MCP_CHLAE
ID MCP_CHLAE Reviewed; 369 AA.
AC P79138; Q7JFM6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Membrane cofactor protein;
DE AltName: CD_antigen=CD46;
DE Flags: Precursor;
GN Name=CD46; Synonyms=MCP;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], BINDING TO MEASLES VIRUS, AND FUNCTION.
RX PubMed=8996635; DOI=10.1248/bpb.19.1541;
RA Murakami Y., Seya T., Kurita M., Nagasawa S.;
RT "Molecular cloning of a complementary DNA for a membrane cofactor protein
RT (MCP, CD46)/measles virus receptor on Vero cells and its functional
RT characterization.";
RL Biol. Pharm. Bull. 19:1541-1545(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-285, INTERACTION WITH MEASLES VIRUS H
RP PROTEIN (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
RC TISSUE=Lymphocyte;
RX PubMed=9223509; DOI=10.1128/jvi.71.8.6144-6154.1997;
RA Hsu E.C., Doerig R.E., Sarangi F., Marcil A., Iorio C., Richardson C.D.;
RT "Artificial mutations and natural variations in the CD46 molecules from
RT human and monkey cells define regions important for measles virus
RT binding.";
RL J. Virol. 71:6144-6154(1997).
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:8996635}.
CC -!- SUBUNIT: Interacts with C3b. Interacts with C4b. Interacts with
CC moesin/MSN. {ECO:0000250|UniProtKB:P15529}.
CC -!- SUBUNIT: (Microbial infection) Binds to Measles virus H protein and
CC acts as a receptor for this virus. {ECO:0000269|PubMed:9223509}.
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 -!- TISSUE SPECIFICITY: Present at the membrane of erythrocytes and
CC lymphocytes (at protein level). {ECO:0000269|PubMed:9223509}.
CC -!- DOMAIN: Sushi domains 1 and 2 are required for interaction with Measles
CC virus H protein. Sushi domains 3 and 4 are the most important for
CC interaction with C3b and C4b.
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DR EMBL; D63811; BAA09881.1; -; mRNA.
DR EMBL; U87920; AAB66820.1; -; mRNA.
DR PIR; JC5138; JC5138.
DR PIR; JC5194; JC5194.
DR AlphaFoldDB; P79138; -.
DR SMR; P79138; -.
DR PRIDE; P79138; -.
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 Complement pathway; Cytoplasmic vesicle; Disulfide bond; Fertilization;
KW Glycoprotein; Host-virus interaction; Immunity; Innate immunity; Membrane;
KW Repeat; Signal; Sushi; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..369
FT /note="Membrane cofactor protein"
FT /id="PRO_0000238970"
FT TOPO_DOM 35..314
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..369
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 REGION 344..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 290
FT /note="O-linked (GalNAc...) threonine"
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 369 AA; 41070 MW; 26E16D15AF768688 CRC64;
MAPPGRRERP FSSGRFPGLL LATLVLQLSS FSDACEAPPT FEAMELIGKP KPYYKVGERV
DYKCKKGYFY VPPLATHSIC DRNHTWLPVS DEGCYREMCP HIRDPLNGEA ILANGSYEFG
SELHFICNEG YYLIGKDILY CELKDTVAVW SGKPPLCEKI LCTPPPKIKN GKHTFSEVEV
FEYLDAVTYS CDPAPGPDPF SLIGESMIYC GNNSTWSHAA PECKVVKCRF PVVENGKQIS
GFGKKFYYKA TVMFECDKGY YLNGSDKIVC ESNSTWDPPV PKCLKGPRPT YKPPVSNYPG
YPKPDEGILD SLDDWVIALI VIVIVVAVAV ICVALYRFLQ GRKKKGKADG GPEYATYQTK
STPPAEQRG
