TRGC2_HUMAN
ID TRGC2_HUMAN Reviewed; 189 AA.
AC P03986; A0A075B6R6;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=T cell receptor gamma constant 2 {ECO:0000303|Ref.4};
GN Name=TRGC2 {ECO:0000303|Ref.4};
GN Synonyms=TCRGC2 {ECO:0000312|HGNC:HGNC:12276};
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 [MRNA].
RX PubMed=3458221; DOI=10.1073/pnas.83.8.2619;
RA Dialynas D.P., Murre C., Quertermous T., Boss J.M., Leiden J.M.,
RA Seidman J.G., Strominger J.L.;
RT "Cloning and sequence analysis of complementary DNA encoding an aberrantly
RT rearranged human T-cell gamma chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2619-2623(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRGC2*06).
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., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., 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., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-110.
RX PubMed=2879283; DOI=10.1073/pnas.83.24.9596;
RA Lefranc M.P., Forster A., Rabbitts T.H.;
RT "Genetic polymorphism and exon changes of the constant regions of the human
RT T-cell rearranging gene gamma.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9596-9600(1986).
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]
RP X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 1-119.
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) gamma 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 TRGC2*06. {ECO:0000305}.
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DR EMBL; M13231; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC006033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M15002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A02141; RWHUGC.
DR PIR; A22340; A22340.
DR PDB; 1HXM; X-ray; 3.12 A; B/D/F/H=1-119.
DR PDBsum; 1HXM; -.
DR AlphaFoldDB; P03986; -.
DR SMR; P03986; -.
DR ComplexPortal; CPX-6603; Gamma-delta T cell receptor complex, TRGC2 variant.
DR IMGT_GENE-DB; TRGC2; -.
DR GlyGen; P03986; 5 sites.
DR BioMuta; TRGC2; -.
DR DMDM; 135528; -.
DR MassIVE; P03986; -.
DR PeptideAtlas; P03986; -.
DR PRIDE; P03986; -.
DR UCSC; uc064cxi.1; human.
DR GeneCards; TRGC2; -.
DR HGNC; HGNC:12276; TRGC2.
DR MIM; 615450; gene.
DR neXtProt; NX_P03986; -.
DR HOGENOM; CLU_077975_3_2_1; -.
DR InParanoid; P03986; -.
DR PhylomeDB; P03986; -.
DR PathwayCommons; P03986; -.
DR SignaLink; P03986; -.
DR EvolutionaryTrace; P03986; -.
DR Pharos; P03986; Tdark.
DR PRO; PR:P03986; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P03986; 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:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IC:ComplexPortal.
DR GO; GO:0046629; P:gamma-delta T cell activation; IC:ComplexPortal.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IC:ComplexPortal.
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; IPR003597; Ig_C1-set.
DR Pfam; PF07654; C1-set; 1.
DR SMART; SM00407; IGc1; 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; T cell receptor; Transmembrane; Transmembrane helix.
FT CHAIN <1..189
FT /note="T cell receptor gamma constant 2"
FT /id="PRO_0000184530"
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 10..104
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 32..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 119..120
FT /note="YN -> DS (in Ref. 1; M13231)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="T -> M (in Ref. 1; M13231)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="R -> G (in Ref. 1; M13231)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 28..39
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:1HXM"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1HXM"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1HXM"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1HXM"
SQ SEQUENCE 189 AA; 21698 MW; DAE7B5AEED04E94F CRC64;
DKQLDADVSP KPTIFLPSIA ETKLQKAGTY LCLLEKFFPD IIKIHWQEKK SNTILGSQEG
NTMKTNDTYM KFSWLTVPEE SLDKEHRCIV RHENNKNGID QEIIFPPIKT DVTTVDPKYN
YSKDANDVIT MDPKDNWSKD ANDTLLLQLT NTSAYYTYLL LLLKSVVYFA IITCCLLRRT
AFCCNGEKS
