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Q7TSA3

- BTLA_MOUSE

UniProt

Q7TSA3 - BTLA_MOUSE

Protein

B- and T-lymphocyte attenuator

Gene

Btla

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    Lymphocyte inhibitory receptor which inhibits lymphocytes during immune response.

    GO - Molecular functioni

    1. protein binding Source: MGI
    2. receptor activity Source: MGI

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: MGI
    2. immune response-regulating cell surface receptor signaling pathway Source: MGI
    3. immune system process Source: UniProtKB-KW
    4. negative regulation of alpha-beta T cell proliferation Source: MGI
    5. negative regulation of B cell proliferation Source: MGI
    6. negative regulation of T cell proliferation Source: MGI

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Enzyme and pathway databases

    ReactomeiREACT_225477. Costimulation by the CD28 family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    B- and T-lymphocyte attenuator
    Alternative name(s):
    B- and T-lymphocyte-associated protein
    CD_antigen: CD272
    Gene namesi
    Name:Btla
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:2658978. Btla.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice exhibit no developmental defects in T- or B-cells in thymus or bone marrow, but increased antibody responses and sensitivity to antigen-induced 'experimental autoimmune encephalomyelitis'. T-cells lacking Btla show increased proliferation with a heightened response to anti-CD3 and a slightly greater response to stimulation with anti-IgM.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441L → H: Loss of interaction with TNFRSF14. 1 Publication
    Mutagenesisi48 – 481R → D: Loss of interaction with TNFRSF14. 1 Publication
    Mutagenesisi65 – 651P → A: Loss of interaction with TNFRSF14. 1 Publication
    Mutagenesisi136 – 1361H → D: Loss of interaction with TNFRSF14. 1 Publication
    Mutagenesisi245 – 2451Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-274 and/or F-299. 2 Publications
    Mutagenesisi274 – 2741Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-245 and/or F-299. 2 Publications
    Mutagenesisi299 – 2991Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-245 and/or F-274. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 306277B- and T-lymphocyte attenuatorPRO_0000014524Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi40 ↔ 691 PublicationPROSITE-ProRule annotation
    Disulfide bondi64 ↔ 1241 PublicationPROSITE-ProRule annotation
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi78 ↔ 851 PublicationPROSITE-ProRule annotation
    Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Phosphorylated on Tyr residues by TNFRSF14 and by antigen receptors cross-linking, both inducing association with PTPN6 and PTPN11.1 Publication
    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiQ7TSA3.

    PTM databases

    PhosphoSiteiQ7TSA3.

    Expressioni

    Tissue specificityi

    Expressed in splenic T- and B-cells as well as lymph node tissues but very weakly in somatic tissues. Also expressed in macrophages, NK cells and dendritic cells. A polymorphic tissue distribution between several strains is seen.2 Publications

    Gene expression databases

    ArrayExpressiQ7TSA3.
    BgeeiQ7TSA3.
    CleanExiMM_BTLA.
    GenevestigatoriQ7TSA3.

    Interactioni

    Subunit structurei

    Interacts with tyrosine phosphatases PTPN6/SHP-1 and PTPN11/SHP-2. Interacts with TNFRSF14/HVEM.4 Publications

    Protein-protein interaction databases

    BioGridi228954. 1 interaction.
    STRINGi10090.ENSMUSP00000067877.

    Structurei

    Secondary structure

    1
    306
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 556
    Beta strandi60 – 678
    Beta strandi69 – 713
    Beta strandi75 – 806
    Beta strandi82 – 876
    Beta strandi94 – 996
    Beta strandi101 – 1044
    Beta strandi106 – 1116
    Helixi116 – 1183
    Beta strandi120 – 1289
    Beta strandi131 – 1344
    Beta strandi138 – 1436

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XAUX-ray1.80A30-150[»]
    ProteinModelPortaliQ7TSA3.
    SMRiQ7TSA3. Positions 40-143.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7TSA3.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 183154ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini205 – 306102CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei184 – 20421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini37 – 139103Ig-like V-typeAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG42530.
    GeneTreeiENSGT00390000017390.
    HOGENOMiHOG000168895.
    HOVERGENiHBG080937.
    InParanoidiQ7TSA3.
    KOiK06707.
    OrthoDBiEOG7F513T.
    PhylomeDBiQ7TSA3.
    TreeFamiTF337694.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view]
    SMARTiSM00409. IG. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7TSA3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKTVPAMLGT PRLFREFFIL HLGLWSILCE KATKRNDEEC PVQLTITRNS    50
    KQSARTGELF KIQCPVKYCV HRPNVTWCKH NGTICVPLEV SPQLYTSWEE 100
    NQSVPVFVLH FKPIHLSDNG SYSCSTNFNS QVINSHSVTI HVRERTQNSS 150
    EHPLITVSDI PDATNASGPS TMEERPGRTW LLYTLLPLGA LLLLLACVCL 200
    LCFLKRIQGK EKKPSDLAGR DTNLVDIPAS SRTNHQALPS GTGIYDNDPW 250
    SSMQDESELT ISLQSERNNQ GIVYASLNHC VIGRNPRQEN NMQEAPTEYA 300
    SICVRS 306
    Length:306
    Mass (Da):34,337
    Last modified:July 19, 2005 - v2
    Checksum:iA5B4584BAC882B93
    GO
    Isoform 2 (identifier: Q7TSA3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         37-142: Missing.

    Show »
    Length:200
    Mass (Da):22,326
    Checksum:i94A167B779171DF0
    GO
    Isoform 3 (identifier: Q7TSA3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         156-157: TV → I

    Show »
    Length:305
    Mass (Da):34,250
    Checksum:i14C51F126F2F519A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411P → E in strain: 129/SvEv; requires 2 nucleotide substitutions. 1 Publication
    Natural varianti45 – 473TIT → NIK in strain: 129/SvEv.
    Natural varianti52 – 521Q → H in strain: 129/SvEv. 1 Publication
    Natural varianti55 – 551R → W in strain: 129/SvEv. 1 Publication
    Natural varianti63 – 631Q → E in strain: 129/SvEv. 1 Publication
    Natural varianti85 – 851C → W in strain: 129/SvEv. 1 Publication
    Natural varianti91 – 911S → G in strain: 129/SvEv. 1 Publication
    Natural varianti102 – 1021Q → R in strain: 129/SvEv. 1 Publication
    Natural varianti143 – 1431R → T in strain: C57BL/6J. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei37 – 142106Missing in isoform 2. 1 PublicationVSP_014836Add
    BLAST
    Alternative sequencei156 – 1572TV → I in isoform 3. 1 PublicationVSP_014837

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY293285 mRNA. Translation: AAP44002.1.
    AK041334 mRNA. Translation: BAC30910.1.
    CCDSiCCDS28195.1. [Q7TSA3-1]
    CCDS28196.1. [Q7TSA3-3]
    RefSeqiNP_001032808.2. NM_001037719.2.
    NP_808252.1. NM_177584.3.
    UniGeneiMm.38199.

    Genome annotation databases

    EnsembliENSMUST00000102802; ENSMUSP00000099866; ENSMUSG00000052013.
    GeneIDi208154.
    KEGGimmu:208154.
    UCSCiuc007zik.1. mouse. [Q7TSA3-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY293285 mRNA. Translation: AAP44002.1 .
    AK041334 mRNA. Translation: BAC30910.1 .
    CCDSi CCDS28195.1. [Q7TSA3-1 ]
    CCDS28196.1. [Q7TSA3-3 ]
    RefSeqi NP_001032808.2. NM_001037719.2.
    NP_808252.1. NM_177584.3.
    UniGenei Mm.38199.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XAU X-ray 1.80 A 30-150 [» ]
    ProteinModelPortali Q7TSA3.
    SMRi Q7TSA3. Positions 40-143.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 228954. 1 interaction.
    STRINGi 10090.ENSMUSP00000067877.

    PTM databases

    PhosphoSitei Q7TSA3.

    Proteomic databases

    PRIDEi Q7TSA3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102802 ; ENSMUSP00000099866 ; ENSMUSG00000052013 .
    GeneIDi 208154.
    KEGGi mmu:208154.
    UCSCi uc007zik.1. mouse. [Q7TSA3-3 ]

    Organism-specific databases

    CTDi 151888.
    MGIi MGI:2658978. Btla.

    Phylogenomic databases

    eggNOGi NOG42530.
    GeneTreei ENSGT00390000017390.
    HOGENOMi HOG000168895.
    HOVERGENi HBG080937.
    InParanoidi Q7TSA3.
    KOi K06707.
    OrthoDBi EOG7F513T.
    PhylomeDBi Q7TSA3.
    TreeFami TF337694.

    Enzyme and pathway databases

    Reactomei REACT_225477. Costimulation by the CD28 family.

    Miscellaneous databases

    EvolutionaryTracei Q7TSA3.
    NextBioi 372176.
    PROi Q7TSA3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7TSA3.
    Bgeei Q7TSA3.
    CleanExi MM_BTLA.
    Genevestigatori Q7TSA3.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view ]
    SMARTi SM00409. IG. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF TYR-245; TYR-274 AND TYR-299, GLYCOSYLATION, TISSUE SPECIFICITY, INTERACTION WITH PTPN6 AND PTPN11, DISRUPTION PHENOTYPE, VARIANTS GLU-41; 45-ASN--LYS-47; HIS-52; TRP-55; GLU-63; TRP-85; GLY-91 AND ARG-102.
      Strain: 129/SvEv.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT THR-143.
      Strain: C57BL/6J.
      Tissue: Thymus.
    3. "Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of B and T lymphocyte attenuator required for association with protein tyrosine phosphatases SHP-1 and SHP-2."
      Gavrieli M., Watanabe N., Loftin S.K., Murphy T.L., Murphy K.M.
      Biochem. Biophys. Res. Commun. 312:1236-1243(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-245; TYR-274 AND TYR-299, INTERACTION WITH PTPN6 AND PTPN11.
    4. "B and T lymphocyte attenuator regulates T cell activation through interaction with herpesvirus entry mediator."
      Sedy J.R., Gavrieli M., Potter K.G., Hurchla M.A., Lindsley R.C., Hildner K., Scheu S., Pfeffer K., Ware C.F., Murphy T.L., Murphy K.M.
      Nat. Immunol. 6:90-98(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF14, PHOSPHORYLATION.
    5. "B and T lymphocyte attenuator exhibits structural and expression polymorphisms and is highly induced in anergic CD4+ T cells."
      Hurchla M.A., Sedy J.R., Gavrieli M., Drake C.G., Murphy T.L., Murphy K.M.
      J. Immunol. 174:3377-3385(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, POLYMORPHISM.
    6. "Structural determinants of herpesvirus entry mediator recognition by murine B and T lymphocyte attenuator."
      Nelson C.A., Fremont M.D., Sedy J.R., Norris P.S., Ware C.F., Murphy K.M., Fremont D.H.
      J. Immunol. 180:940-947(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-150, MUTAGENESIS OF LEU-44; ARG-48; PRO-65 AND HIS-136, INTERACTION WITH TNFRSF14/HVEM, DISULFIDE BONDS.

    Entry informationi

    Entry nameiBTLA_MOUSE
    AccessioniPrimary (citable) accession number: Q7TSA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 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