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P09793

- CTLA4_MOUSE

UniProt

P09793 - CTLA4_MOUSE

Protein

Cytotoxic T-lymphocyte protein 4

Gene

Ctla4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    1. immune response Source: InterPro

    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
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:88556. Ctla4.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: MGI
    2. integral component of membrane Source: UniProtKB-KW

    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_0000014735Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi58 ↔ 129
    Disulfide bondi85 ↔ 103
    Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi157 – 157InterchainPROSITE-ProRule annotation
    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

    PRIDEiP09793.

    PTM databases

    PhosphoSiteiP09793.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in lymphoid tissues.1 Publication

    Gene expression databases

    CleanExiMM_CTLA4.
    GenevestigatoriP09793.

    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 interaction.
    IntActiP09793. 1 interaction.
    MINTiMINT-8019867.

    Structurei

    Secondary structure

    1
    223
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi39 – 413
    Beta strandi44 – 474
    Beta strandi54 – 629
    Beta strandi68 – 769
    Beta strandi81 – 899
    Beta strandi91 – 966
    Beta strandi103 – 1086
    Beta strandi111 – 1166
    Helixi121 – 1233
    Beta strandi125 – 13814
    Beta strandi140 – 1434
    Beta strandi147 – 1504

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DQTX-ray2.00A/B/C/D38-154[»]
    ProteinModelPortaliP09793.
    SMRiP09793. Positions 38-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09793.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini36 – 161126ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini183 – 22341CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei162 – 18221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 145110Ig-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

    eggNOGiNOG42442.
    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.
    [Graphical view]
    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

    MACLGLRRYK AQLQLPSRTW PFVALLTLLF IPVFSEAIQV TQPSVVLASS    50
    HGVASFPCEY SPSHNTDEVR VTVLRQTNDQ MTEVCATTFT EKNTVGFLDY 100
    PFCSGTFNES RVNLTIQGLR AVDTGLYLCK VELMYPPPYF VGMGNGTQIY 150
    VIDPEPCPDS DFLLWILVAV SLGLFFYSFL VSAVSLSKML KKRSPLTTGV 200
    YVKMPPTEPE CEKQFQPYFI PIN 223
    Length:223
    Mass (Da):24,993
    Last modified:July 1, 1989 - v1
    Checksum:i5318FAAF416F4685
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti182 – 1821S → T in AAF01489. (PubMed:10493833)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05719 mRNA. Translation: CAA29191.1 .
    AF142145 Genomic DNA. Translation: AAF01489.1 .
    M74362 Genomic DNA. Translation: AAA37489.1 .
    CCDSi CCDS14993.1.
    PIRi A29063.
    RefSeqi NP_033973.2. NM_009843.4.
    UniGenei Mm.390.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DQT X-ray 2.00 A/B/C/D 38-154 [» ]
    ProteinModelPortali P09793.
    SMRi P09793. Positions 38-154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198575. 1 interaction.
    IntActi P09793. 1 interaction.
    MINTi MINT-8019867.

    PTM databases

    PhosphoSitei P09793.

    Proteomic databases

    PRIDEi P09793.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 12477.
    KEGGi mmu:12477.

    Organism-specific databases

    CTDi 1493.
    MGIi MGI:88556. Ctla4.

    Phylogenomic databases

    eggNOGi NOG42442.
    HOGENOMi HOG000112047.
    HOVERGENi HBG057978.
    InParanoidi P09793.
    KOi K06538.
    PhylomeDBi P09793.

    Miscellaneous databases

    EvolutionaryTracei P09793.
    NextBioi 281362.
    PROi P09793.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_CTLA4.
    Genevestigatori P09793.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR008096. CTLA4.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    [Graphical view ]
    Pfami PF07686. V-set. 1 hit.
    [Graphical view ]
    PRINTSi PR01720. CTLANTIGEN4.
    SMARTi SM00409. IG. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Complete sequence determination of the mouse and human CTLA4 gene loci: cross-species DNA sequence similarity beyond exon borders."
      Ling V., Wu P.W., Finnerty H.F., Sharpe A.H., Gray G.S., Collins M.
      Genomics 60:341-355(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: 129/SvJ.
    3. "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."
      Harper K., Balzano C., Rouvier E., Mattei M.-G., Luciani M.-F., Golstein P.
      J. Immunol. 147:1037-1044(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-36.
    4. "Structure of murine CTLA-4 and its role in modulating T cell responsiveness."
      Ostrov D.A., Shi W., Schwartz J.-C., Almo S.C., Nathenson S.G.
      Science 290:816-819(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 38-154.

    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: October 1, 2014
    This is version 128 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

    External Data

    Dasty 3