 119220585  457 CKQGHLACGD-LCVPPEQLCDFEEQCAGGEDEQAC 490
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 ...
 572-728 1.72e-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: 160.97  E-value: 1.72e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    572 PREVSCNFERD-TCSWYPGHLSDTHWRWVES----RGPDHDHTTGQGHFVLLDpTDPLAWGHSAHLLSRPQVPAAPTECL 646
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSatgiPGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    647 SFWYHLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGshaQYQLLFEGLR-DGYHGTMALDDVAV 723
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 119220585    724 RPGPC 728
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 577-729 3.78e-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: 160.22  E-value: 3.78e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   577 CNFERDT-CSWYPGHLSDTHWRWV----ESRGPDHDHT--TGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFW 649
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVsgpsVKTGPSSDHTqgTGSGHFMYVDTSSG-APGQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   650 YHLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGshaQYQLLFEGLRD-GYHGTMALDDVAVRPG 726
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQ---PFQVVFEGIRGgGSRGGIALDDISLSSG 156


                   ...
gi 119220585   727 PCW 729
Cdd:pfam00629  157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 577-728 4.83e-45

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: 159.85  E-value: 4.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  577 CNFERDTCSWYPGHLSDTHWRWVES------RGPDHDHTTGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFWY 650
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGstpspgTPPDHTHGTGSGHYLYVESSSG-REGQKARLLSPLLPPPRSSHCLSFWY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  651 HLHGPQIGTLRLAMRREGE--ETHLWSRSGTQGNRWHEAWATLSHqpgSHAQYQLLFEGLRD-GYHGTMALDDVAVRPGP 727
Cdd:cd06263    80 HMYGSGVGTLNVYVREEGGglGTLLWSASGGQGNQWQEAEVTLSA---SSKPFQVVFEGVRGsGSRGDIALDDISLSPGP 156


                  .
gi 119220585  728 C 728
Cdd:cd06263   157 C 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 734-889 3.96e-40

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: 145.58  E-value: 3.96e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   734 CSFEDSD-CGFS--PGGQGLWRRQANASGHAawGPPTDHTTETAQGHYMVVDTSpdALPRGQTASLTSKEHRPLAQPACL 810
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   811 TFWYHGSLRSPGTLRVYLEERGRHQ---VLSLSAHGGLAWRLGSMDVQA-ERAWRVVFEAVAAGVAHSYVALDDLLLQDG 886
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLdtlLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 119220585   887 PCP 889
Cdd:pfam00629  157 PCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 889-1055 2.11e-39

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: 143.64  E-value: 2.11e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    889 PQPGSCDFESG-LCGWSHLAWPGlggYSWDWGGGATpsRYPQPPVDHTLGTeaGHFAFFETGVLGPGgRAAWLRSEPLPA 967
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDD---GHWERVSSAT--GIPGPNRDHTTGN--GHFMFFETSSGAEG-QTARLLSPPLYE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    968 T-PASCLRFWYHMGFPEHfykGELKVLLHSAQGQLA--VWGAGGHRRHQWLEAQVEV-ASAKEFQIVFEATLGGqPALGP 1043
Cdd:smart00137   73 NrSTHCLTFWYYMYGSGS---GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGK-GHSGY 148

                           170
                    ....*....|..
gi 119220585   1044 IALDDVEYLAGQ 1055
Cdd:smart00137  149 IALDDILLSNGP 160
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 734-888 6.22e-39

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: 142.13  E-value: 6.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  734 CSFEDSDCGFSPG--GQGLWRRQANASGHaaWGPPTDHTTETAQGHYMVVDTSPDalPRGQTASLTSKEHRPLAQPACLT 811
Cdd:cd06263     1 CDFEDGLCGWTQDstDDFDWTRVSGSTPS--PGTPPDHTHGTGSGHYLYVESSSG--REGQKARLLSPLLPPPRSSHCLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  812 FWYHGSLRSPGTLRVYLEERGRHQ---VLSLSAHGGLAWRLGSMDVQAERA-WRVVFEAVAAGVAHSYVALDDLLLQDGP 887
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVREEGGGLgtlLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSPGP 156


                  .
gi 119220585  888 C 888
Cdd:cd06263   157 C 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 894-1055 1.53e-37

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: 138.28  E-value: 1.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  894 CDFESGLCGWSHLAWPGLggySWDWGGGATPSryPQPPVDHTLGTEAGHFAFFETGVlGPGGRAAWLRSEPLPAT-PASC 972
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDF---DWTRVSGSTPS--PGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  973 LRFWYHMGFPEHfykGELKVLLHSAQGQL--AVWGAGGHRRHQWLEAQVEV-ASAKEFQIVFEATLGGQPAlGPIALDDV 1049
Cdd:cd06263    75 LSFWYHMYGSGV---GTLNVYVREEGGGLgtLLWSASGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSR-GDIALDDI 150


                  ....*.
gi 119220585 1050 EYLAGQ 1055
Cdd:cd06263   151 SLSPGP 156
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 66-219 8.43e-37

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: 135.97  E-value: 8.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   66 CDFEQDPCGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAASS-CkLRL 144
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSShC-LSF 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119220585  145 WYHAASGDVAELRVELTHGAETLT--LWQSTGPWGPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLEFWD 219
Cdd:cd06263    78 WYHMYGSGVGTLNVYVREEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 63-219 1.24e-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: 135.93  E-value: 1.24e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585     63 PFACDFEQD-PCGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTdlGWYMAVGTHRGKEASTAALRSPTLREAASSCK 141
Cdd:smart00137    3 PGNCDFEEGsTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRSTHC 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    142 LRLWYHAASGDVAELRVELT--HGAETLTLWQSTGPWGPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLEFWD 219
Cdd:smart00137   79 LTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILLSN 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 894-1057 1.32e-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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 132.87  E-value: 1.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   894 CDFESG-LCGWSHLAwpgLGGYSWDWGGGatPSRYPQPPVDHTLGTEAGHFAFFETgVLGPGGRAAWLRSEPLPATPAS- 971
Cdd:pfam00629    1 CDFEDGnLCGWTQDS---SDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDT-SSGAPGQTARLLSPLLPPSRSPq 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   972 CLRFWYHMGFPehfYKGELKVLLHSAQGQL--AVWGAGGHRRHQWLEAQVEV-ASAKEFQIVFEATLGGqPALGPIALDD 1048
Cdd:pfam00629   75 CLRFWYHMSGS---GVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLsSSTQPFQVVFEGIRGG-GSRGGIALDD 150


                   ....*....
gi 119220585  1049 VEyLAGQHC 1057
Cdd:pfam00629  151 IS-LSSGPC 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 66-217 1.27e-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: 129.79  E-value: 1.27e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    66 CDFEQDP-CGWRDISTSGYSWLRDRAGAalEGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAASSCKLRL 144
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPS--VKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119220585   145 WYHAASGDVAELRVELTHGAETL--TLWQSTGPWGPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLEF 217
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISL 153
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 271-424 8.27e-30

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: 116.31  E-value: 8.27e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   271 TDFETG-LGPWNRSE----GWSRNHragGPERPSWPRRDHSRNSAQGSFLV---SVAEPGTPAILSSPEFQASGTSNCsL 342
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERVS---GPSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   343 VFYQYLSGSEAGCLQLFLQTLGPGAPRapvLLRRRRGELGTAWVRDRVDIQS-AYPFQILLAGQ--TGPGGVVGLDD-LI 418
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDT---LLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIrgGGSRGGIALDDiSL 153


                   ....*.
gi 119220585   419 LSDHCR 424
Cdd:pfam00629  154 SSGPCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 734-888 2.71e-23

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: 97.41  E-value: 2.71e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    734 CSFED-SDCGFS----PGGQglWRRQANASGHAawGPPTDHTTETaqGHYMVVDTSPdaLPRGQTASLTSKEHRPLAQPA 808
Cdd:smart00137    6 CDFEEgSTCGWHqdsnDDGH--WERVSSATGIP--GPNRDHTTGN--GHFMFFETSS--GAEGQTARLLSPPLYENRSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    809 CLTFWYHGSLRSPGTLRVYLEERGRHQ---VLSLSAHGGLAWRLGSMDVQAE-RAWRVVFEAVAAGVAHSYVALDDLLLQ 884
Cdd:smart00137   78 CLTFWYYMYGSGSGTLNVYVRENNGSQdtlLWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGKGHSGYIALDDILLS 157


                    ....
gi 119220585    885 DGPC 888
Cdd:smart00137  158 NGPC 161
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 249-422 2.62e-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: 94.72  E-value: 2.62e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    249 DGEDNCGDlsdENPLTCGRHIATDFEtglGPWNRSEGWsrnhraggpERPSWPRRDHSRNSaqGSFL---VSVAEPGTPA 325
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSA---------TGIPGPNRDHTTGN--GHFMffeTSSGAEGQTA 63

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    326 ILSSPEFQASGTSNCsLVFYQYLSGSEAGCLQLFLQTLGPGAPRapvLLRRRRGELGTAWVRDRVDIQS-AYPFQILLAG 404
Cdd:smart00137   64 RLLSPPLYENRSTHC-LTFWYYMYGSGSGTLNVYVRENNGSQDT---LLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEG 139

                           170       180
                    ....*....|....*....|
gi 119220585    405 QTGPG--GVVGLDDLILSDH 422
Cdd:smart00137  140 TRGKGhsGYIALDDILLSNG 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 272-422 1.63e-16

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: 77.80  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  272 DFETGL-GPWNRSEGWSRNHRAGGPERPSWPRRDHSRNSAQGSFLV---SVAEPGTPAILSSPEFQASGTSNCsLVFYQY 347
Cdd:cd06263     2 DFEDGLcGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYvesSSGREGQKARLLSPLLPPPRSSHC-LSFWYH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119220585  348 LSGSEAGCLQLFLQTLGPGAPRapvLLRRRRGELGTAWVRDRVDIQS-AYPFQILLAGQTGPG--GVVGLDDLILSDH 422
Cdd:cd06263    81 MYGSGVGTLNVYVREEGGGLGT---LLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGsrGDIALDDISLSPG 155
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-261 1.02e-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: 51.82  E-value: 1.02e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 119220585  229 CPPGHHHCQNKVCVEPQQLCDGEDNCGDLSDEN 261
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 229-260 1.64e-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: 51.09  E-value: 1.64e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 119220585    229 CPPGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 457-490 4.13e-05

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: 41.42  E-value: 4.13e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 119220585  457 CKQGHLACGD-LCVPPEQLCDFEEQCAGGEDEQAC 490
Cdd:cd00112     1 CPPNEFRCANgRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
229-260 5.39e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.47  E-value: 5.39e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 119220585   229 CPPGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 457-487 1.87e-03

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: 36.84  E-value: 1.87e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 119220585    457 CKQGHLACGD-LCVPPEQLCDFEEQCAGGEDE 487
Cdd:smart00192    2 CPPGEFQCDNgRCIPSSWVCDGVDDCGDGSDE 33
 
Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 572-728 1.72e-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: 160.97  E-value: 1.72e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    572 PREVSCNFERD-TCSWYPGHLSDTHWRWVES----RGPDHDHTTGQGHFVLLDpTDPLAWGHSAHLLSRPQVPAAPTECL 646
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSatgiPGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    647 SFWYHLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGshaQYQLLFEGLR-DGYHGTMALDDVAV 723
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 119220585    724 RPGPC 728
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 577-729 3.78e-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: 160.22  E-value: 3.78e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   577 CNFERDT-CSWYPGHLSDTHWRWV----ESRGPDHDHT--TGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFW 649
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVsgpsVKTGPSSDHTqgTGSGHFMYVDTSSG-APGQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   650 YHLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGshaQYQLLFEGLRD-GYHGTMALDDVAVRPG 726
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQ---PFQVVFEGIRGgGSRGGIALDDISLSSG 156


                   ...
gi 119220585   727 PCW 729
Cdd:pfam00629  157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 577-728 4.83e-45

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: 159.85  E-value: 4.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  577 CNFERDTCSWYPGHLSDTHWRWVES------RGPDHDHTTGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFWY 650
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGstpspgTPPDHTHGTGSGHYLYVESSSG-REGQKARLLSPLLPPPRSSHCLSFWY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  651 HLHGPQIGTLRLAMRREGE--ETHLWSRSGTQGNRWHEAWATLSHqpgSHAQYQLLFEGLRD-GYHGTMALDDVAVRPGP 727
Cdd:cd06263    80 HMYGSGVGTLNVYVREEGGglGTLLWSASGGQGNQWQEAEVTLSA---SSKPFQVVFEGVRGsGSRGDIALDDISLSPGP 156


                  .
gi 119220585  728 C 728
Cdd:cd06263   157 C 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 734-889 3.96e-40

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: 145.58  E-value: 3.96e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   734 CSFEDSD-CGFS--PGGQGLWRRQANASGHAawGPPTDHTTETAQGHYMVVDTSpdALPRGQTASLTSKEHRPLAQPACL 810
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   811 TFWYHGSLRSPGTLRVYLEERGRHQ---VLSLSAHGGLAWRLGSMDVQA-ERAWRVVFEAVAAGVAHSYVALDDLLLQDG 886
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLdtlLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 119220585   887 PCP 889
Cdd:pfam00629  157 PCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 889-1055 2.11e-39

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: 143.64  E-value: 2.11e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    889 PQPGSCDFESG-LCGWSHLAWPGlggYSWDWGGGATpsRYPQPPVDHTLGTeaGHFAFFETGVLGPGgRAAWLRSEPLPA 967
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDD---GHWERVSSAT--GIPGPNRDHTTGN--GHFMFFETSSGAEG-QTARLLSPPLYE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    968 T-PASCLRFWYHMGFPEHfykGELKVLLHSAQGQLA--VWGAGGHRRHQWLEAQVEV-ASAKEFQIVFEATLGGqPALGP 1043
Cdd:smart00137   73 NrSTHCLTFWYYMYGSGS---GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGK-GHSGY 148

                           170
                    ....*....|..
gi 119220585   1044 IALDDVEYLAGQ 1055
Cdd:smart00137  149 IALDDILLSNGP 160
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 734-888 6.22e-39

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: 142.13  E-value: 6.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  734 CSFEDSDCGFSPG--GQGLWRRQANASGHaaWGPPTDHTTETAQGHYMVVDTSPDalPRGQTASLTSKEHRPLAQPACLT 811
Cdd:cd06263     1 CDFEDGLCGWTQDstDDFDWTRVSGSTPS--PGTPPDHTHGTGSGHYLYVESSSG--REGQKARLLSPLLPPPRSSHCLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  812 FWYHGSLRSPGTLRVYLEERGRHQ---VLSLSAHGGLAWRLGSMDVQAERA-WRVVFEAVAAGVAHSYVALDDLLLQDGP 887
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVREEGGGLgtlLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSPGP 156


                  .
gi 119220585  888 C 888
Cdd:cd06263   157 C 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 894-1055 1.53e-37

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: 138.28  E-value: 1.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  894 CDFESGLCGWSHLAWPGLggySWDWGGGATPSryPQPPVDHTLGTEAGHFAFFETGVlGPGGRAAWLRSEPLPAT-PASC 972
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDF---DWTRVSGSTPS--PGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  973 LRFWYHMGFPEHfykGELKVLLHSAQGQL--AVWGAGGHRRHQWLEAQVEV-ASAKEFQIVFEATLGGQPAlGPIALDDV 1049
Cdd:cd06263    75 LSFWYHMYGSGV---GTLNVYVREEGGGLgtLLWSASGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSR-GDIALDDI 150


                  ....*.
gi 119220585 1050 EYLAGQ 1055
Cdd:cd06263   151 SLSPGP 156
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 66-219 8.43e-37

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: 135.97  E-value: 8.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   66 CDFEQDPCGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAASS-CkLRL 144
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSShC-LSF 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119220585  145 WYHAASGDVAELRVELTHGAETLT--LWQSTGPWGPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLEFWD 219
Cdd:cd06263    78 WYHMYGSGVGTLNVYVREEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 63-219 1.24e-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: 135.93  E-value: 1.24e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585     63 PFACDFEQD-PCGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTdlGWYMAVGTHRGKEASTAALRSPTLREAASSCK 141
Cdd:smart00137    3 PGNCDFEEGsTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRSTHC 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    142 LRLWYHAASGDVAELRVELT--HGAETLTLWQSTGPWGPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLEFWD 219
Cdd:smart00137   79 LTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILLSN 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 894-1057 1.32e-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.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 132.87  E-value: 1.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   894 CDFESG-LCGWSHLAwpgLGGYSWDWGGGatPSRYPQPPVDHTLGTEAGHFAFFETgVLGPGGRAAWLRSEPLPATPAS- 971
Cdd:pfam00629    1 CDFEDGnLCGWTQDS---SDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDT-SSGAPGQTARLLSPLLPPSRSPq 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   972 CLRFWYHMGFPehfYKGELKVLLHSAQGQL--AVWGAGGHRRHQWLEAQVEV-ASAKEFQIVFEATLGGqPALGPIALDD 1048
Cdd:pfam00629   75 CLRFWYHMSGS---GVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLsSSTQPFQVVFEGIRGG-GSRGGIALDD 150


                   ....*....
gi 119220585  1049 VEyLAGQHC 1057
Cdd:pfam00629  151 IS-LSSGPC 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 66-217 1.27e-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: 129.79  E-value: 1.27e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    66 CDFEQDP-CGWRDISTSGYSWLRDRAGAalEGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAASSCKLRL 144
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPS--VKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119220585   145 WYHAASGDVAELRVELTHGAETL--TLWQSTGPWGPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLEF 217
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISL 153
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 271-424 8.27e-30

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: 116.31  E-value: 8.27e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   271 TDFETG-LGPWNRSE----GWSRNHragGPERPSWPRRDHSRNSAQGSFLV---SVAEPGTPAILSSPEFQASGTSNCsL 342
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERVS---GPSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585   343 VFYQYLSGSEAGCLQLFLQTLGPGAPRapvLLRRRRGELGTAWVRDRVDIQS-AYPFQILLAGQ--TGPGGVVGLDD-LI 418
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDT---LLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIrgGGSRGGIALDDiSL 153


                   ....*.
gi 119220585   419 LSDHCR 424
Cdd:pfam00629  154 SSGPCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 734-888 2.71e-23

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: 97.41  E-value: 2.71e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    734 CSFED-SDCGFS----PGGQglWRRQANASGHAawGPPTDHTTETaqGHYMVVDTSPdaLPRGQTASLTSKEHRPLAQPA 808
Cdd:smart00137    6 CDFEEgSTCGWHqdsnDDGH--WERVSSATGIP--GPNRDHTTGN--GHFMFFETSS--GAEGQTARLLSPPLYENRSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    809 CLTFWYHGSLRSPGTLRVYLEERGRHQ---VLSLSAHGGLAWRLGSMDVQAE-RAWRVVFEAVAAGVAHSYVALDDLLLQ 884
Cdd:smart00137   78 CLTFWYYMYGSGSGTLNVYVRENNGSQdtlLWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGKGHSGYIALDDILLS 157


                    ....
gi 119220585    885 DGPC 888
Cdd:smart00137  158 NGPC 161
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 249-422 2.62e-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: 94.72  E-value: 2.62e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    249 DGEDNCGDlsdENPLTCGRHIATDFEtglGPWNRSEGWsrnhraggpERPSWPRRDHSRNSaqGSFL---VSVAEPGTPA 325
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSA---------TGIPGPNRDHTTGN--GHFMffeTSSGAEGQTA 63

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585    326 ILSSPEFQASGTSNCsLVFYQYLSGSEAGCLQLFLQTLGPGAPRapvLLRRRRGELGTAWVRDRVDIQS-AYPFQILLAG 404
Cdd:smart00137   64 RLLSPPLYENRSTHC-LTFWYYMYGSGSGTLNVYVRENNGSQDT---LLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEG 139

                           170       180
                    ....*....|....*....|
gi 119220585    405 QTGPG--GVVGLDDLILSDH 422
Cdd:smart00137  140 TRGKGhsGYIALDDILLSNG 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 272-422 1.63e-16

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: 77.80  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220585  272 DFETGL-GPWNRSEGWSRNHRAGGPERPSWPRRDHSRNSAQGSFLV---SVAEPGTPAILSSPEFQASGTSNCsLVFYQY 347
Cdd:cd06263     2 DFEDGLcGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYvesSSGREGQKARLLSPLLPPPRSSHC-LSFWYH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119220585  348 LSGSEAGCLQLFLQTLGPGAPRapvLLRRRRGELGTAWVRDRVDIQS-AYPFQILLAGQTGPG--GVVGLDDLILSDH 422
Cdd:cd06263    81 MYGSGVGTLNVYVREEGGGLGT---LLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGsrGDIALDDISLSPG 155
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-261 1.02e-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: 51.82  E-value: 1.02e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 119220585  229 CPPGHHHCQNKVCVEPQQLCDGEDNCGDLSDEN 261
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 229-260 1.64e-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: 51.09  E-value: 1.64e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 119220585    229 CPPGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 457-490 4.13e-05

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: 41.42  E-value: 4.13e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 119220585  457 CKQGHLACGD-LCVPPEQLCDFEEQCAGGEDEQAC 490
Cdd:cd00112     1 CPPNEFRCANgRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
229-260 5.39e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.47  E-value: 5.39e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 119220585   229 CPPGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 457-487 1.87e-03

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: 36.84  E-value: 1.87e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 119220585    457 CKQGHLACGD-LCVPPEQLCDFEEQCAGGEDE 487
Cdd:smart00192    2 CPPGEFQCDNgRCIPSSWVCDGVDDCGDGSDE 33
 
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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