MCP_SAGMY
ID MCP_SAGMY Reviewed; 285 AA.
AC O19124; O62684;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Membrane cofactor protein;
DE AltName: CD_antigen=CD46;
DE Flags: Precursor; Fragment;
GN Name=CD46; Synonyms=MCP;
OS Saguinus mystax (Moustached tamarin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Saguinus.
OX NCBI_TaxID=9488;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-186 (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=9525611; DOI=10.1128/jvi.72.4.2905-2916.1998;
RA Hsu E.C., Sarangi F., Iorio C., Sidhu M.S., Udem S.A., Dillehay D.L.,
RA Xu W., Rota P.A., Bellini W.J., Richardson C.D.;
RT "A single amino acid change in the hemagglutinin protein of measles virus
RT determines its ability to bind CD46 and reveals another receptor on
RT marmoset B cells.";
RL J. Virol. 72:2905-2916(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 (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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O19124-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O19124-2; Sequence=VSP_019041, VSP_019042;
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; U87918; AAB66818.1; -; mRNA.
DR EMBL; AF025482; AAC39670.1; -; mRNA.
DR AlphaFoldDB; O19124; -.
DR SMR; O19124; -.
DR GO; GO:0009986; C:cell surface; IEA:InterPro.
DR GO; GO:0002079; C:inner acrosomal membrane; IEA:UniProtKB-SubCell.
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 Alternative splicing; Complement pathway; Cytoplasmic vesicle;
KW Disulfide bond; Fertilization; Glycoprotein; Immunity; Innate immunity;
KW Membrane; Repeat; Signal; Sushi.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..285
FT /note="Membrane cofactor protein"
FT /id="PRO_0000238975"
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 40
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
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)"
FT /evidence="ECO:0000303|PubMed:9223509"
FT /id="VSP_019041"
FT VAR_SEQ 34..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9223509"
FT /id="VSP_019042"
FT NON_TER 285
SQ SEQUENCE 285 AA; 31857 MW; 0E10FF51C1B2CD3E 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 PKCVK
