TRDC_HUMAN
ID TRDC_HUMAN Reviewed; 153 AA.
AC B7Z8K6;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=T cell receptor delta constant {ECO:0000303|Ref.4};
GN Name=TRDC {ECO:0000303|Ref.4};
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 TRDC*01).
RX PubMed=3413078; DOI=10.1073/pnas.85.16.6097;
RA Takihara Y., Tkachuk D., Michalopoulos E., Champagne E., Reimann J.,
RA Minden M., Mak T.W.;
RT "Sequence and organization of the diversity, joining, and constant region
RT genes of the human T-cell delta-chain locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6097-6101(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (IMGT ALLELE TRDC*01).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRDC*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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10] {ECO:0007744|PDB:1HXM}
RP X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 1-109, AND DISULFIDE BONDS.
RX PubMed=11459064; DOI=10.1038/35081115;
RA Allison T.J., Winter C.C., Fournie J.-J., Bonneville M., Garboczi D.N.;
RT "Structure of a human gammadelta T-cell antigen receptor.";
RL Nature 411:820-824(2001).
CC -!- FUNCTION: Constant region of T cell receptor (TR) delta chain that
CC participates in the antigen recognition (PubMed:24600447). Gamma-delta
CC TRs recognize a variety of self and foreign non-peptide antigens
CC frequently expressed at the epithelial boundaries between the host and
CC external environment, including endogenous lipids presented by MH-like
CC 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 TRDC*01. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61033.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH13992.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M22150; AAA61033.1; ALT_INIT; Genomic_DNA.
DR EMBL; M22148; AAA61033.1; JOINED; Genomic_DNA.
DR EMBL; M22149; AAA61033.1; JOINED; Genomic_DNA.
DR EMBL; AK303587; BAH13992.1; ALT_INIT; mRNA.
DR EMBL; AC244502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 1HXM; X-ray; 3.12 A; A/C/E/G=1-109.
DR PDBsum; 1HXM; -.
DR AlphaFoldDB; B7Z8K6; -.
DR SMR; B7Z8K6; -.
DR ComplexPortal; CPX-6582; Gamma-delta T cell receptor complex, TRGC1 variant.
DR ComplexPortal; CPX-6603; Gamma-delta T cell receptor complex, TRGC2 variant.
DR IMGT_GENE-DB; TRDC; -.
DR GlyGen; B7Z8K6; 2 sites.
DR BioMuta; TRDC; -.
DR MassIVE; B7Z8K6; -.
DR PeptideAtlas; B7Z8K6; -.
DR PRIDE; B7Z8K6; -.
DR ProteomicsDB; 6955; -.
DR GeneCards; TRDC; -.
DR HGNC; HGNC:12253; TRDC.
DR MIM; 186810; gene.
DR neXtProt; NX_B7Z8K6; -.
DR InParanoid; B7Z8K6; -.
DR OMA; YPKNVNI; -.
DR PhylomeDB; B7Z8K6; -.
DR PathwayCommons; B7Z8K6; -.
DR ChiTaRS; TRDC; human.
DR EvolutionaryTrace; B7Z8K6; -.
DR Pharos; B7Z8K6; Tdark.
DR PRO; PR:B7Z8K6; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; B7Z8K6; protein.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0042106; C:gamma-delta T cell receptor complex; IC:ComplexPortal.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IC:ComplexPortal.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0046629; P:gamma-delta T cell activation; IC:ComplexPortal.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
DR GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IC:ComplexPortal.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003597; Ig_C1-set.
DR Pfam; PF07654; C1-set; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Membrane; Receptor; Reference proteome;
KW T cell receptor; Transmembrane; Transmembrane helix.
FT CHAIN <1..153
FT /note="T cell receptor delta constant"
FT /id="PRO_0000393473"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 85..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 20..71
FT /evidence="ECO:0000269|PubMed:11459064,
FT ECO:0007744|PDB:1HXM"
FT NON_TER 1
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:1HXM"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1HXM"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1HXM"
SQ SEQUENCE 153 AA; 17085 MW; B1C4D262622929E4 CRC64;
SQPHTKPSVF VMKNGTNVAC LVKEFYPKDI RINLVSSKKI TEFDPAIVIS PSGKYNAVKL
GKYEDSNSVT CSVQHDNKTV HSTDFEVKTD STDHVKPKET ENTKQPSKSC HKPKAIVHTE
KVNMMSLTVL GLRMLFAKTV AVNFLLTAKL FFL
