ID   MCP_PONAB               Reviewed;         355 AA.
AC   Q5R4D0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Membrane cofactor protein;
DE   AltName: CD_antigen=CD46;
DE   Flags: Precursor;
GN   Name=CD46; Synonyms=MCP;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a cofactor for complement factor I, a serine protease
CC       which protects autologous cells against complement-mediated injury by
CC       cleaving C3b and C4b deposited on host tissue. May be involved in the
CC       fusion of the spermatozoa with the oocyte during fertilization. Also
CC       acts as a costimulatory factor for T-cells which induces the
CC       differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells
CC       suppress immune responses by secreting interleukin-10, and therefore
CC       are thought to prevent autoimmunity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with C3b. Interacts with C4b. Interacts with
CC       moesin/MSN. {ECO:0000250|UniProtKB:P15529}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       inner membrane {ECO:0000250}; Single-pass type I membrane protein
CC       {ECO:0000250}. Note=Inner acrosomal membrane of spermatozoa.
CC       {ECO:0000250}.
CC   -!- DOMAIN: Sushi domains 3 and 4 are the most important for interaction
CC       with C3b and C4b. {ECO:0000250}.
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DR   EMBL; CR861321; CAH93386.1; -; mRNA.
DR   RefSeq; NP_001127658.1; NM_001134186.1.
DR   AlphaFoldDB; Q5R4D0; -.
DR   SMR; Q5R4D0; -.
DR   STRING; 9601.ENSPPYP00000000275; -.
DR   GeneID; 100174740; -.
DR   KEGG; pon:100174740; -.
DR   CTD; 4179; -.
DR   eggNOG; ENOG502QPUC; Eukaryota.
DR   InParanoid; Q5R4D0; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0009986; C:cell surface; IEA:InterPro.
DR   GO; GO:0002079; C:inner acrosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; 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   Complement pathway; Cytoplasmic vesicle; Disulfide bond; Fertilization;
KW   Glycoprotein; Immunity; Innate immunity; Membrane; Reference proteome;
KW   Repeat; Signal; Sushi; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..355
FT                   /note="Membrane cofactor protein"
FT                   /id="PRO_0000238973"
FT   TOPO_DOM        35..300
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        322..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..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        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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"
SQ   SEQUENCE   355 AA;  39333 MW;  1B1F63E2628DC4AC CRC64;
     MAPPGRRECA FPSRRFPGLL LAALVLLLSS FSDACEEPPT FEAMELIGKP KPYYDIGERV
     DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIGDPLNGQA ILANGTYEFG
     YQIHFICNEG YYLIGNEILY CELKGSVAIW GGKPPICEKV LCTPPPKIKN GKHTFSEVEV
     FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSHAA PECKVVKCRF PVVENGKQIS
     GFGKKFYYKA TVMFECDKGF YLNGSNTIVC DSNSTWDPPV PKCLKGYPKP EEGILDSLDD
     WVIALIVIAI VVGVAVICAV LYGYLQRRKK KGNADGGAEY ATYQTKSTTP AEQRG