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Membrane cofactor protein (CD antigen CD46)

 MCP_MOUSE               Reviewed;         365 AA.
O88174; Q9R0R9;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
20-JUN-2018, entry version 120.
RecName: Full=Membrane cofactor protein;
AltName: CD_antigen=CD46;
Flags: Precursor;
Name=Cd46; Synonyms=Mcp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=9461505; DOI=10.1042/bj3300163;
Tsujimura A., Shida K., Kitamura M., Nomura M., Takeda J., Tanaka H.,
Matsumoto M., Matsumiya K., Okuyama A., Nishimune Y., Okabe M.,
Seya T.;
"Molecular cloning of a murine homologue of membrane cofactor protein
(CD46): preferential expression in testicular germ cells.";
Biochem. J. 330:163-168(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=9799332; DOI=10.1007/s002510050447;
Miwa T., Nonaka M., Okada N., Wakana S., Shiroishi T., Okada H.;
"Molecular cloning of rat and mouse membrane cofactor protein (MCP,
CD46): preferential expression in testis and close linkage between the
mouse Mcp and Cr2 genes on distal chromosome 1.";
Immunogenetics 48:363-371(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10630288; DOI=10.1007/s002510050600;
Nomura M., Tsujimura A., Shida K., Matsumoto M., Matsuda Y.,
Toyoshima K., Seya T.;
"Membrane and secretory forms of mouse membrane cofactor protein
(CD46) generated from a single gene through alternative splicing.";
Immunogenetics 50:245-254(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
GLYCOSYLATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
DISRUPTION PHENOTYPE.
PubMed=12640142; DOI=10.1128/MCB.23.7.2614-2622.2003;
Inoue N., Ikawa M., Nakanishi T., Matsumoto M., Nomura M., Seya T.,
Okabe M.;
"Disruption of mouse CD46 causes an accelerated spontaneous acrosome
reaction in sperm.";
Mol. Cell. Biol. 23:2614-2622(2003).
-!- FUNCTION: May be involved in the fusion of the spermatozoa with
the oocyte during fertilization. {ECO:0000269|PubMed:12640142}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasmic vesicle, secretory
vesicle, acrosome inner membrane; Single-pass type I membrane
protein. Note=Inner acrosomal membrane of spermatozoa.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=O88174-1; Sequence=Displayed;
Name=2;
IsoId=O88174-2; Sequence=VSP_019038, VSP_019039;
Note=Lacks transmembrane domain, probably secreted.;
-!- TISSUE SPECIFICITY: Present only in testis (at protein level).
{ECO:0000269|PubMed:12640142, ECO:0000269|PubMed:9461505,
ECO:0000269|PubMed:9799332}.
-!- DEVELOPMENTAL STAGE: Not expressed until 29 dpc. Expressed in
parallel with synthesis of spermatids.
{ECO:0000269|PubMed:9461505}.
-!- PTM: May be O-glycosylated. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12640142}.
-!- DISRUPTION PHENOTYPE: Mice have normal testis and fertile sperm.
{ECO:0000269|PubMed:12640142}.
-----------------------------------------------------------------------
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EMBL; AB001566; BAA31859.1; -; mRNA.
EMBL; AB010919; BAA34810.1; -; mRNA.
EMBL; AB022600; BAA86056.1; -; mRNA.
EMBL; AK006632; BAB24682.1; -; mRNA.
CCDS; CCDS35828.1; -. [O88174-1]
RefSeq; NP_034908.1; NM_010778.4. [O88174-1]
UniGene; Mm.12884; -.
ProteinModelPortal; O88174; -.
SMR; O88174; -.
STRING; 10090.ENSMUSP00000123931; -.
PhosphoSitePlus; O88174; -.
PaxDb; O88174; -.
PRIDE; O88174; -.
Ensembl; ENSMUST00000162650; ENSMUSP00000123931; ENSMUSG00000016493. [O88174-1]
GeneID; 17221; -.
KEGG; mmu:17221; -.
UCSC; uc007eet.1; mouse. [O88174-1]
CTD; 4179; -.
MGI; MGI:1203290; Cd46.
eggNOG; ENOG410IY7G; Eukaryota.
eggNOG; ENOG4111CPD; LUCA.
GeneTree; ENSGT00910000143999; -.
HOGENOM; HOG000113502; -.
HOVERGEN; HBG006335; -.
InParanoid; O88174; -.
KO; K04007; -.
OMA; TCLYRCL; -.
OrthoDB; EOG091G0DWA; -.
PhylomeDB; O88174; -.
TreeFam; TF334137; -.
Reactome; R-MMU-977606; Regulation of Complement cascade.
ChiTaRS; Cd46; mouse.
PRO; PR:O88174; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000016493; -.
CleanEx; MM_CD46; -.
ExpressionAtlas; O88174; baseline and differential.
Genevisible; O88174; MM.
GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0002079; C:inner acrosomal membrane; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0001848; F:complement binding; ISO:MGI.
GO; GO:0032613; P:interleukin-10 production; ISO:MGI.
GO; GO:0043086; P:negative regulation of catalytic activity; IEA:GOC.
GO; GO:0045916; P:negative regulation of complement activation; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:MGI.
GO; GO:0043382; P:positive regulation of memory T cell differentiation; ISO:MGI.
GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISO:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISO:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0008593; P:regulation of Notch signaling pathway; ISO:MGI.
GO; GO:0035581; P:sequestering of extracellular ligand from receptor; ISO:MGI.
GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
GO; GO:0002456; P:T cell mediated immunity; ISO:MGI.
CDD; cd00033; CCP; 4.
InterPro; IPR017341; CD46.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00084; Sushi; 4.
PIRSF; PIRSF037971; TLX_CD46; 1.
SMART; SM00032; CCP; 4.
SUPFAM; SSF57535; SSF57535; 4.
PROSITE; PS50923; SUSHI; 4.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasmic vesicle;
Disulfide bond; Fertilization; Glycoprotein; Membrane;
Reference proteome; Repeat; Secreted; Signal; Sushi; Transmembrane;
Transmembrane helix.
SIGNAL 1 44 {ECO:0000255}.
CHAIN 45 365 Membrane cofactor protein.
/FTId=PRO_0000238971.
TOPO_DOM 45 329 Extracellular. {ECO:0000255}.
TRANSMEM 330 350 Helical. {ECO:0000255}.
TOPO_DOM 351 365 Cytoplasmic. {ECO:0000255}.
DOMAIN 45 106 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 107 170 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 171 236 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 237 296 Sushi 4. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 205 205 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 301 301 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 304 304 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 310 310 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 312 312 O-linked (GalNAc...) threonine.
{ECO:0000255}.
DISULFID 109 151 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 137 168 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 173 221 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 202 234 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 239 281 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 267 294 {ECO:0000255|PROSITE-ProRule:PRU00302}.
VAR_SEQ 297 310 GPRPTHPTKPPVYN -> VTF (in isoform 2).
{ECO:0000303|PubMed:10630288}.
/FTId=VSP_019038.
VAR_SEQ 311 365 Missing (in isoform 2).
{ECO:0000303|PubMed:10630288}.
/FTId=VSP_019039.
SEQUENCE 365 AA; 40881 MW; 84A4CA8EE165C629 CRC64;
MTAAPLMPDS THPCRRRKSY TFFWCSLGVY AEALLFLLSH LSDACELPRP FEAMELKGTP
KLFYAVGEKI EYKCKKGYLY LSPYLMIATC EPNHTWVPIS DAGCIKVQCT MLQDPSFGKV
YYIDGSFSWG ARAKFTCMEG YYVVGMSVLH CVLKGDDEAY WNGYPPHCEK IYCLPPPKIK
NGTHTLTDIN VFKYHEAVSY SCDPTPGPDK FSLVGTSMIF CAGHNTWSNS PPECKVVKCP
NPVLQNGRLI SGAGEIFSYQ STVMFECLQG FYMEGSSMVI CSANNSWEPS IPKCLKGPRP
THPTKPPVYN YTGYPSPREG IFSQELDAWI IALIVITSIV GVFILCLIVL RCFEHRKKTN
VSAAR


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