CTLA4_CANLF
ID CTLA4_CANLF Reviewed; 223 AA.
AC Q9XSI1; Q9TT02;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Cytotoxic T-lymphocyte protein 4;
DE AltName: Full=Cytotoxic T-lymphocyte-associated antigen 4;
DE Short=CTLA-4;
DE AltName: CD_antigen=CD152;
DE Flags: Precursor;
GN Name=CTLA4;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle;
RX PubMed=10663567; DOI=10.1007/s002510050013;
RA Khatlani T.S., Ohno K., Inokuma H., Onishi T.;
RT "Cloning and sequencing of dog cDNA encoding the T-cell costimulatory
RT molecule CTLA-4.";
RL Immunogenetics 51:79-81(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Doberman Pinscher X Alaska husky;
RA Wei Z., Happ G.M.;
RT "Molecular cloning and sequencing of canine CTLA-4 gene and its
RT relationship with autoimmune disease.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inhibitory receptor acting as a major negative regulator of
CC T-cell responses. The affinity of CTLA4 for its natural B7 family
CC ligands, CD80 and CD86, is considerably stronger than the affinity of
CC their cognate stimulatory coreceptor CD28.
CC {ECO:0000250|UniProtKB:P16410}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Binds to CD80/B7-1 and CD86/B7.2.
CC Interacts with ICOSLG. {ECO:0000250|UniProtKB:P16410}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16410};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16410}.
CC Note=Exists primarily an intracellular antigen whose surface expression
CC is tightly regulated by restricted trafficking to the cell surface and
CC rapid internalization. {ECO:0000250|UniProtKB:P16410}.
CC -!- PTM: N-glycosylation is important for dimerization.
CC {ECO:0000250|UniProtKB:P16410}.
CC -!- PTM: Phosphorylation at Tyr-201 prevents binding to the AP-2 adapter
CC complex, blocks endocytosis, and leads to retention of CTLA4 on the
CC cell surface. {ECO:0000250|UniProtKB:P16410}.
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DR EMBL; AF143204; AAD31889.1; -; mRNA.
DR EMBL; AF215893; AAF23813.1; -; mRNA.
DR AlphaFoldDB; Q9XSI1; -.
DR SMR; Q9XSI1; -.
DR STRING; 9612.ENSCAFP00000018967; -.
DR PaxDb; Q9XSI1; -.
DR eggNOG; ENOG502RZVK; Eukaryota.
DR InParanoid; Q9XSI1; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; IBA:GO_Central.
DR GO; GO:0042129; P:regulation of T cell proliferation; IEA:InterPro.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR008096; CTLA4.
DR InterPro; IPR040216; CTLA4/CD28.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR11494; PTHR11494; 1.
DR PANTHER; PTHR11494:SF8; PTHR11494:SF8; 1.
DR Pfam; PF07686; V-set; 1.
DR PRINTS; PR01720; CTLANTIGEN4.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..223
FT /note="Cytotoxic T-lymphocyte protein 4"
FT /id="PRO_0000014733"
FT TOPO_DOM 36..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..140
FT /note="Ig-like V-type"
FT REGION 46..50
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P16410"
FT REGION 134..139
FT /note="Important for interaction with CD80 and CD86"
FT /evidence="ECO:0000250|UniProtKB:P16410"
FT REGION 150..155
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P16410"
FT MOD_RES 201
FT /note="Phosphotyrosine; by TXK and JAK2"
FT /evidence="ECO:0000250|UniProtKB:P16410"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..129
FT /evidence="ECO:0000250|UniProtKB:P16410"
FT DISULFID 85..103
FT /evidence="ECO:0000250|UniProtKB:P16410"
FT DISULFID 157
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P16410"
FT CONFLICT 11
FT /note="V -> A (in Ref. 2; AAF23813)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="S -> C (in Ref. 2; AAF23813)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="A -> V (in Ref. 2; AAF23813)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="M -> V (in Ref. 2; AAF23813)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="G -> D (in Ref. 2; AAF23813)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="G -> E (in Ref. 2; AAF23813)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 24206 MW; D70D8BE1F1A6F060 CRC64;
MAGFGFRRHG VQPDLASRTW PCTALFSLLF IPVFSKGMHA AQPAVVLASS RGVASFVCEY
GSSGNAAEVR VTMLRQAGSQ MTEVCAATYT VEDELAFLDD STCTGTSSGN KVNLTIQGLR
AMGTGLYICK VELMYPPPYY VGMGNGTQIY VIDPEPCPDS DFLLWILAAV SSGLFFYSFL
ITAVSLSKML KKRSPLTTGV YVKMPPTGPE CEKQFQPYFI PIN
