TRDV3_HUMAN
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 03-AUG-2022, entry version 107.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE TRDV3*01).
RX PubMed=9110172; DOI=10.1101/gr.7.4.330;
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., 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 [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. (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 Rise
RT 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 Differentiation and
RT 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 barrier
RT tissues.";
RL Nat. Rev. Immunol. 17:733-745(2017).
RN [9] {ECO:0007744|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., 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) delta
CC chain that participates in the antigen recognition (PubMed:24600447).
CC Gamma-delta TRs recognize a variety of self and foreign non-peptide
CC antigens frequently expressed at the epithelial boundaries between the
CC host and external environment, including endogenous lipids presented by
CC MH-like protein CD1D and phosphoantigens presented by butyrophilin-like
CC molecule BTN3A1. Upon antigen recognition induces rapid, innate-like
CC immune responses involved in pathogen clearance and tissue repair
CC (PubMed:28920588, PubMed:23348415). Binding of gamma-delta TR complex
CC to antigen triggers phosphorylation of immunoreceptor tyrosine-based
CC activation motifs (ITAMs) in the CD3 chains by the LCK and FYN kinases,
CC allowing the recruitment, phosphorylation, and activation of ZAP70 that
CC facilitates phosphorylation of the scaffolding proteins LCP2 and LAT.
CC This lead to the formation of a supramolecular signalosome that
CC recruits the phospholipase PLCG1, resulting in calcium mobilization and
CC ERK activation, ultimately leading to T cell expansion and
CC differentiation into effector cells (PubMed:25674089). Gamma-delta TRs
CC are produced through somatic rearrangement of a limited repertoire of
CC variable (V), diversity (D), and joining (J) genes. The potential
CC diversity of gamma-delta TRs is conferred by the unique ability to
CC rearrange (D) genes in tandem and to utilize all three reading frames.
CC The combinatorial diversity is considerably increased by the sequence
CC exonuclease trimming and random nucleotide (N) region additions which
CC 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 delta
CC chain; disulfide-linked. The gamma-delta TR is associated with the
CC transmembrane signaling CD3 coreceptor proteins following the
CC stoichiometry: a single gamma-delta TR heterodimer associates with one
CC CD3D-CD3E heterodimer, one CD3G-CD3E heterodimer and one CD247
CC homodimer forming a stable octomeric structure. Upon activation, gamma-
CC delta TR complex associates with FCER1G to initiate intracellular
CC signaling. {ECO:0000303|PubMed:25674089}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}.
CC -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele TRDV3*01. {ECO:0000305}.
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DR EMBL; AC244502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE000521; AAB69041.1; -; Genomic_DNA.
DR PIR; C31769; C31769.
DR PDB; 1TVD; X-ray; 1.90 A; A/B=19-113.
DR PDB; 7LLI; X-ray; 3.20 A; F/L=19-112.
DR PDBsum; 1TVD; -.
DR PDBsum; 7LLI; -.
DR AlphaFoldDB; A0JD37; -.
DR SMR; A0JD37; -.
DR IMGT_GENE-DB; TRDV3; -.
DR BioMuta; TRDV3; -.
DR PRIDE; A0JD37; -.
DR Ensembl; ENST00000535880.2; ENSP00000451750.1; ENSG00000256590.2.
DR UCSC; uc001web.2; human.
DR GeneCards; TRDV3; -.
DR HGNC; HGNC:12264; TRDV3.
DR HPA; ENSG00000256590; Group enriched (epididymis, lymphoid tissue).
DR neXtProt; NX_A0JD37; -.
DR OpenTargets; ENSG00000256590; -.
DR VEuPathDB; HostDB:ENSG00000256590; -.
DR GeneTree; ENSGT00730000111639; -.
DR HOGENOM; CLU_077975_8_1_1; -.
DR OMA; QFILYRD; -.
DR PhylomeDB; A0JD37; -.
DR PathwayCommons; A0JD37; -.
DR EvolutionaryTrace; A0JD37; -.
DR Pharos; A0JD37; Tdark.
DR PRO; PR:A0JD37; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; A0JD37; protein.
DR Bgee; ENSG00000256590; Expressed in pancreatic ductal cell and 89 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0006955; P:immune response; 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; Adaptive immunity; Cell membrane; Disulfide bond; Immunity;
KW Immunoglobulin domain; Innate immunity; Membrane; Receptor;
KW Reference proteome; Signal; T cell receptor.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..113
FT /note="T cell receptor delta variable 3"
FT /evidence="ECO:0000255"
FT /id="PRO_5014083227"
FT DOMAIN 19..>113
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 40..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:9461220, ECO:0007744|PDB:1TVD"
FT NON_TER 113
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1TVD"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1TVD"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1TVD"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1TVD"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1TVD"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:1TVD"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1TVD"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1TVD"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1TVD"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1TVD"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1TVD"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1TVD"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:1TVD"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1TVD"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:1TVD"
SQ SEQUENCE 113 AA; 12981 MW; F9FD706E5200B595 CRC64;
MILTVGFSFL FFYRGTLCDK VTQSSPDQTV ASGSEVVLLC TYDTVYSNPD LFWYRIRPDY
SFQFVFYGDN SRSEGADFTQ GRFSVKHILT QKAFHLVISP VRTEDSATYY CAF
