MCP_CAVPO
ID MCP_CAVPO Reviewed; 379 AA.
AC P70105; P97261; P97262; P97263; P97264; P97939;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Membrane cofactor protein;
DE AltName: CD_antigen=CD46;
DE Flags: Precursor;
GN Name=CD46; Synonyms=MCP;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS GMP1; GM1; GM2; GM3 AND
RP GM4).
RC STRAIN=Hartley; TISSUE=Liver, and Testis;
RX PubMed=8943400;
RA Hosokawa M., Nonaka M., Okada N., Nonaka M., Okada H.;
RT "Molecular cloning of guinea pig membrane cofactor protein: preferential
RT expression in testis.";
RL J. Immunol. 157:4946-4952(1996).
CC -!- FUNCTION: May be involved in the fusion of the spermatozoa with the
CC oocyte during fertilization.
CC -!- SUBUNIT: Interacts with C3b. Interacts with C4b. Interacts with
CC moesin/MSN. {ECO:0000250|UniProtKB:P15529}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=GMP1;
CC IsoId=P70105-1; Sequence=Displayed;
CC Name=GM1;
CC IsoId=P70105-2; Sequence=VSP_008757;
CC Name=GM2; Synonyms=GMP2;
CC IsoId=P70105-3; Sequence=VSP_008760;
CC Name=GM3;
CC IsoId=P70105-4; Sequence=VSP_008761;
CC Name=GM4;
CC IsoId=P70105-5; Sequence=VSP_008758, VSP_008759;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in testis.
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DR EMBL; D88358; BAA13594.1; -; mRNA.
DR EMBL; D84134; BAA12236.1; -; Genomic_DNA.
DR EMBL; D84130; BAA12232.1; -; mRNA.
DR EMBL; D84131; BAA12233.1; -; mRNA.
DR EMBL; D84132; BAA12234.1; -; mRNA.
DR EMBL; D84133; BAA12235.1; -; mRNA.
DR RefSeq; NP_001166399.2; NM_001172928.2. [P70105-1]
DR AlphaFoldDB; P70105; -.
DR SMR; P70105; -.
DR STRING; 10141.ENSCPOP00000001186; -.
DR GeneID; 100135498; -.
DR KEGG; cpoc:100135498; -.
DR CTD; 4179; -.
DR eggNOG; ENOG502QPUC; Eukaryota.
DR HOGENOM; CLU_020107_1_0_1; -.
DR InParanoid; P70105; -.
DR OrthoDB; 1239877at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 4.
DR InterPro; IPR017341; CD46.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 4.
DR PIRSF; PIRSF037971; TLX_CD46; 1.
DR SMART; SM00032; CCP; 4.
DR SUPFAM; SSF57535; SSF57535; 4.
DR PROSITE; PS50923; SUSHI; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Fertilization; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..379
FT /note="Membrane cofactor protein"
FT /id="PRO_0000006007"
FT TOPO_DOM 36..316
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..96
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 97..159
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 160..225
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 226..285
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT DISULFID 36..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 64..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 99..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 127..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 162..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 191..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 228..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 256..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT VAR_SEQ 225..285
FT /note="Missing (in isoform GM2)"
FT /evidence="ECO:0000303|PubMed:8943400"
FT /id="VSP_008760"
FT VAR_SEQ 225..236
FT /note="VVKCPLPVVKNG -> GNNLLMYLLLHF (in isoform GM4)"
FT /evidence="ECO:0000303|PubMed:8943400"
FT /id="VSP_008758"
FT VAR_SEQ 237..379
FT /note="Missing (in isoform GM4)"
FT /evidence="ECO:0000303|PubMed:8943400"
FT /id="VSP_008759"
FT VAR_SEQ 286..327
FT /note="Missing (in isoform GM3)"
FT /evidence="ECO:0000303|PubMed:8943400"
FT /id="VSP_008761"
FT VAR_SEQ 348..379
FT /note="SPEKVMPAIQISDHMVNAPILMPSTVQNPMKR -> RQDDRFN (in
FT isoform GM1)"
FT /evidence="ECO:0000303|PubMed:8943400"
FT /id="VSP_008757"
SQ SEQUENCE 379 AA; 42159 MW; 5DA56B058C8A1573 CRC64;
MAPPLHGESR AASWWRILGA CLLAAVFLLA ASSDACVLPP PFEAMEPINP KPYYEIGEKV
EYRCKKGYLR QPFYLMVATC EKNHSWVPIT DDGCIKKQCT YLNPPPKGRV EYINGTRTWG
DIVHFSCVEG FYVSGIAALS CELRGDNVDW NGRVPTCEKV LCSPPPKIQN GKYTFSDVQV
FEYFEAVTYS CDAVQGPDKL SLVGNEVLYC AGHQKWSSAA PECKVVKCPL PVVKNGKQIS
GLGQTFFYQA TVTFQCLPGF YFNGSSTVVC GSDNTWKPSI PECLKGPKPT HPTKPPVYNY
PGYPNPREGI FDQELNLWII ILLILIAVVG LALILLCACR FFERKKKSPE KVMPAIQISD
HMVNAPILMP STVQNPMKR
