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 27-MAR-2024, entry version 112. 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 octameric 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; A0A5B9; 1 site, No reported glycans. DR GlyGen; A0A5B9; 1 site. DR iPTMnet; A0A5B9; -. DR PhosphoSitePlus; A0A5B9; -. DR BioMuta; TRBC2; -. DR jPOST; A0A5B9; -. DR MassIVE; A0A5B9; -. DR PeptideAtlas; A0A5B9; -. DR ProteomicsDB; 1; -. DR ABCD; A0A5B9; 10 sequenced antibodies. DR UCSC; uc064itq.1; human. DR AGR; HGNC:12157; -. DR GeneCards; TRBC2; -. DR HGNC; HGNC:12157; TRBC2. DR HPA; ENSG00000211772; Tissue enriched (lymphoid). DR MIM; 615445; gene. DR neXtProt; NX_A0A5B9; -. DR HOGENOM; CLU_077975_0_1_1; -. DR InParanoid; A0A5B9; -. DR OMA; NISASAW; -. 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:0005886; C:plasma membrane; IDA:ComplexPortal. DR GO; GO:0002250; P:adaptive immune response; NAS:ComplexPortal. DR GO; GO:0046631; P:alpha-beta T cell activation; NAS:ComplexPortal. DR GO; GO:0050852; P:T cell receptor signaling pathway; NAS:ComplexPortal. DR CDD; cd05769; IgC1_TCR_beta; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR23411:SF32; T CELL RECEPTOR BETA CONSTANT 1-RELATED; 1. DR PANTHER; PTHR23411; TAPASIN; 1. DR Pfam; PF07654; C1-set; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; Immunoglobulin; 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 //