ID   TRGV5_HUMAN             Reviewed;         118 AA.
AC   A0A0B4J1U4;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 1.
DT   13-FEB-2019, entry version 23.
DE   RecName: Full=T cell receptor gamma variable 5 {ECO:0000303|Ref.2};
DE   Flags: Precursor;
GN   Name=TRGV5 {ECO:0000303|Ref.2};
GN   Synonyms=TCRGV5 {ECO:0000312|HGNC:HGNC:12290};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRGV5*01).
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(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.
RL   (2001).
RN   [3]
RP   REVIEW ON FUNCTION AND ANTIGEN RECOGNITION.
RX   PubMed=23348415; DOI=10.1038/nri3384;
RA   Vantourout P., Hayday A.;
RT   "Six-of-the-best: unique contributions of gammadelta T cells to
RT   immunology.";
RL   Nat. Rev. Immunol. 13:88-100(2013).
RN   [4]
RP   REVIEW ONGAMMA DELTA T CELL RECEPTOR DIVERSITY.
RX   PubMed=24387714; DOI=10.1146/annurev-immunol-032713-120216;
RA   Chien Y.H., Meyer C., Bonneville M.;
RT   "gammadelta T cells: first line of defense and beyond.";
RL   Annu. Rev. Immunol. 32:121-155(2014).
RN   [5]
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
RT   Rise of Immunoinformatics.";
RL   Front. Immunol. 5:22-22(2014).
RN   [6]
RP   REVIEW ON T CELL RECEPTOR SIGNALING, AND SUBUNIT.
RX   PubMed=25674089; DOI=10.3389/fimmu.2015.00015;
RA   Ribeiro S.T., Ribot J.C., Silva-Santos B.;
RT   "Five Layers of Receptor Signaling in gammadelta T-Cell
RT   Differentiation and Activation.";
RL   Front. Immunol. 6:15-15(2015).
RN   [7]
RP   REVIEW ON FUNCTION.
RX   PubMed=28920588; DOI=10.1038/nri.2017.101;
RA   Nielsen M.M., Witherden D.A., Havran W.L.;
RT   "gammadelta T cells in homeostasis and host defence of epithelial
RT   barrier tissues.";
RL   Nat. Rev. Immunol. 17:733-745(2017).
CC   -!- FUNCTION: V region of the variable domain of T cell receptor (TR)
CC       gamma chain that participates in the antigen recognition
CC       (PubMed:24600447). Gamma-delta TRs recognize a variety of self and
CC       foreign non-peptide antigens frequently expressed at the
CC       epithelial boundaries between the host and external environment,
CC       including endogenous lipids presented by MH-like protein CD1D and
CC       phosphoantigens presented by butyrophilin-like molecule BTN3A1.
CC       Upon antigen recognition induces rapid, innate-like immune
CC       responses involved in pathogen clearance and tissue repair
CC       (PubMed:23348415, PubMed:28920588). Binding of gamma-delta TR
CC       complex to antigen triggers phosphorylation of immunoreceptor
CC       tyrosine-based activation motifs (ITAMs) in the CD3 chains by the
CC       LCK and FYN kinases, allowing the recruitment, phosphorylation,
CC       and activation of ZAP70 that facilitates phosphorylation of the
CC       scaffolding proteins LCP2 and LAT. This lead to the formation of a
CC       supramolecular signalosome that recruits the phospholipase PLCG1,
CC       resulting in calcium mobilization and ERK activation, ultimately
CC       leading to T cell expansion and differentiation into effector
CC       cells (PubMed:25674089). Gamma-delta TRs are produced through
CC       somatic rearrangement of a limited repertoire of variable (V),
CC       diversity (D), and joining (J) genes. The potential diversity of
CC       gamma-delta TRs is conferred by the unique ability to rearrange
CC       (D) genes in tandem and to utilize all three reading frames. The
CC       combinatorial diversity is considerably increased by the sequence
CC       exonuclease trimming and random nucleotide (N) region additions
CC       which occur during the V-(D)-J rearrangements (PubMed:24387714).
CC       {ECO:0000303|PubMed:23348415, ECO:0000303|PubMed:24387714,
CC       ECO:0000303|PubMed:24600447, ECO:0000303|PubMed:25674089,
CC       ECO:0000303|PubMed:28920588}.
CC   -!- SUBUNIT: Gamma-delta TR is a heterodimer composed of a gamma and
CC       delta chain; disulfide-linked. The gamma-delta TR is associated
CC       with the transmembrane signaling CD3 coreceptor proteins following
CC       the stoichiometry: a single gamma-delta TR heterodimer associates
CC       with one CD3D-CD3E heterodimer, one CD3G-CD3E heterodimer and one
CC       CD247 homodimer forming a stable octomeric structure. Upon
CC       activation, gamma-delta TR complex associates with FCER1G to
CC       initiate intracellular signaling. {ECO:0000303|PubMed:25674089}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}.
CC   -!- POLYMORPHISM: There are several alleles. The sequence shown is
CC       that of IMGT allele TRGV5*01. {ECO:0000305}.
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DR   EMBL; AC006033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; A0A0B4J1U4; -.
DR   SMR; A0A0B4J1U4; -.
DR   IMGT_GENE-DB; TRGV5; -.
DR   BioMuta; TRGV5; -.
DR   Ensembl; ENST00000390344; ENSP00000374867; ENSG00000211697.
DR   EuPathDB; HostDB:ENSG00000211697.3; -.
DR   GeneCards; TRGV5; -.
DR   HGNC; HGNC:12290; TRGV5.
DR   OpenTargets; ENSG00000211697; -.
DR   GeneTree; ENSGT00440000034436; -.
DR   OMA; SARIHCE; -.
DR   PhylomeDB; A0A0B4J1U4; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000211697; Expressed in 78 organ(s), highest expression level in leukocyte.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
KW   Immunity; Immunoglobulin domain; Innate immunity; Membrane;
KW   Polymorphism; Receptor; Reference proteome; Signal.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18    118       T cell receptor gamma variable 5.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_5002105557.
FT   DOMAIN       18   >118       Ig-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00114}.
FT   CARBOHYD    106    106       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   DISULFID     41    113       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   NON_TER     118    118
SQ   SEQUENCE   118 AA;  13601 MW;  2152254BAC832649 CRC64;
     MRWALLVLLA FLSPASQKSS NLEGGTKSVT RPTRSSAEIT CDLTVINAFY IHWYLHQEGK
     APQRLLYYDV SNSKDVLESG LSPGKYYTHT PRRWSWILIL RNLIENDSGV YYCATWDR
//