TRBC2_HUMAN
ID TRBC2_HUMAN Reviewed; 178 AA.
AC A0A5B9; A0A075B6S1;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=T cell receptor beta constant 2 {ECO:0000303|Ref.5};
GN Name=TRBC2 {ECO:0000303|Ref.5};
GN Synonyms=TCRBC2 {ECO:0000303|PubMed:8650574};
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 TRBC2*01).
RX PubMed=3860845; DOI=10.1073/pnas.82.15.5068;
RA Tunnacliffe A., Kefford R., Milstein C., Forster A., Rabbitts T.H.;
RT "Sequence and evolution of the human T-cell antigen receptor beta-chain
RT genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5068-5072(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE TRBC2*02).
RX PubMed=8650574; DOI=10.1126/science.272.5269.1755;
RA Rowen L., Koop B.F., Hood L.;
RT "The complete 685-kilobase DNA sequence of the human beta T cell receptor
RT locus.";
RL Science 272:1755-1762(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRBC2*03).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRBC2*01).
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP REVIEW ON T CELL REPERTOIRE DIVERSITY.
RX PubMed=15040585; DOI=10.1038/nri1292;
RA Nikolich-Zugich J., Slifka M.K., Messaoudi I.;
RT "The many important facets of T-cell repertoire diversity.";
RL Nat. Rev. Immunol. 4:123-132(2004).
RN [7]
RP REVIEW ON T CELL RECEPTOR-CD3 COMPLEX ASSEMBLY, AND SUBCELLULAR LOCATION.
RX PubMed=20452950; DOI=10.1101/cshperspect.a005140;
RA Wucherpfennig K.W., Gagnon E., Call M.J., Huseby E.S., Call M.E.;
RT "Structural biology of the T-cell receptor: insights into receptor
RT assembly, ligand recognition, and initiation of signaling.";
RL Cold Spring Harb. Perspect. Biol. 2:A005140-A005140(2010).
RN [8]
RP REVIEW ON T CELL RECEPTOR SIGNALING.
RX PubMed=23524462; DOI=10.1038/nri3403;
RA Brownlie R.J., Zamoyska R.;
RT "T cell receptor signalling networks: branched, diversified and bounded.";
RL Nat. Rev. Immunol. 13:257-269(2013).
RN [9]
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 [10]
RP REVIEW ON FUNCTION.
RX PubMed=25493333; DOI=10.1146/annurev-immunol-032414-112334;
RA Rossjohn J., Gras S., Miles J.J., Turner S.J., Godfrey D.I., McCluskey J.;
RT "T cell antigen receptor recognition of antigen-presenting molecules.";
RL Annu. Rev. Immunol. 33:169-200(2015).
RN [11] {ECO:0007744|PDB:1AO7}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=8906788; DOI=10.1038/384134a0;
RA Garboczi D.N., Ghosh P., Utz U., Fan Q.R., Biddison W.E., Wiley D.C.;
RT "Structure of the complex between human T-cell receptor, viral peptide and
RT HLA-A2.";
RL Nature 384:134-141(1996).
RN [12] {ECO:0007744|PDB:1BD2}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=9586631; DOI=10.1016/s1074-7613(00)80546-4;
RA Ding Y.H., Smith K.J., Garboczi D.N., Utz U., Biddison W.E., Wiley D.C.;
RT "Two human T cell receptors bind in a similar diagonal mode to the HLA-
RT A2/Tax peptide complex using different TCR amino acids.";
RL Immunity 8:403-411(1998).
RN [13] {ECO:0007744|PDB:2EYR, ECO:0007744|PDB:2EYS, ECO:0007744|PDB:2EYT}
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=16505140; DOI=10.1084/jem.20051777;
RA Kjer-Nielsen L., Borg N.A., Pellicci D.G., Beddoe T., Kostenko L.,
RA Clements C.S., Williamson N.A., Smyth M.J., Besra G.S., Reid H.H.,
RA Bharadwaj M., Godfrey D.I., Rossjohn J., McCluskey J.;
RT "A structural basis for selection and cross-species reactivity of the semi-
RT invariant NKT cell receptor in CD1d/glycolipid recognition.";
RL J. Exp. Med. 203:661-673(2006).
RN [14] {ECO:0007744|PDB:3O8X, ECO:0007744|PDB:3O9W}
RP X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 1-128, AND DISULFIDE BONDS.
RX PubMed=20921281; DOI=10.1084/jem.20101335;
RA Li Y., Girardi E., Wang J., Yu E.D., Painter G.F., Kronenberg M.,
RA Zajonc D.M.;
RT "The Valpha14 invariant natural killer T cell TCR forces microbial
RT glycolipids and CD1d into a conserved binding mode.";
RL J. Exp. Med. 207:2383-2393(2010).
RN [15] {ECO:0007744|PDB:3KXF}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=20483993; DOI=10.1073/pnas.1004926107;
RA Burrows S.R., Chen Z., Archbold J.K., Tynan F.E., Beddoe T.,
RA Kjer-Nielsen L., Miles J.J., Khanna R., Moss D.J., Liu Y.C., Gras S.,
RA Kostenko L., Brennan R.M., Clements C.S., Brooks A.G., Purcell A.W.,
RA McCluskey J., Rossjohn J.;
RT "Hard wiring of T cell receptor specificity for the major
RT histocompatibility complex is underpinned by TCR adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10608-10613(2010).
RN [16] {ECO:0007744|PDB:3TVM}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-128, AND DISULFIDE BONDS.
RX PubMed=22195564; DOI=10.1016/j.chembiol.2011.10.015;
RA Tyznik A.J., Farber E., Girardi E., Birkholz A., Li Y., Chitale S., So R.,
RA Arora P., Khurana A., Wang J., Porcelli S.A., Zajonc D.M., Kronenberg M.,
RA Howell A.R.;
RT "Glycolipids that elicit IFN-gamma-biased responses from natural killer T
RT cells.";
RL Chem. Biol. 18:1620-1630(2011).
RN [17] {ECO:0007744|PDB:3O6F}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-130, AND DISULFIDE BONDS.
RX PubMed=21297580; DOI=10.1038/emboj.2011.21;
RA Yin Y., Li Y., Kerzic M.C., Martin R., Mariuzza R.A.;
RT "Structure of a TCR with high affinity for self-antigen reveals basis for
RT escape from negative selection.";
RL EMBO J. 30:1137-1148(2011).
RN [18] {ECO:0007744|PDB:3QUX}
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 1-128, AND DISULFIDE BONDS.
RX PubMed=21552205; DOI=10.1038/emboj.2011.145;
RA Aspeslagh S., Li Y., Yu E.D., Pauwels N., Trappeniers M., Girardi E.,
RA Decruy T., Van Beneden K., Venken K., Drennan M., Leybaert L., Wang J.,
RA Franck R.W., Van Calenbergh S., Zajonc D.M., Elewaut D.;
RT "Galactose-modified iNKT cell agonists stabilized by an induced fit of CD1d
RT prevent tumour metastasis.";
RL EMBO J. 30:2294-2305(2011).
RN [19] {ECO:0007744|PDB:3TA3}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-128, AND DISULFIDE BONDS.
RX PubMed=22069376; DOI=10.1371/journal.pbio.1001189;
RA Girardi E., Yu E.D., Li Y., Tarumoto N., Pei B., Wang J., Illarionov P.,
RA Kinjo Y., Kronenberg M., Zajonc D.M.;
RT "Unique interplay between sugar and lipid in determining the antigenic
RT potency of bacterial antigens for NKT cells.";
RL PLoS Biol. 9:E1001189-E1001189(2011).
RN [20] {ECO:0007744|PDB:3T0E}
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 1-130, AND DISULFIDE BONDS.
RX PubMed=22431638; DOI=10.1073/pnas.1118801109;
RA Yin Y., Wang X.X., Mariuzza R.A.;
RT "Crystal structure of a complete ternary complex of T-cell receptor,
RT peptide-MHC, and CD4.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5405-5410(2012).
RN [21] {ECO:0007744|PDB:4MVB, ECO:0007744|PDB:4MXQ, ECO:0007744|PDB:4N0C, ECO:0007744|PDB:4N5E, ECO:0007744|PDB:4NHU}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RA Birnbaum M.E., Adams J.J., Garcia K.C.;
RT "Interrogating TCR Signal Strength and Cross-Reactivity by Yeast Display of
RT pMHC.";
RL Submitted (OCT-2013) to the PDB data bank.
RN [22] {ECO:0007744|PDB:4P4K}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=24995984; DOI=10.1016/j.cell.2014.04.048;
RA Clayton G.M., Wang Y., Crawford F., Novikov A., Wimberly B.T., Kieft J.S.,
RA Falta M.T., Bowerman N.A., Marrack P., Fontenot A.P., Dai S., Kappler J.W.;
RT "Structural basis of chronic beryllium disease: linking allergic
RT hypersensitivity and autoimmunity.";
RL Cell 158:132-142(2014).
RN [23] {ECO:0007744|PDB:4C56}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=25015819; DOI=10.4049/jimmunol.1401268;
RA Rodstrom K.E., Elbing K., Lindkvist-Petersson K.;
RT "Structure of the superantigen staphylococcal enterotoxin B in complex with
RT TCR and peptide-MHC demonstrates absence of TCR-peptide contacts.";
RL J. Immunol. 193:1998-2004(2014).
RN [24] {ECO:0007744|PDB:4ONH}
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=25298532; DOI=10.1073/pnas.1408549111;
RA Roy S., Ly D., Li N.S., Altman J.D., Piccirilli J.A., Moody D.B.,
RA Adams E.J.;
RT "Molecular basis of mycobacterial lipid antigen presentation by CD1c and
RT its recognition by alphabeta T cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E4648-E4657(2014).
RN [25] {ECO:0007744|PDB:4Y16, ECO:0007744|PDB:4Y2D, ECO:0007744|PDB:4Y4F, ECO:0007744|PDB:4Y4H, ECO:0007744|PDB:4Y4K}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-128, AND DISULFIDE BONDS.
RX PubMed=26018083; DOI=10.1074/jbc.m115.654814;
RA Birkholz A., Nemcovic M., Yu E.D., Girardi E., Wang J., Khurana A.,
RA Pauwels N., Farber E., Chitale S., Franck R.W., Tsuji M., Howell A.,
RA Van Calenbergh S., Kronenberg M., Zajonc D.M.;
RT "Lipid and Carbohydrate Modifications of alpha-Galactosylceramide
RT Differently Influence Mouse and Human Type I Natural Killer T Cell
RT Activation.";
RL J. Biol. Chem. 290:17206-17217(2015).
RN [26] {ECO:0007744|PDB:4ZAK}
RP X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 21-128, AND DISULFIDE BONDS.
RX PubMed=26078271; DOI=10.4049/jimmunol.1500070;
RA Birkholz A.M., Girardi E., Wingender G., Khurana A., Wang J., Zhao M.,
RA Zahner S., Illarionov P.A., Wen X., Li M., Yuan W., Porcelli S.A.,
RA Besra G.S., Zajonc D.M., Kronenberg M.;
RT "A Novel Glycolipid Antigen for NKT Cells That Preferentially Induces IFN-
RT gamma Production.";
RL J. Immunol. 195:924-933(2015).
RN [27] {ECO:0007744|PDB:4UDT, ECO:0007744|PDB:4UDU}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=26147596; DOI=10.1371/journal.pone.0131988;
RA Rodstrom K.E., Regenthal P., Lindkvist-Petersson K.;
RT "Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the
RT Role of TCR Loop Positioning in Superantigen Recognition.";
RL PLoS ONE 10:e0131988-e0131988(2015).
RN [28] {ECO:0007744|PDB:5EU6}
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=26917722; DOI=10.1074/jbc.m115.707414;
RA Bianchi V., Bulek A., Fuller A., Lloyd A., Attaf M., Rizkallah P.J.,
RA Dolton G., Sewell A.K., Cole D.K.;
RT "A Molecular Switch Abrogates Glycoprotein 100 (gp100) T-cell Receptor
RT (TCR) Targeting of a Human Melanoma Antigen.";
RL J. Biol. Chem. 291:8951-8959(2016).
RN [29] {ECO:0007744|PDB:5HYJ}
RP X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=27183386; DOI=10.1172/jci88165;
RA Stadinski B.D., Obst R., Huseby E.S.;
RT "A 'hotspot' for autoimmune T cells in type 1 diabetes.";
RL J. Clin. Invest. 126:2040-2042(2016).
RN [30] {ECO:0007744|PDB:5C07, ECO:0007744|PDB:5C08, ECO:0007744|PDB:5C09, ECO:0007744|PDB:5C0A, ECO:0007744|PDB:5C0B, ECO:0007744|PDB:5C0C}
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=27183389; DOI=10.1172/jci85679;
RA Cole D.K., Bulek A.M., Dolton G., Schauenberg A.J., Szomolay B.,
RA Rittase W., Trimby A., Jothikumar P., Fuller A., Skowera A., Rossjohn J.,
RA Zhu C., Miles J.J., Peakman M., Wooldridge L., Rizkallah P.J., Sewell A.K.;
RT "Hotspot autoimmune T cell receptor binding underlies pathogen and insulin
RT peptide cross-reactivity.";
RL J. Clin. Invest. 126:2191-2204(2016).
RN [31] {ECO:0007744|PDB:4WW1, ECO:0007744|PDB:4WW2, ECO:0007744|PDB:4WWK}
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=26875526; DOI=10.1038/ncomms10570;
RA Le Nours J., Praveena T., Pellicci D.G., Gherardin N.A., Ross F.J.,
RA Lim R.T., Besra G.S., Keshipeddy S., Richardson S.K., Howell A.R., Gras S.,
RA Godfrey D.I., Rossjohn J., Uldrich A.P.;
RT "Atypical natural killer T-cell receptor recognition of CD1d-lipid
RT antigens.";
RL Nat. Commun. 7:10570-10570(2016).
RN [32] {ECO:0007744|PDB:5HHM, ECO:0007744|PDB:5HHO}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=27036003; DOI=10.1073/pnas.1603106113;
RA Valkenburg S.A., Josephs T.M., Clemens E.B., Grant E.J., Nguyen T.H.,
RA Wang G.C., Price D.A., Miller A., Tong S.Y., Thomas P.G., Doherty P.C.,
RA Rossjohn J., Gras S., Kedzierska K.;
RT "Molecular basis for universal HLA-A*0201-restricted CD8+ T-cell immunity
RT against influenza viruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:4440-4445(2016).
RN [33] {ECO:0007744|PDB:5BRZ, ECO:0007744|PDB:5BS0}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=26758806; DOI=10.1038/srep18851;
RA Raman M.C., Rizkallah P.J., Simmons R., Donnellan Z., Dukes J., Bossi G.,
RA Le Provost G.S., Todorov P., Baston E., Hickman E., Mahon T., Hassan N.,
RA Vuidepot A., Sami M., Cole D.K., Jakobsen B.K.;
RT "Direct molecular mimicry enables off-target cardiovascular toxicity by an
RT enhanced affinity TCR designed for cancer immunotherapy.";
RL Sci. Rep. 6:18851-18851(2016).
RN [34] {ECO:0007744|PDB:5FK9, ECO:0007744|PDB:5FKA}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=27180909; DOI=10.1038/srep25796;
RA Rodstrom K.E., Regenthal P., Bahl C., Ford A., Baker D.,
RA Lindkvist-Petersson K.;
RT "Two common structural motifs for TCR recognition by staphylococcal
RT enterotoxins.";
RL Sci. Rep. 6:25796-25796(2016).
RN [35] {ECO:0007744|PDB:5KS9, ECO:0007744|PDB:5KSA, ECO:0007744|PDB:5KSB}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-129, AND DISULFIDE BONDS.
RX PubMed=27568928; DOI=10.1016/j.str.2016.07.010;
RA Petersen J., Kooy-Winkelaar Y., Loh K.L., Tran M., van Bergen J.,
RA Koning F., Rossjohn J., Reid H.H.;
RT "Diverse T cell receptor gene usage in HLA-DQ8-associated celiac disease
RT converges into a consensus binding solution.";
RL Structure 24:1643-1657(2016).
CC -!- FUNCTION: Constant region of T cell receptor (TR) beta chain
CC (PubMed:24600447). Alpha-beta T cell receptors are antigen specific
CC receptors which are essential to the immune response and are present on
CC the cell surface of T lymphocytes. Recognize peptide-major
CC histocompatibility (MH) (pMH) complexes that are displayed by antigen
CC presenting cells (APC), a prerequisite for efficient T cell adaptive
CC immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR
CC to pMH complex initiates TR-CD3 clustering on the cell surface and
CC intracellular activation of LCK that phosphorylates the ITAM motifs of
CC CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn,
CC ZAP70 phosphorylates LAT, which recruits numerous signaling molecules
CC to form the LAT signalosome. The LAT signalosome propagates signal
CC branching to three major signaling pathways, the calcium, the mitogen-
CC activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-
CC B (NF-kB) pathways, leading to the mobilization of transcription
CC factors that are critical for gene expression and essential for T cell
CC growth and differentiation (PubMed:23524462). The T cell repertoire is
CC generated in the thymus, by V-(D)-J rearrangement. This repertoire is
CC then shaped by intrathymic selection events to generate a peripheral T
CC cell pool of self-MH restricted, non-autoaggressive T cells. Post-
CC thymic interaction of alpha-beta TR with the pMH complexes shapes TR
CC structural and functional avidity (PubMed:15040585).
CC {ECO:0000303|PubMed:15040585, ECO:0000303|PubMed:23524462,
CC ECO:0000303|PubMed:24600447, ECO:0000303|PubMed:25493333}.
CC -!- SUBUNIT: Alpha-beta TR is a heterodimer composed of an alpha and beta
CC chain; disulfide-linked. The alpha-beta TR is associated with the
CC transmembrane signaling CD3 coreceptor proteins to form the TR-CD3 (TcR
CC or TCR). The assembly of alpha-beta TR heterodimers with CD3 occurs in
CC the endoplasmic reticulum where a single alpha-beta TR heterodimer
CC associates with one CD3D-CD3E heterodimer, one CD3G-CD3E heterodimer
CC and one CD247 homodimer forming a stable octomeric structure. CD3D-CD3E
CC and CD3G-CD3E heterodimers preferentially associate with TR alpha and
CC TR beta chains, respectively. The association of the CD247 homodimer is
CC the last step of TcR assembly in the endoplasmic reticulum and is
CC required for transport to the cell surface.
CC {ECO:0000303|PubMed:20452950}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:20452950}.
CC -!- DOMAIN: The connecting peptide (CP) domain is essential for signal
CC transmission in response to antigenic stimulation, likely downstream
CC from ZAP70 recruitment. {ECO:0000250|UniProtKB:P01850}.
CC -!- DOMAIN: The TM domain mediates the interaction with the CD3 subunits.
CC {ECO:0000250|UniProtKB:P01850}.
CC -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele TRBC2*03. {ECO:0000305}.
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DR EMBL; M12888; AAA60662.1; -; Genomic_DNA.
DR EMBL; L36092; AAC80214.1; -; Genomic_DNA.
DR EMBL; AC245427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471198; EAW51905.1; -; Genomic_DNA.
DR PDB; 1AO7; X-ray; 2.60 A; E=1-129.
DR PDB; 1BD2; X-ray; 2.50 A; E=1-129.
DR PDB; 2EYR; X-ray; 2.40 A; B=1-129.
DR PDB; 2EYS; X-ray; 2.21 A; B=1-129.
DR PDB; 2EYT; X-ray; 2.60 A; B/D=1-129.
DR PDB; 3KXF; X-ray; 3.10 A; E/H/O/P=1-129.
DR PDB; 3O6F; X-ray; 2.80 A; D/H=1-130.
DR PDB; 3O8X; X-ray; 2.74 A; D=13-128.
DR PDB; 3O9W; X-ray; 2.80 A; D=13-128.
DR PDB; 3QUX; X-ray; 2.91 A; D=13-128.
DR PDB; 3T0E; X-ray; 4.00 A; D=1-130.
DR PDB; 3TA3; X-ray; 2.70 A; D=13-128.
DR PDB; 3TVM; X-ray; 2.80 A; D/H=13-128.
DR PDB; 4C56; X-ray; 2.90 A; B/H=1-129.
DR PDB; 4MVB; X-ray; 3.09 A; B=1-129.
DR PDB; 4MXQ; X-ray; 2.60 A; D=1-129.
DR PDB; 4N0C; X-ray; 2.90 A; D/H=1-129.
DR PDB; 4N5E; X-ray; 3.06 A; D=1-129.
DR PDB; 4NHU; X-ray; 2.90 A; B/D=1-147.
DR PDB; 4ONH; X-ray; 3.01 A; B=1-129.
DR PDB; 4P4K; X-ray; 2.80 A; D/H=1-129.
DR PDB; 4UDT; X-ray; 1.35 A; B=1-129.
DR PDB; 4UDU; X-ray; 2.50 A; B=1-129.
DR PDB; 4WW1; X-ray; 1.38 A; B=1-129.
DR PDB; 4WW2; X-ray; 2.48 A; B=1-129.
DR PDB; 4WWK; X-ray; 3.10 A; B=1-129.
DR PDB; 4Y16; X-ray; 2.60 A; D=13-128.
DR PDB; 4Y2D; X-ray; 3.05 A; D/H=13-128.
DR PDB; 4Y4F; X-ray; 3.19 A; D/H=13-128.
DR PDB; 4Y4H; X-ray; 3.10 A; D/H=13-128.
DR PDB; 4Y4K; X-ray; 2.90 A; D=13-128.
DR PDB; 4ZAK; X-ray; 2.82 A; D=18-128.
DR PDB; 5BRZ; X-ray; 2.62 A; E=1-129.
DR PDB; 5BS0; X-ray; 2.40 A; E=1-129.
DR PDB; 5C07; X-ray; 2.11 A; E/J=1-129.
DR PDB; 5C08; X-ray; 2.33 A; E/J=1-129.
DR PDB; 5C09; X-ray; 2.48 A; E/J=1-129.
DR PDB; 5C0A; X-ray; 2.46 A; E/J=1-129.
DR PDB; 5C0B; X-ray; 2.03 A; E/J=1-129.
DR PDB; 5C0C; X-ray; 1.97 A; E/J=1-129.
DR PDB; 5EU6; X-ray; 2.02 A; E=1-129.
DR PDB; 5FK9; X-ray; 3.10 A; B=1-129.
DR PDB; 5FKA; X-ray; 2.40 A; B=1-129.
DR PDB; 5HHM; X-ray; 2.50 A; E/J=1-129.
DR PDB; 5HHO; X-ray; 2.95 A; E=1-129.
DR PDB; 5HYJ; X-ray; 3.06 A; E/J=1-129.
DR PDB; 5KS9; X-ray; 2.55 A; F/H=1-129.
DR PDB; 5KSA; X-ray; 2.00 A; D=1-129.
DR PDB; 5KSB; X-ray; 2.90 A; F/H=1-129.
DR PDB; 6CPH; X-ray; 1.70 A; E=1-129.
DR PDB; 6CQL; X-ray; 2.40 A; E=1-129.
DR PDB; 6CQQ; X-ray; 2.80 A; E/J=1-129.
DR PDB; 6CQR; X-ray; 3.04 A; E/J=1-129.
DR PDB; 6MIV; Other; 2.05 A; D=21-128.
DR PDB; 6MIY; X-ray; 2.75 A; D/H=21-128.
DR PDB; 6MJ4; X-ray; 2.00 A; D=21-128.
DR PDB; 6MJ6; X-ray; 2.45 A; D=21-128.
DR PDB; 6MJA; X-ray; 2.35 A; D=21-128.
DR PDB; 6MJI; X-ray; 2.30 A; D=21-128.
DR PDB; 6MJJ; X-ray; 1.93 A; D=21-128.
DR PDB; 6MJQ; X-ray; 3.00 A; D/H=21-128.
DR PDB; 7NDT; X-ray; 3.00 A; EEE/JJJ=1-129.
DR PDBsum; 1AO7; -.
DR PDBsum; 1BD2; -.
DR PDBsum; 2EYR; -.
DR PDBsum; 2EYS; -.
DR PDBsum; 2EYT; -.
DR PDBsum; 3KXF; -.
DR PDBsum; 3O6F; -.
DR PDBsum; 3O8X; -.
DR PDBsum; 3O9W; -.
DR PDBsum; 3QUX; -.
DR PDBsum; 3T0E; -.
DR PDBsum; 3TA3; -.
DR PDBsum; 3TVM; -.
DR PDBsum; 4C56; -.
DR PDBsum; 4MVB; -.
DR PDBsum; 4MXQ; -.
DR PDBsum; 4N0C; -.
DR PDBsum; 4N5E; -.
DR PDBsum; 4NHU; -.
DR PDBsum; 4ONH; -.
DR PDBsum; 4P4K; -.
DR PDBsum; 4UDT; -.
DR PDBsum; 4UDU; -.
DR PDBsum; 4WW1; -.
DR PDBsum; 4WW2; -.
DR PDBsum; 4WWK; -.
DR PDBsum; 4Y16; -.
DR PDBsum; 4Y2D; -.
DR PDBsum; 4Y4F; -.
DR PDBsum; 4Y4H; -.
DR PDBsum; 4Y4K; -.
DR PDBsum; 4ZAK; -.
DR PDBsum; 5BRZ; -.
DR PDBsum; 5BS0; -.
DR PDBsum; 5C07; -.
DR PDBsum; 5C08; -.
DR PDBsum; 5C09; -.
DR PDBsum; 5C0A; -.
DR PDBsum; 5C0B; -.
DR PDBsum; 5C0C; -.
DR PDBsum; 5EU6; -.
DR PDBsum; 5FK9; -.
DR PDBsum; 5FKA; -.
DR PDBsum; 5HHM; -.
DR PDBsum; 5HHO; -.
DR PDBsum; 5HYJ; -.
DR PDBsum; 5KS9; -.
DR PDBsum; 5KSA; -.
DR PDBsum; 5KSB; -.
DR PDBsum; 6CPH; -.
DR PDBsum; 6CQL; -.
DR PDBsum; 6CQQ; -.
DR PDBsum; 6CQR; -.
DR PDBsum; 6MIV; -.
DR PDBsum; 6MIY; -.
DR PDBsum; 6MJ4; -.
DR PDBsum; 6MJ6; -.
DR PDBsum; 6MJA; -.
DR PDBsum; 6MJI; -.
DR PDBsum; 6MJJ; -.
DR PDBsum; 6MJQ; -.
DR PDBsum; 7NDT; -.
DR AlphaFoldDB; A0A5B9; -.
DR SMR; A0A5B9; -.
DR ComplexPortal; CPX-6482; Alpha-beta T cell receptor complex, TRBC2 variant.
DR IMGT_GENE-DB; TRBC2; -.
DR GlyGen; A0A5B9; 1 site.
DR iPTMnet; A0A5B9; -.
DR PhosphoSitePlus; A0A5B9; -.
DR BioMuta; TRBC2; -.
DR jPOST; A0A5B9; -.
DR MassIVE; A0A5B9; -.
DR PeptideAtlas; A0A5B9; -.
DR PRIDE; A0A5B9; -.
DR ProteomicsDB; 1; -.
DR ABCD; A0A5B9; 10 sequenced antibodies.
DR UCSC; uc064itq.1; human.
DR GeneCards; TRBC2; -.
DR HGNC; HGNC:12157; TRBC2.
DR MIM; 615445; gene.
DR neXtProt; NX_A0A5B9; -.
DR HOGENOM; CLU_077975_0_1_1; -.
DR InParanoid; A0A5B9; -.
DR OMA; KFLYIML; -.
DR PhylomeDB; A0A5B9; -.
DR PathwayCommons; A0A5B9; -.
DR ChiTaRS; TRBC2; human.
DR EvolutionaryTrace; A0A5B9; -.
DR Pharos; A0A5B9; Tdark.
DR PRO; PR:A0A5B9; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A0A5B9; protein.
DR GO; GO:0042105; C:alpha-beta T cell receptor complex; IPI:ComplexPortal.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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; IDA: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:0046631; P:alpha-beta T cell activation; 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: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; 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..178
FT /note="T cell receptor beta constant 2"
FT /id="PRO_0000393471"
FT TRANSMEM 145..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 8..117
FT /note="Ig-like C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 130..144
FT /note="Connecting peptide"
FT /evidence="ECO:0000250|UniProtKB:P01850"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 30..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:16505140, ECO:0000269|PubMed:20483993,
FT ECO:0000269|PubMed:20921281, ECO:0000269|PubMed:21297580,
FT ECO:0000269|PubMed:21552205, ECO:0000269|PubMed:22069376,
FT ECO:0000269|PubMed:22195564, ECO:0000269|PubMed:22431638,
FT ECO:0000269|PubMed:24995984, ECO:0000269|PubMed:25015819,
FT ECO:0000269|PubMed:25298532, ECO:0000269|PubMed:26018083,
FT ECO:0000269|PubMed:26078271, ECO:0000269|PubMed:26147596,
FT ECO:0000269|PubMed:26758806, ECO:0000269|PubMed:26875526,
FT ECO:0000269|PubMed:26917722, ECO:0000269|PubMed:27036003,
FT ECO:0000269|PubMed:27180909, ECO:0000269|PubMed:27183386,
FT ECO:0000269|PubMed:27183389, ECO:0000269|PubMed:27568928,
FT ECO:0000269|PubMed:8906788, ECO:0000269|PubMed:9586631,
FT ECO:0000269|Ref.21, ECO:0007744|PDB:1AO7,
FT ECO:0007744|PDB:1BD2, ECO:0007744|PDB:2EYR,
FT ECO:0007744|PDB:2EYS, ECO:0007744|PDB:2EYT,
FT ECO:0007744|PDB:3KXF, ECO:0007744|PDB:3O6F,
FT ECO:0007744|PDB:3O8X, ECO:0007744|PDB:3O9W,
FT ECO:0007744|PDB:3QUX, ECO:0007744|PDB:3T0E,
FT ECO:0007744|PDB:3TA3, ECO:0007744|PDB:3TVM,
FT ECO:0007744|PDB:4C56, ECO:0007744|PDB:4MVB,
FT ECO:0007744|PDB:4MXQ, ECO:0007744|PDB:4N0C,
FT ECO:0007744|PDB:4N5E, ECO:0007744|PDB:4NHU,
FT ECO:0007744|PDB:4ONH, ECO:0007744|PDB:4P4K,
FT ECO:0007744|PDB:4UDT, ECO:0007744|PDB:4UDU,
FT ECO:0007744|PDB:4WW1, ECO:0007744|PDB:4WW2,
FT ECO:0007744|PDB:4Y16, ECO:0007744|PDB:4Y2D,
FT ECO:0007744|PDB:4Y4F, ECO:0007744|PDB:4Y4H,
FT ECO:0007744|PDB:4Y4K, ECO:0007744|PDB:4ZAK,
FT ECO:0007744|PDB:5BRZ, ECO:0007744|PDB:5BS0,
FT ECO:0007744|PDB:5C07, ECO:0007744|PDB:5C08,
FT ECO:0007744|PDB:5C09, ECO:0007744|PDB:5C0A,
FT ECO:0007744|PDB:5C0B, ECO:0007744|PDB:5C0C,
FT ECO:0007744|PDB:5EU6, ECO:0007744|PDB:5FK9,
FT ECO:0007744|PDB:5FKA, ECO:0007744|PDB:5HHM,
FT ECO:0007744|PDB:5HHO, ECO:0007744|PDB:5HYJ,
FT ECO:0007744|PDB:5KS9, ECO:0007744|PDB:5KSA,
FT ECO:0007744|PDB:5KSB"
FT DISULFID 130
FT /note="Interchain (with C-94 in TRAC)"
FT /evidence="ECO:0000250|UniProtKB:P01850"
FT CONFLICT 9
FT /note="K -> E (in Ref. 2; AAC80214, 1; AAA60662 and 4;
FT EAW51905)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:4UDT"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 24..38
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4WW1"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:4UDT"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6MJ6"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:4UDT"
SQ SEQUENCE 178 AA; 19968 MW; AADCED8ADBCAA89E CRC64;
DLKNVFPPKV AVFEPSEAEI SHTQKATLVC LATGFYPDHV ELSWWVNGKE VHSGVSTDPQ
PLKEQPALND SRYCLSSRLR VSATFWQNPR NHFRCQVQFY GLSENDEWTQ DRAKPVTQIV
SAEAWGRADC GFTSESYQQG VLSATILYEI LLGKATLYAV LVSALVLMAM VKRKDSRG
