MCP_SAGOE
ID MCP_SAGOE Reviewed; 370 AA.
AC O62837; O62834; O62835; O62838; Q9TSH6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Membrane cofactor protein;
DE AltName: CD_antigen=CD46;
DE Flags: Precursor;
GN Name=CD46; Synonyms=MCP;
OS Saguinus oedipus (Cotton-top tamarin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Saguinus.
OX NCBI_TaxID=9490;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), GLYCOSYLATION, AND
RP FUNCTION.
RC TISSUE=B-cell;
RX PubMed=9494106; DOI=10.1042/bj3301351;
RA Murakami Y., Seya T., Kurita M., Fukui A., Ueda S., Nagasawa S.;
RT "Molecular cloning of membrane cofactor protein (MCP; CD46) on B95a cell,
RT an Epstein-Barr virus-transformed marmoset B cell line: B95a-MCP is
RT susceptible to infection by the CAM, but not the Nagahata strain of the
RT measles virus.";
RL Biochem. J. 330:1351-1359(1998).
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. {ECO:0000269|PubMed:9494106}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=O62837-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O62837-2; Sequence=VSP_019043, VSP_019044, VSP_019046;
CC Name=3;
CC IsoId=O62837-3; Sequence=VSP_019043, VSP_019044, VSP_019045,
CC VSP_019047;
CC Name=4;
CC IsoId=O62837-4; Sequence=VSP_019046;
CC -!- DOMAIN: Sushi domains 3 and 4 are the most important for interaction
CC with C3b and C4b. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:9494106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25597.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA25598.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA25599.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA25628.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D63848; BAA25596.1; -; mRNA.
DR EMBL; D78369; BAA25597.1; ALT_INIT; mRNA.
DR EMBL; D82076; BAA25598.1; ALT_INIT; mRNA.
DR EMBL; D85750; BAA25599.1; ALT_INIT; mRNA.
DR EMBL; D89756; BAA25628.1; ALT_INIT; mRNA.
DR AlphaFoldDB; O62837; -.
DR SMR; O62837; -.
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 1: Evidence at protein level;
KW Alternative splicing; Complement pathway; Cytoplasmic vesicle;
KW Disulfide bond; Fertilization; Glycoprotein; Immunity; Innate immunity;
KW Membrane; Repeat; Signal; Sushi; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..370
FT /note="Membrane cofactor protein"
FT /id="PRO_0000238976"
FT TOPO_DOM 33..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..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 287
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT DISULFID 35..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 33
FT /note="D -> G (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:9494106"
FT /id="VSP_019043"
FT VAR_SEQ 34..96
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:9494106"
FT /id="VSP_019044"
FT VAR_SEQ 285
FT /note="K -> KELPPSSIKPPTLSHS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9494106"
FT /id="VSP_019045"
FT VAR_SEQ 286..299
FT /note="VSTSPATVSPTSSV -> GPRPTYKPPVSRY (in isoform 2 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:9494106"
FT /id="VSP_019046"
FT VAR_SEQ 299
FT /note="V -> VPGPRPTYKPPVSRY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9494106"
FT /id="VSP_019047"
FT CONFLICT 312
FT /note="S -> I (in Ref. 1; BAA25628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 40933 MW; D2952CE8929E157B CRC64;
MAPPSRRECP SPSWRFPGLL LAALVLLRSS CSDACGPPPT FEAMELTSRP KPYYKVGERV
EYDCKKGYHH FAPFLTHSIC DRNHTWLPIS DEPCVRKVCH YIPNPLHGEA ILANGSYSFG
NQLHFICNDG YYLIGKEILY CELKGSDAVW SGRPPICQKI LCKPPPKINN GKHTFSDVDV
FEYLDAVTYS CDPAPGPDPF SLIGESTIYC RDNSVWSGDA PECKVVKCRF PVIENGKQIA
GFGKKFYYKA TVIFECDEGF HIIGSDTIVC NSNSTWDPPV PKCVKVSTSP ATVSPTSSVP
GYPNPDEGML NSLDEWAIAL IVIAILVGVA IISFGLHRYL QRRKKKGKAD GTAEYATYQS
KSATLAEQRS
