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Protein

Cytotoxic T-lymphocyte protein 4

Gene

Ctla4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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
Synonyms:Cd152
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:88556. Ctla4.

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_000001473536 – 223Cytotoxic T-lymphocyte protein 4Add BLAST188

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi58 ↔ 129Combined sources1 Publication
Disulfide bondi85 ↔ 103Combined sources1 Publication
Glycosylationi108N-linked (GlcNAc...)Sequence analysis1
Glycosylationi113N-linked (GlcNAc...)Sequence analysis1
Glycosylationi145N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi157InterchainPROSITE-ProRule annotation
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

EPDiP09793.
PaxDbiP09793.
PRIDEiP09793.

PTM databases

iPTMnetiP09793.
PhosphoSitePlusiP09793.

Expressioni

Tissue specificityi

Widely expressed with highest levels in lymphoid tissues.1 Publication

Gene expression databases

CleanExiMM_CTLA4.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi198575. 1 interactor.
IntActiP09793. 1 interactor.
MINTiMINT-8019867.
STRINGi10090.ENSMUSP00000027164.

Structurei

Secondary structure

1223
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 41Combined sources3
Beta strandi44 – 47Combined sources4
Beta strandi54 – 62Combined sources9
Beta strandi68 – 79Combined sources12
Beta strandi81 – 89Combined sources9
Beta strandi91 – 96Combined sources6
Beta strandi103 – 108Combined sources6
Beta strandi111 – 116Combined sources6
Helixi121 – 123Combined sources3
Beta strandi125 – 138Combined sources14
Beta strandi140 – 143Combined sources4
Beta strandi147 – 150Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DQTX-ray2.00A/B/C/D38-154[»]
5E56X-ray1.50A38-154[»]
5E5MX-ray2.18A/C/E/G38-154[»]
ProteinModelPortaliP09793.
SMRiP09793.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09793.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 145Ig-like V-typeAdd BLAST110

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.
InParanoidiP09793.
KOiK06538.
PhylomeDBiP09793.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR008096. CTLA4.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01720. CTLANTIGEN4.
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09793-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACLGLRRYK AQLQLPSRTW PFVALLTLLF IPVFSEAIQV TQPSVVLASS
60 70 80 90 100
HGVASFPCEY SPSHNTDEVR VTVLRQTNDQ MTEVCATTFT EKNTVGFLDY
110 120 130 140 150
PFCSGTFNES RVNLTIQGLR AVDTGLYLCK VELMYPPPYF VGMGNGTQIY
160 170 180 190 200
VIDPEPCPDS DFLLWILVAV SLGLFFYSFL VSAVSLSKML KKRSPLTTGV
210 220
YVKMPPTEPE CEKQFQPYFI PIN
Length:223
Mass (Da):24,993
Last modified:July 1, 1989 - v1
Checksum:i5318FAAF416F4685
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti182S → T in AAF01489 (PubMed:10493833).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05719 mRNA. Translation: CAA29191.1.
AF142145 Genomic DNA. Translation: AAF01489.1.
M74362 Genomic DNA. Translation: AAA37489.1.
CCDSiCCDS14993.1.
PIRiA29063.
RefSeqiNP_033973.2. NM_009843.4.
UniGeneiMm.390.

Genome annotation databases

GeneIDi12477.
KEGGimmu:12477.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05719 mRNA. Translation: CAA29191.1.
AF142145 Genomic DNA. Translation: AAF01489.1.
M74362 Genomic DNA. Translation: AAA37489.1.
CCDSiCCDS14993.1.
PIRiA29063.
RefSeqiNP_033973.2. NM_009843.4.
UniGeneiMm.390.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DQTX-ray2.00A/B/C/D38-154[»]
5E56X-ray1.50A38-154[»]
5E5MX-ray2.18A/C/E/G38-154[»]
ProteinModelPortaliP09793.
SMRiP09793.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198575. 1 interactor.
IntActiP09793. 1 interactor.
MINTiMINT-8019867.
STRINGi10090.ENSMUSP00000027164.

PTM databases

iPTMnetiP09793.
PhosphoSitePlusiP09793.

Proteomic databases

EPDiP09793.
PaxDbiP09793.
PRIDEiP09793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi12477.
KEGGimmu:12477.

Organism-specific databases

CTDi1493.
MGIiMGI:88556. Ctla4.

Phylogenomic databases

eggNOGiENOG410IJ05. Eukaryota.
ENOG410YUQR. LUCA.
HOGENOMiHOG000112047.
HOVERGENiHBG057978.
InParanoidiP09793.
KOiK06538.
PhylomeDBiP09793.

Miscellaneous databases

EvolutionaryTraceiP09793.
PROiP09793.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CTLA4.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR008096. CTLA4.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01720. CTLANTIGEN4.
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCTLA4_MOUSE
AccessioniPrimary (citable) accession number: P09793
Secondary accession number(s): Q9QZZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 147 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.