Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Topological domaini36 – 161ExtracellularSequence analysisAdd BLAST126
Transmembranei162 – 182HelicalSequence analysisAdd BLAST21
Topological domaini183 – 223CytoplasmicSequence analysisAdd BLAST41

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Sequence analysisAdd BLAST35
ChainiPRO_000001473336 – 223Cytotoxic T-lymphocyte protein 4Add BLAST188

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi58 ↔ 129By similarity
Disulfide bondi85 ↔ 103By similarity
Glycosylationi113N-linked (GlcNAc...)Sequence analysis1
Glycosylationi145N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi157InterchainBy similarity
Modified residuei201Phosphotyrosine; by TXK and JAK2By similarity1

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 140Ig-like V-typeAdd BLAST102

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni46 – 50HomodimerizationBy similarity5
Regioni150 – 155HomodimerizationBy similarity6

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)DescriptionActionsGraphical viewLength
Sequence conflicti11V → A in AAF23813 (Ref. 2) Curated1
Sequence conflicti35S → C in AAF23813 (Ref. 2) Curated1
Sequence conflicti40A → V in AAF23813 (Ref. 2) Curated1
Sequence conflicti73M → V in AAF23813 (Ref. 2) Curated1
Sequence conflicti123G → D in AAF23813 (Ref. 2) Curated1
Sequence conflicti208G → E in AAF23813 (Ref. 2) Curated1

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.
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...

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: October 5, 2016
This is version 88 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.