MCP_RAT
ID MCP_RAT Reviewed; 355 AA.
AC Q9Z0M4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Membrane cofactor protein;
DE AltName: CD_antigen=CD46;
DE Flags: Precursor;
GN Name=Cd46; Synonyms=Mcp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9799332; DOI=10.1007/s002510050447;
RA Miwa T., Nonaka M., Okada N., Wakana S., Shiroishi T., Okada H.;
RT "Molecular cloning of rat and mouse membrane cofactor protein (MCP, CD46):
RT preferential expression in testis and close linkage between the mouse Mcp
RT and Cr2 genes on distal chromosome 1.";
RL Immunogenetics 48:363-371(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RC TISSUE=Testis;
RX PubMed=10469244; DOI=10.1046/j.1365-2567.1999.00861.x;
RA Mead R., Hinchliffe S.J., Morgan B.P.;
RT "Molecular cloning, expression and characterization of the rat analogue of
RT human membrane cofactor protein (MCP/CD46).";
RL Immunology 98:137-143(1999).
RN [3]
RP GLYCOSYLATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=15215199; DOI=10.1095/biolreprod.104.030114;
RA Mizuno M., Harris C.L., Johnson P.M., Morgan B.P.;
RT "Rat membrane cofactor protein (MCP; CD46) is expressed only in the
RT acrosome of developing and mature spermatozoa and mediates binding to
RT immobilized activated C3.";
RL Biol. Reprod. 71:1374-1383(2004).
CC -!- FUNCTION: May be involved in the fusion of the spermatozoa with the
CC oocyte during fertilization. {ECO:0000269|PubMed:10469244,
CC ECO:0000269|PubMed:15215199}.
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:0000269|PubMed:15215199}; Single-pass membrane
CC protein {ECO:0000269|PubMed:15215199}. Note=Inner acrosomal membrane of
CC spermatozoa.
CC -!- TISSUE SPECIFICITY: Specifically expressed in testis. Within testis,
CC present only in elongated spermatids and spermatozoa (at protein
CC level). {ECO:0000269|PubMed:10469244, ECO:0000269|PubMed:15215199,
CC ECO:0000269|PubMed:9799332}.
CC -!- DEVELOPMENTAL STAGE: Not expressed in embryonic and immature rats.
CC Expressed in parallel with synthesis of spermatids.
CC {ECO:0000269|PubMed:15215199}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:15215199}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15215199}.
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DR EMBL; AB010920; BAA34811.1; -; mRNA.
DR RefSeq; NP_062063.1; NM_019190.1.
DR AlphaFoldDB; Q9Z0M4; -.
DR SMR; Q9Z0M4; -.
DR STRING; 10116.ENSRNOP00000053980; -.
DR GlyGen; Q9Z0M4; 2 sites.
DR PaxDb; Q9Z0M4; -.
DR GeneID; 29333; -.
DR KEGG; rno:29333; -.
DR CTD; 4179; -.
DR RGD; 3061; Cd46.
DR VEuPathDB; HostDB:ENSRNOG00000008193; -.
DR eggNOG; ENOG502QPUC; Eukaryota.
DR HOGENOM; CLU_020107_1_2_1; -.
DR InParanoid; Q9Z0M4; -.
DR OMA; PPPFEAM; -.
DR OrthoDB; 1239877at2759; -.
DR PhylomeDB; Q9Z0M4; -.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR PRO; PR:Q9Z0M4; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000007917; Expressed in testis and 19 other tissues.
DR Genevisible; Q9Z0M4; RN.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0002079; C:inner acrosomal membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045296; F:cadherin binding; ISO:RGD.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:RGD.
DR GO; GO:0043382; P:positive regulation of memory T cell differentiation; ISO:RGD.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:RGD.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISO:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISO:RGD.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0035581; P:sequestering of extracellular ligand from receptor; ISO:RGD.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR GO; GO:0002456; P:T cell mediated immunity; ISO:RGD.
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 Cytoplasmic vesicle; Disulfide bond; Fertilization; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..355
FT /note="Membrane cofactor protein"
FT /id="PRO_0000238974"
FT TOPO_DOM 43..326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..104
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 105..168
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 169..234
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 235..294
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT DISULFID 107..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 135..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 171..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 200..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 237..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 265..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 355 AA; 39787 MW; 01DF87033ACD41B4 CRC64;
MTAAPLTPDP THPRRRRKSY TFFSLGIYAE ALLFLLSSLS DACEPPPPFE AMELKDKPKP
HYAIGEIIEY TCKKGYLYLS PYPMTAICQP NHTWVPISDH GCIKVQCTML QDPSFGKVHY
IDGRFSWGAR VKYTCMNGYY MVGMSVLQCE LNGNGDAFWN GHPPSCKKVY CLPPPKIKNG
THTFTDIKVF KYHEAVIYSC DPNPGPDKFS LVGPSMLFCA GHNTWSSDPP ECKVVKCPFP
VLQNGRQISR TEKKFSYQAL VLFQCLEGFY MEGSSMVVCG AKSSWEPSIP QCLKGPKPHS
TKPPVYSESG YPSPREGIFG QEFDAWIIAL IVVTSVVGVI VICLIILRCS EYRKK
