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Cytotoxic T-lymphocyte protein 4 (Cytotoxic T-lymphocyte-associated antigen 4) (CTLA-4) (CD antigen CD152)

 CTLA4_MOUSE             Reviewed;         223 AA.
P09793; Q9QZZ7;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
28-FEB-2018, entry version 153.
RecName: Full=Cytotoxic T-lymphocyte protein 4;
AltName: Full=Cytotoxic T-lymphocyte-associated antigen 4;
Short=CTLA-4;
AltName: CD_antigen=CD152;
Flags: Precursor;
Name=Ctla4; Synonyms=Cd152;
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].
PubMed=3496540; DOI=10.1038/328267a0;
Brunet J.-F., Denizot F., Luciani M.-F., Roux-Dosseto M., Suzan M.,
Mattei M.-G., Golstein P.;
"A new member of the immunoglobulin superfamily -- CTLA-4.";
Nature 328:267-270(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=129/SvJ;
PubMed=10493833; DOI=10.1006/geno.1999.5930;
Ling V., Wu P.W., Finnerty H.F., Sharpe A.H., Gray G.S., Collins M.;
"Complete sequence determination of the mouse and human CTLA4 gene
loci: cross-species DNA sequence similarity beyond exon borders.";
Genomics 60:341-355(1999).
[3]
NUCLEOTIDE SEQUENCE OF 1-36.
PubMed=1713603;
Harper K., Balzano C., Rouvier E., Mattei M.-G., Luciani M.-F.,
Golstein P.;
"CTLA-4 and CD28 activated lymphocyte molecules are closely related in
both mouse and human as to sequence, message expression, gene
structure, and chromosomal location.";
J. Immunol. 147:1037-1044(1991).
[4]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 38-154, AND DISULFIDE BONDS.
PubMed=11052947; DOI=10.1126/science.290.5492.816;
Ostrov D.A., Shi W., Schwartz J.-C., Almo S.C., Nathenson S.G.;
"Structure of murine CTLA-4 and its role in modulating T cell
responsiveness.";
Science 290:816-819(2000).
-!- FUNCTION: Inhibitory receptor acting as a major negative regulator
of T-cell responses. The affinity of CTLA4 for its natural B7
family ligands, CD80 and CD86, is considerably stronger than the
affinity of their cognate stimulatory coreceptor CD28.
{ECO:0000250|UniProtKB:P16410}.
-!- SUBUNIT: Homodimer; disulfide-linked. Binds to CD80/B7-1 and
CD86/B7.2. Interacts with ICOSLG. {ECO:0000250|UniProtKB:P16410}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P16410}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P16410}. Note=Exists primarily an
intracellular antigen whose surface expression is tightly
regulated by restricted trafficking to the cell surface and rapid
internalisation;. {ECO:0000250|UniProtKB:P16410}.
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in
lymphoid tissues. {ECO:0000269|PubMed:10493833}.
-!- PTM: N-glycosylation is important for dimerization.
{ECO:0000250|UniProtKB:P16410}.
-!- PTM: Phosphorylation at Tyr-201 prevents binding to the AP-2
adapter complex, blocks endocytosis, and leads to retention of
CTLA4 on the cell surface. {ECO:0000250|UniProtKB:P16410}.
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EMBL; X05719; CAA29191.1; -; mRNA.
EMBL; AF142145; AAF01489.1; -; Genomic_DNA.
EMBL; M74362; AAA37489.1; -; Genomic_DNA.
CCDS; CCDS14993.1; -.
PIR; A29063; A29063.
RefSeq; NP_033973.2; NM_009843.4.
UniGene; Mm.390; -.
PDB; 1DQT; X-ray; 2.00 A; A/B/C/D=38-154.
PDB; 5E56; X-ray; 1.50 A; A=38-154.
PDB; 5E5M; X-ray; 2.18 A; A/C/E/G=38-154.
PDBsum; 1DQT; -.
PDBsum; 5E56; -.
PDBsum; 5E5M; -.
ProteinModelPortal; P09793; -.
SMR; P09793; -.
BioGrid; 198575; 1.
ELM; P09793; -.
IntAct; P09793; 1.
MINT; P09793; -.
STRING; 10090.ENSMUSP00000027164; -.
iPTMnet; P09793; -.
PhosphoSitePlus; P09793; -.
EPD; P09793; -.
PaxDb; P09793; -.
PRIDE; P09793; -.
GeneID; 12477; -.
KEGG; mmu:12477; -.
CTD; 1493; -.
MGI; MGI:88556; Ctla4.
eggNOG; ENOG410IJ05; Eukaryota.
eggNOG; ENOG410YUQR; LUCA.
HOGENOM; HOG000112047; -.
HOVERGEN; HBG057978; -.
InParanoid; P09793; -.
KO; K06538; -.
PhylomeDB; P09793; -.
EvolutionaryTrace; P09793; -.
PRO; PR:P09793; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_CTLA4; -.
GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0098636; C:protein complex involved in cell adhesion; ISO:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
GO; GO:0030889; P:negative regulation of B cell proliferation; ISO:MGI.
GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR008096; CTLA4.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
PANTHER; PTHR11494:SF8; PTHR11494:SF8; 1.
Pfam; PF07686; V-set; 1.
PRINTS; PR01720; CTLANTIGEN4.
SMART; SM00409; IG; 1.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 223 Cytotoxic T-lymphocyte protein 4.
/FTId=PRO_0000014735.
TOPO_DOM 36 161 Extracellular. {ECO:0000255}.
TRANSMEM 162 182 Helical. {ECO:0000255}.
TOPO_DOM 183 223 Cytoplasmic. {ECO:0000255}.
DOMAIN 36 145 Ig-like V-type.
REGION 46 50 Homodimerization.
{ECO:0000250|UniProtKB:P16410}.
REGION 134 139 Important for interaction with CD80 and
CD86. {ECO:0000250|UniProtKB:P16410}.
REGION 150 155 Homodimerization.
{ECO:0000250|UniProtKB:P16410}.
MOD_RES 201 201 Phosphotyrosine; by TXK and JAK2.
{ECO:0000250|UniProtKB:P16410}.
CARBOHYD 108 108 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 58 129 {ECO:0000244|PDB:1DQT,
ECO:0000269|PubMed:11052947}.
DISULFID 85 103 {ECO:0000244|PDB:1DQT,
ECO:0000269|PubMed:11052947}.
DISULFID 157 157 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
CONFLICT 182 182 S -> T (in Ref. 2; AAF01489).
{ECO:0000305}.
STRAND 39 41 {ECO:0000244|PDB:5E56}.
STRAND 44 47 {ECO:0000244|PDB:5E56}.
STRAND 54 62 {ECO:0000244|PDB:5E56}.
STRAND 68 79 {ECO:0000244|PDB:5E56}.
STRAND 81 89 {ECO:0000244|PDB:5E56}.
STRAND 91 96 {ECO:0000244|PDB:1DQT}.
STRAND 103 108 {ECO:0000244|PDB:5E56}.
STRAND 111 116 {ECO:0000244|PDB:5E56}.
HELIX 121 123 {ECO:0000244|PDB:5E56}.
STRAND 125 138 {ECO:0000244|PDB:5E56}.
STRAND 140 143 {ECO:0000244|PDB:5E56}.
STRAND 147 150 {ECO:0000244|PDB:5E56}.
SEQUENCE 223 AA; 24993 MW; 5318FAAF416F4685 CRC64;
MACLGLRRYK AQLQLPSRTW PFVALLTLLF IPVFSEAIQV TQPSVVLASS HGVASFPCEY
SPSHNTDEVR VTVLRQTNDQ MTEVCATTFT EKNTVGFLDY PFCSGTFNES RVNLTIQGLR
AVDTGLYLCK VELMYPPPYF VGMGNGTQIY VIDPEPCPDS DFLLWILVAV SLGLFFYSFL
VSAVSLSKML KKRSPLTTGV YVKMPPTEPE CEKQFQPYFI PIN


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