ID TRDV3_HUMAN Reviewed; 113 AA. AC A0JD37; DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 13-FEB-2019, entry version 89. DE RecName: Full=T cell receptor delta variable 3 {ECO:0000303|Ref.3}; DE Flags: Precursor; GN Name=TRDV3 {ECO:0000303|Ref.3}; GN Synonyms=hDV103S1 {ECO:0000303|PubMed:9110172}; 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 [GENOMIC DNA] (IMGT ALLELE TRDV3*01). RX PubMed=9110172; RA Boysen C., Simon M.I., Hood L.; RT "Analysis of the 1.1-Mb human alpha/delta T-cell receptor locus with RT bacterial artificial chromosome clones."; RL Genome Res. 7:330-338(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRDV3*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., RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., RA 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., RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., RA Quetier F., Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [3] 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 [4] 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 [5] RP REVIEW ON GAMMA 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 [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 RT Rise of Immunoinformatics."; RL Front. Immunol. 5:22-22(2014). RN [7] 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 [8] 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). RN [9] {ECO:0000244|PDB:1TVD} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 19-113, AND DISULFIDE BONDS. RX PubMed=9461220; DOI=10.1038/35172; RA Li H., Lebedeva M.I., Llera A.S., Fields B.A., Brenner M.B., RA Mariuzza R.A.; RT "Structure of the Vdelta domain of a human gammadelta T-cell antigen RT receptor."; RL Nature 391:502-506(1998). CC -!- FUNCTION: V region of the variable domain of T cell receptor (TR) CC delta 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:28920588, PubMed:23348415). 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 TRDV3*01. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC244502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AE000521; AAB69041.1; -; Genomic_DNA. DR PIR; C31769; C31769. DR UniGene; Hs.74647; -. DR PDB; 1TVD; X-ray; 1.90 A; A/B=19-113. DR PDBsum; 1TVD; -. DR SMR; A0JD37; -. DR IMGT_GENE-DB; TRDV3; -. DR BioMuta; TRDV3; -. DR Ensembl; ENST00000535880; ENSP00000451750; ENSG00000256590. DR UCSC; uc001web.2; human. DR EuPathDB; HostDB:ENSG00000256590.2; -. DR GeneCards; TRDV3; -. DR HGNC; HGNC:12264; TRDV3. DR OpenTargets; ENSG00000256590; -. DR GeneTree; ENSGT00730000111639; -. DR HOVERGEN; HBG105972; -. DR OMA; GRFSVKH; -. DR ChiTaRS; TRDV3; human. DR Proteomes; UP000005640; Chromosome 14. DR Bgee; ENSG00000256590; Expressed in 50 organ(s), highest expression level in gastrocnemius. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0002377; P:immunoglobulin production; IBA:GO_Central. 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 SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond; KW Immunity; Immunoglobulin domain; Innate immunity; Membrane; KW Polymorphism; Receptor; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 113 T cell receptor delta variable 3. FT {ECO:0000255}. FT /FTId=PRO_5014083227. FT DOMAIN 19 >113 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT DISULFID 40 111 {ECO:0000244|PDB:1TVD, FT ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:9461220}. FT NON_TER 113 113 FT STRAND 20 22 {ECO:0000244|PDB:1TVD}. FT STRAND 28 31 {ECO:0000244|PDB:1TVD}. FT STRAND 36 38 {ECO:0000244|PDB:1TVD}. FT STRAND 41 43 {ECO:0000244|PDB:1TVD}. FT STRAND 46 48 {ECO:0000244|PDB:1TVD}. FT STRAND 51 56 {ECO:0000244|PDB:1TVD}. FT STRAND 62 68 {ECO:0000244|PDB:1TVD}. FT STRAND 73 75 {ECO:0000244|PDB:1TVD}. FT HELIX 77 79 {ECO:0000244|PDB:1TVD}. FT TURN 80 82 {ECO:0000244|PDB:1TVD}. FT STRAND 83 88 {ECO:0000244|PDB:1TVD}. FT HELIX 89 91 {ECO:0000244|PDB:1TVD}. FT STRAND 93 100 {ECO:0000244|PDB:1TVD}. FT HELIX 103 105 {ECO:0000244|PDB:1TVD}. FT STRAND 107 113 {ECO:0000244|PDB:1TVD}. SQ SEQUENCE 113 AA; 12981 MW; F9FD706E5200B595 CRC64; MILTVGFSFL FFYRGTLCDK VTQSSPDQTV ASGSEVVLLC TYDTVYSNPD LFWYRIRPDY SFQFVFYGDN SRSEGADFTQ GRFSVKHILT QKAFHLVISP VRTEDSATYY CAF //