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TVA24_HUMAN
ID   TVA24_HUMAN             Reviewed;         114 AA.
AC   A0A0B4J272;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=T cell receptor alpha variable 24 {ECO:0000303|Ref.2};
DE   Flags: Precursor;
GN   Name=TRAV24 {ECO:0000303|Ref.2};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRAV24*01).
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [2]
RP   NOMENCLATURE.
RA   Lefranc M.P., Lefranc G.;
RT   "The T Cell Receptor FactsBook.";
RL   (In) Lefranc M.P., Lefranc G. (eds.);
RL   The T Cell Receptor FactsBook., pp.1-397, Academic Press, London. (2001).
RN   [3]
RP   REVIEW ON T CELL REPERTOIRE DIVERSITY.
RX   PubMed=15040585; DOI=10.1038/nri1292;
RA   Nikolich-Zugich J., Slifka M.K., Messaoudi I.;
RT   "The many important facets of T-cell repertoire diversity.";
RL   Nat. Rev. Immunol. 4:123-132(2004).
RN   [4]
RP   REVIEW ON T CELL RECEPTOR-CD3 COMPLEX ASSEMBLY, AND SUBCELLULAR LOCATION.
RX   PubMed=20452950; DOI=10.1101/cshperspect.a005140;
RA   Wucherpfennig K.W., Gagnon E., Call M.J., Huseby E.S., Call M.E.;
RT   "Structural biology of the T-cell receptor: insights into receptor
RT   assembly, ligand recognition, and initiation of signaling.";
RL   Cold Spring Harb. Perspect. Biol. 2:A005140-A005140(2010).
RN   [5]
RP   REVIEW ON T CELL RECEPTOR SIGNALING.
RX   PubMed=23524462; DOI=10.1038/nri3403;
RA   Brownlie R.J., Zamoyska R.;
RT   "T cell receptor signalling networks: branched, diversified and bounded.";
RL   Nat. Rev. Immunol. 13:257-269(2013).
RN   [6]
RP   NOMENCLATURE.
RX   PubMed=24600447; DOI=10.3389/fimmu.2014.00022;
RA   Lefranc M.P.;
RT   "Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and Rise
RT   of Immunoinformatics.";
RL   Front. Immunol. 5:22-22(2014).
RN   [7]
RP   REVIEW ON FUNCTION.
RX   PubMed=25493333; DOI=10.1146/annurev-immunol-032414-112334;
RA   Rossjohn J., Gras S., Miles J.J., Turner S.J., Godfrey D.I., McCluskey J.;
RT   "T cell antigen receptor recognition of antigen-presenting molecules.";
RL   Annu. Rev. Immunol. 33:169-200(2015).
CC   -!- FUNCTION: V region of the variable domain of T cell receptor (TR) alpha
CC       chain that participates in the antigen recognition (PubMed:24600447).
CC       Alpha-beta T cell receptors are antigen specific receptors which are
CC       essential to the immune response and are present on the cell surface of
CC       T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH)
CC       complexes that are displayed by antigen presenting cells (APC), a
CC       prerequisite for efficient T cell adaptive immunity against pathogens
CC       (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates
CC       TR-CD3 clustering on the cell surface and intracellular activation of
CC       LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247
CC       enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT,
CC       which recruits numerous signaling molecules to form the LAT
CC       signalosome. The LAT signalosome propagates signal branching to three
CC       major signaling pathways, the calcium, the mitogen-activated protein
CC       kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB)
CC       pathways, leading to the mobilization of transcription factors that are
CC       critical for gene expression and essential for T cell growth and
CC       differentiation (PubMed:23524462). The T cell repertoire is generated
CC       in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped
CC       by intrathymic selection events to generate a peripheral T cell pool of
CC       self-MH restricted, non-autoaggressive T cells. Post-thymic interaction
CC       of alpha-beta TR with the pMH complexes shapes TR structural and
CC       functional avidity (PubMed:15040585). {ECO:0000303|PubMed:15040585,
CC       ECO:0000303|PubMed:23524462, ECO:0000303|PubMed:24600447,
CC       ECO:0000303|PubMed:25493333}.
CC   -!- SUBUNIT: Alpha-beta TR is a heterodimer composed of an alpha and beta
CC       chain; disulfide-linked. The alpha-beta TR is associated with the
CC       transmembrane signaling CD3 coreceptor proteins to form the TR-CD3 (TcR
CC       or TCR). The assembly of alpha-beta TR heterodimers with CD3 occurs in
CC       the endoplasmic reticulum where a single alpha-beta TR heterodimer
CC       associates with one CD3D-CD3E heterodimer, one CD3G-CD3E heterodimer
CC       and one CD247 homodimer forming a stable octomeric structure. CD3D-CD3E
CC       and CD3G-CD3E heterodimers preferentially associate with TR alpha and
CC       TR beta chains, respectively. The association of the CD247 homodimer is
CC       the last step of TcR assembly in the endoplasmic reticulum and is
CC       required for transport to the cell surface.
CC       {ECO:0000303|PubMed:20452950}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:20452950}.
CC   -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC       IMGT allele TRAV24*01. {ECO:0000305}.
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DR   EMBL; AC245505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PDB; 6CPH; X-ray; 1.70 A; D=23-114.
DR   PDB; 6CQL; X-ray; 2.40 A; D=23-114.
DR   PDB; 6CQN; X-ray; 2.50 A; D=23-114.
DR   PDB; 6CQQ; X-ray; 2.80 A; D/I=23-114.
DR   PDB; 6CQR; X-ray; 3.04 A; D/I=23-114.
DR   PDBsum; 6CPH; -.
DR   PDBsum; 6CQL; -.
DR   PDBsum; 6CQN; -.
DR   PDBsum; 6CQQ; -.
DR   PDBsum; 6CQR; -.
DR   AlphaFoldDB; A0A0B4J272; -.
DR   SMR; A0A0B4J272; -.
DR   IMGT_GENE-DB; TRAV24; -.
DR   GlyGen; A0A0B4J272; 1 site.
DR   BioMuta; TRAV24; -.
DR   Ensembl; ENST00000390453.1; ENSP00000451837.1; ENSG00000211805.1.
DR   GeneCards; TRAV24; -.
DR   HGNC; HGNC:12121; TRAV24.
DR   HPA; ENSG00000211805; Tissue enriched (lymphoid).
DR   neXtProt; NX_A0A0B4J272; -.
DR   OpenTargets; ENSG00000211805; -.
DR   VEuPathDB; HostDB:ENSG00000211805; -.
DR   GeneTree; ENSGT00940000163717; -.
DR   HOGENOM; CLU_077975_8_3_1; -.
DR   OMA; YLCAITQ; -.
DR   PhylomeDB; A0A0B4J272; -.
DR   ChiTaRS; TRAV24; human.
DR   Pharos; A0A0B4J272; Tdark.
DR   PRO; PR:A0A0B4J272; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; A0A0B4J272; protein.
DR   Bgee; ENSG00000211805; Expressed in granulocyte and 87 other tissues.
DR   GO; GO:0042101; C:T cell receptor complex; IEA:UniProtKB-KW.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0009617; P:response to bacterium; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013106; Ig_V-set.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Cell membrane; Disulfide bond;
KW   Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Receptor;
KW   Reference proteome; Signal; T cell receptor.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..114
FT                   /note="T cell receptor alpha variable 24"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5002092613"
FT   DOMAIN          23..>114
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        45..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   NON_TER         114
FT   STRAND          27..36
FT                   /evidence="ECO:0007829|PDB:6CPH"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:6CPH"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:6CQL"
FT   STRAND          54..60
FT                   /evidence="ECO:0007829|PDB:6CPH"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:6CQN"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:6CPH"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:6CPH"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:6CPH"
FT   TURN            90..93
FT                   /evidence="ECO:0007829|PDB:6CPH"
FT   STRAND          94..101
FT                   /evidence="ECO:0007829|PDB:6CPH"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:6CPH"
FT   STRAND          108..114
FT                   /evidence="ECO:0007829|PDB:6CPH"
SQ   SEQUENCE   114 AA;  12919 MW;  52B5D2B3360ED89B CRC64;
     MEKNPLAAPL LILWFHLDCV SSILNVEQSP QSLHVQEGDS TNFTCSFPSS NFYALHWYRW
     ETAKSPEALF VMTLNGDEKK KGRISATLNT KEGYSYLYIK GSQPEDSATY LCAF
 
 
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