TRGC1_HUMAN
ID TRGC1_HUMAN Reviewed; 173 AA.
AC P0CF51; A0A075B6Q9;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=T cell receptor gamma constant 1 {ECO:0000303|Ref.3};
GN Name=TRGC1 {ECO:0000303|Ref.3};
GN Synonyms=TCRGC1 {ECO:0000312|HGNC:HGNC:12275};
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 TRGC1*01).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRGC1*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., 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 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:4LFH, ECO:0007744|PDB:4LHU}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-122.
RX PubMed=24076636; DOI=10.1038/ni.2713;
RA Uldrich A.P., Le Nours J., Pellicci D.G., Gherardin N.A., McPherson K.G.,
RA Lim R.T., Patel O., Beddoe T., Gras S., Rossjohn J., Godfrey D.I.;
RT "CD1d-lipid antigen recognition by the gammadelta TCR.";
RL Nat. Immunol. 14:1137-1145(2013).
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 TRGC1*01. {ECO:0000305}.
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DR EMBL; M14998; AAA75392.1; -; Genomic_DNA.
DR EMBL; M14996; AAA75392.1; JOINED; Genomic_DNA.
DR EMBL; M14997; AAA75392.1; JOINED; Genomic_DNA.
DR EMBL; AC006033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 4LFH; X-ray; 2.30 A; G=1-122.
DR PDB; 4LHU; X-ray; 2.87 A; G=1-122.
DR PDBsum; 4LFH; -.
DR PDBsum; 4LHU; -.
DR AlphaFoldDB; P0CF51; -.
DR SMR; P0CF51; -.
DR ComplexPortal; CPX-6582; Gamma-delta T cell receptor complex, TRGC1 variant.
DR IMGT_GENE-DB; TRGC1; -.
DR GlyGen; P0CF51; 4 sites.
DR iPTMnet; P0CF51; -.
DR PhosphoSitePlus; P0CF51; -.
DR BioMuta; TRGC1; -.
DR PeptideAtlas; P0CF51; -.
DR PRIDE; P0CF51; -.
DR ProteomicsDB; 52442; -.
DR UCSC; uc064cxn.1; human.
DR GeneCards; TRGC1; -.
DR HGNC; HGNC:12275; TRGC1.
DR MIM; 186970; gene.
DR neXtProt; NX_P0CF51; -.
DR HOGENOM; CLU_077975_3_2_1; -.
DR InParanoid; P0CF51; -.
DR PhylomeDB; P0CF51; -.
DR SignaLink; P0CF51; -.
DR Pharos; P0CF51; Tdark.
DR PRO; PR:P0CF51; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P0CF51; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
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:0050852; P:T cell receptor signaling pathway; IC:ComplexPortal.
DR DisProt; DP01967; -.
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..173
FT /note="T cell receptor gamma constant 1"
FT /id="PRO_0000393472"
FT TRANSMEM 139..161
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 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 135
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 NON_TER 1
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:4LFH"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:4LFH"
FT STRAND 26..40
FT /evidence="ECO:0007829|PDB:4LFH"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:4LFH"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4LHU"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4LFH"
FT STRAND 68..78
FT /evidence="ECO:0007829|PDB:4LFH"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4LFH"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4LHU"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4LFH"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4LFH"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4LFH"
SQ SEQUENCE 173 AA; 19804 MW; 67C65AF5C03D33BB CRC64;
DKQLDADVSP KPTIFLPSIA ETKLQKAGTY LCLLEKFFPD VIKIHWQEKK SNTILGSQEG
NTMKTNDTYM KFSWLTVPEK SLDKEHRCIV RHENNKNGVD QEIIFPPIKT DVITMDPKDN
CSKDANDTLL LQLTNTSAYY MYLLLLLKSV VYFAIITCCL LRRTAFCCNG EKS
