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Protein

Cytotoxic T-lymphocyte protein 4

Gene

CTLA4

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Cytotoxic T-lymphocyte protein 4
Alternative name(s):
Cytotoxic T-lymphocyte-associated antigen 4
Short name:
CTLA-4
CD_antigen: CD152
Gene namesi
Name:CTLA4
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 161126ExtracellularSequence analysisAdd
BLAST
Transmembranei162 – 18221HelicalSequence analysisAdd
BLAST
Topological domaini183 – 22341CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence analysisAdd
BLAST
Chaini36 – 223188Cytotoxic T-lymphocyte protein 4PRO_0000014733Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 129By similarity
Disulfide bondi85 ↔ 103By similarity
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence analysis
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence analysis
Disulfide bondi157 – 157InterchainBy similarity
Modified residuei201 – 2011Phosphotyrosine; by TXK and JAK2By similarity

Post-translational modificationi

N-glycosylation is important for dimerization.By similarity
Phosphorylation at Tyr-201 prevents binding to the AP-2 adapter complex, blocks endocytosis, and leads to retention of CTLA4 on the cell surface.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9XSI1.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Binds to CD80/B7-1 and CD86/B7.2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000018967.

Structurei

3D structure databases

ProteinModelPortaliQ9XSI1.
SMRiQ9XSI1. Positions 37-161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 140102Ig-like V-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 505HomodimerizationBy similarity
Regioni150 – 1556HomodimerizationBy similarity

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJ05. Eukaryota.
ENOG410YUQR. LUCA.
HOGENOMiHOG000112047.
HOVERGENiHBG057978.
InParanoidiQ9XSI1.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR008096. CTLA4.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01720. CTLANTIGEN4.
SUPFAMiSSF48726. SSF48726. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9XSI1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGFGFRRHG VQPDLASRTW PCTALFSLLF IPVFSKGMHA AQPAVVLASS
60 70 80 90 100
RGVASFVCEY GSSGNAAEVR VTMLRQAGSQ MTEVCAATYT VEDELAFLDD
110 120 130 140 150
STCTGTSSGN KVNLTIQGLR AMGTGLYICK VELMYPPPYY VGMGNGTQIY
160 170 180 190 200
VIDPEPCPDS DFLLWILAAV SSGLFFYSFL ITAVSLSKML KKRSPLTTGV
210 220
YVKMPPTGPE CEKQFQPYFI PIN
Length:223
Mass (Da):24,206
Last modified:November 1, 1999 - v1
Checksum:iD70D8BE1F1A6F060
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111V → A in AAF23813 (Ref. 2) Curated
Sequence conflicti35 – 351S → C in AAF23813 (Ref. 2) Curated
Sequence conflicti40 – 401A → V in AAF23813 (Ref. 2) Curated
Sequence conflicti73 – 731M → V in AAF23813 (Ref. 2) Curated
Sequence conflicti123 – 1231G → D in AAF23813 (Ref. 2) Curated
Sequence conflicti208 – 2081G → E in AAF23813 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF143204 mRNA. Translation: AAD31889.1.
AF215893 mRNA. Translation: AAF23813.1.
UniGeneiCfa.3557.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF143204 mRNA. Translation: AAD31889.1.
AF215893 mRNA. Translation: AAF23813.1.
UniGeneiCfa.3557.

3D structure databases

ProteinModelPortaliQ9XSI1.
SMRiQ9XSI1. Positions 37-161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000018967.

Proteomic databases

PaxDbiQ9XSI1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IJ05. Eukaryota.
ENOG410YUQR. LUCA.
HOGENOMiHOG000112047.
HOVERGENiHBG057978.
InParanoidiQ9XSI1.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR008096. CTLA4.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01720. CTLANTIGEN4.
SUPFAMiSSF48726. SSF48726. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of dog cDNA encoding the T-cell costimulatory molecule CTLA-4."
    Khatlani T.S., Ohno K., Inokuma H., Onishi T.
    Immunogenetics 51:79-81(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Beagle.
  2. "Molecular cloning and sequencing of canine CTLA-4 gene and its relationship with autoimmune disease."
    Wei Z., Happ G.M.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Doberman Pinscher X Alaska husky.

Entry informationi

Entry nameiCTLA4_CANLF
AccessioniPrimary (citable) accession number: Q9XSI1
Secondary accession number(s): Q9TT02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.