TRBC1_HUMAN
ID TRBC1_HUMAN Reviewed; 176 AA.
AC P01850; A0A0J9YYE9; A0A5B8; A6NH51;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=T cell receptor beta constant 1 {ECO:0000303|Ref.7};
GN Name=TRBC1 {ECO:0000303|Ref.7};
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] (IMGT ALLELE TRBC1*01).
RX PubMed=6336315; DOI=10.1038/308145a0;
RA Yanagi Y., Yoshikai Y., Leggett K., Clark S.P., Aleksander I., Mak T.W.;
RT "A human T cell-specific cDNA clone encodes a protein having extensive
RT homology to immunoglobulin chains.";
RL Nature 308:145-149(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE TRBC1*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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE TRBC1*01).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRBC1*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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRBC1*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 [6]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF GLN-139.
RX PubMed=9382891; DOI=10.1084/jem.186.11.1933;
RA Baeckstroem B.T., Hausmann B.T., Palmer E.;
RT "Signaling efficiency of the T cell receptor controlled by a single amino
RT acid in the beta chain constant region.";
RL J. Exp. Med. 186:1933-1938(1997).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
RP DISULFIDE BOND, SUBUNIT, MUTAGENESIS OF VAL-162, AND DOMAIN.
RX PubMed=27791034; DOI=10.1073/pnas.1611445113;
RA Krshnan L., Park S., Im W., Call M.J., Call M.E.;
RT "A conserved alphabeta transmembrane interface forms the core of a compact
RT T-cell receptor-CD3 structure within the membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E6649-E6658(2016).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-129 IN COMPLEX WITH HLA-A/B2M
RP HETERODIMER AND TRAC.
RX PubMed=12796775; DOI=10.1038/ni942;
RA Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I., Jones E.Y.;
RT "A structural basis for immunodominant human T cell receptor recognition.";
RL Nat. Immunol. 4:657-663(2003).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-129 IN COMPLEX WITH HLA-B/B2M
RP HETERODIMER AND TRAC, AND DISULFIDE BOND.
RX PubMed=19167249; DOI=10.1016/j.immuni.2008.11.011;
RA Gras S., Burrows S.R., Kjer-Nielsen L., Clements C.S., Liu Y.C.,
RA Sullivan L.C., Bell M.J., Brooks A.G., Purcell A.W., McCluskey J.,
RA Rossjohn J.;
RT "The shaping of T cell receptor recognition by self-tolerance.";
RL Immunity 30:193-203(2009).
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:9382891, PubMed:23524462). The T
CC cell repertoire is generated in the thymus, by V-(D)-J rearrangement.
CC This repertoire is then shaped by intrathymic selection events to
CC generate a peripheral T cell pool of self-MH restricted, non-
CC autoaggressive T cells. Post-thymic interaction of alpha-beta TR with
CC the pMH complexes shapes TR structural and functional avidity
CC (PubMed:15040585). {ECO:0000269|PubMed:9382891,
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:0000269|PubMed:27791034, 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:0000269|PubMed:9382891}.
CC -!- DOMAIN: The TM domain mediates the interaction with the CD3 subunits.
CC {ECO:0000269|PubMed:27791034}.
CC -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele TRBC1*01. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA25134.1; Type=Miscellaneous discrepancy; Note=Chimeric mRNA corresponding to regions V, J and C of T cell receptor (TR) alpha chain.; Evidence={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; X00437; CAA25134.1; ALT_SEQ; mRNA.
DR EMBL; M12887; AAA60661.1; -; Genomic_DNA.
DR EMBL; L36092; AAC80213.1; -; Genomic_DNA.
DR EMBL; AC245427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471198; EAW51914.1; -; Genomic_DNA.
DR PIR; B25777; RWHUCY.
DR PDB; 1AO7; X-ray; 2.60 A; E=1-129.
DR PDB; 1FYT; X-ray; 2.60 A; E=1-133.
DR PDB; 1J8H; X-ray; 2.40 A; E=1-133.
DR PDB; 1KGC; X-ray; 1.50 A; E=1-129.
DR PDB; 1KTK; X-ray; 3.00 A; E/F=4-129.
DR PDB; 1MI5; X-ray; 2.50 A; E=1-129.
DR PDB; 1OGA; X-ray; 1.40 A; E=1-129.
DR PDB; 1YMM; X-ray; 3.50 A; E=1-130.
DR PDB; 1ZGL; X-ray; 2.80 A; P/R/T/V=1-130.
DR PDB; 2AK4; X-ray; 2.50 A; E/J/P/U=1-129.
DR PDB; 2AXH; X-ray; 2.70 A; A/B=1-129.
DR PDB; 2BNQ; X-ray; 1.70 A; E=1-129.
DR PDB; 2BNR; X-ray; 1.90 A; E=1-129.
DR PDB; 2BNU; X-ray; 1.40 A; B=1-129.
DR PDB; 2CDE; X-ray; 3.50 A; B/D/F=1-129.
DR PDB; 2CDF; X-ray; 2.25 A; B=1-129.
DR PDB; 2CDG; X-ray; 2.60 A; B=1-129.
DR PDB; 2ESV; X-ray; 2.60 A; E=1-129.
DR PDB; 2F53; X-ray; 2.10 A; E=1-129.
DR PDB; 2F54; X-ray; 2.70 A; E/L=5-129.
DR PDB; 2GJ6; X-ray; 2.56 A; E=1-129.
DR PDB; 2IAL; X-ray; 1.92 A; B/D=1-129.
DR PDB; 2IAM; X-ray; 2.80 A; D=1-129.
DR PDB; 2IAN; X-ray; 2.80 A; E/J/O/T=1-129.
DR PDB; 2NTS; X-ray; 2.40 A; P=5-127.
DR PDB; 2NW2; X-ray; 1.40 A; B=1-129.
DR PDB; 2NX5; X-ray; 2.70 A; E/J/P/U=1-129.
DR PDB; 2P5E; X-ray; 1.89 A; E=1-129.
DR PDB; 2P5W; X-ray; 2.20 A; E=1-129.
DR PDB; 2PO6; X-ray; 3.20 A; D/H=1-129.
DR PDB; 2PYE; X-ray; 2.30 A; E=1-129.
DR PDB; 2PYF; X-ray; 2.20 A; B=1-129.
DR PDB; 2VLJ; X-ray; 2.40 A; E=1-129.
DR PDB; 2VLK; X-ray; 2.50 A; E=1-129.
DR PDB; 2VLM; X-ray; 1.98 A; E=1-129.
DR PDB; 2VLR; X-ray; 2.30 A; E/J=1-129.
DR PDB; 2XN9; X-ray; 2.30 A; B=1-129.
DR PDB; 2XNA; X-ray; 2.10 A; B=1-129.
DR PDB; 3ARB; X-ray; 2.70 A; D=1-129.
DR PDB; 3ARD; X-ray; 3.01 A; D=1-129.
DR PDB; 3ARE; X-ray; 2.80 A; D=1-129.
DR PDB; 3ARF; X-ray; 2.90 A; D=1-129.
DR PDB; 3ARG; X-ray; 3.00 A; D=1-129.
DR PDB; 3D39; X-ray; 2.81 A; E=1-129.
DR PDB; 3D3V; X-ray; 2.80 A; E=1-129.
DR PDB; 3DX9; X-ray; 2.75 A; B/D=1-129.
DR PDB; 3DXA; X-ray; 3.50 A; E/J/O=1-129.
DR PDB; 3FFC; X-ray; 2.80 A; E/J=1-129.
DR PDB; 3HE6; X-ray; 2.90 A; D=1-129.
DR PDB; 3HG1; X-ray; 3.00 A; E=1-129.
DR PDB; 3KPR; X-ray; 2.60 A; E/J=1-129.
DR PDB; 3KPS; X-ray; 2.70 A; E=1-129.
DR PDB; 3O4L; X-ray; 2.54 A; E=1-129.
DR PDB; 3TN0; X-ray; 3.20 A; D=1-129.
DR PDB; 4G8E; X-ray; 2.20 A; B=1-129.
DR PDB; 4G8F; X-ray; 2.10 A; B=1-129.
DR PDB; 4GG6; X-ray; 3.20 A; F/H=1-129.
DR PDB; 4GG8; X-ray; 3.20 A; B/F=1-129.
DR PDB; 4IIQ; X-ray; 2.86 A; B=1-129.
DR PDB; 4JFD; X-ray; 2.46 A; E=1-129.
DR PDB; 4JFE; X-ray; 2.70 A; E=1-129.
DR PDB; 4JFF; X-ray; 2.43 A; E=1-129.
DR PDB; 4JFH; X-ray; 2.40 A; E=1-129.
DR PDB; 4JRX; X-ray; 2.30 A; E=1-129.
DR PDB; 4JRY; X-ray; 2.80 A; E=1-129.
DR PDB; 4L4T; X-ray; 2.00 A; E/H=1-129.
DR PDB; 4L4V; X-ray; 1.90 A; E/H=1-129.
DR PDB; 4L9L; X-ray; 3.40 A; B=1-129.
DR PDB; 4LCC; X-ray; 3.26 A; B=1-129.
DR PDB; 4LCW; X-ray; 2.40 A; E/H=1-129.
DR PDB; 4MJI; X-ray; 2.99 A; E/J=1-129.
DR PDB; 4MNQ; X-ray; 2.74 A; E=1-129.
DR PDB; 4NQC; X-ray; 2.50 A; E/H=1-129.
DR PDB; 4NQD; X-ray; 2.20 A; E/H=1-129.
DR PDB; 4NQE; X-ray; 2.10 A; E/H=1-129.
DR PDB; 4OZF; X-ray; 2.70 A; H=1-129.
DR PDB; 4OZG; X-ray; 3.00 A; F/H=1-129.
DR PDB; 4OZH; X-ray; 2.80 A; F/H=1-129.
DR PDB; 4OZI; X-ray; 3.20 A; F/H=1-129.
DR PDB; 4P46; X-ray; 2.85 A; B=1-127.
DR PDB; 4PRH; X-ray; 2.50 A; E=1-129.
DR PDB; 4PRI; X-ray; 2.40 A; E=1-129.
DR PDB; 4PRP; X-ray; 2.50 A; E=1-129.
DR PDB; 4X6B; X-ray; 2.10 A; B/D=1-129.
DR PDB; 4X6C; X-ray; 2.80 A; F/H=1-129.
DR PDB; 4X6D; X-ray; 2.98 A; F/H=1-129.
DR PDB; 4ZDH; X-ray; 2.10 A; B=1-129.
DR PDBsum; 1AO7; -.
DR PDBsum; 1FYT; -.
DR PDBsum; 1J8H; -.
DR PDBsum; 1KGC; -.
DR PDBsum; 1KTK; -.
DR PDBsum; 1MI5; -.
DR PDBsum; 1OGA; -.
DR PDBsum; 1YMM; -.
DR PDBsum; 1ZGL; -.
DR PDBsum; 2AK4; -.
DR PDBsum; 2AXH; -.
DR PDBsum; 2BNQ; -.
DR PDBsum; 2BNR; -.
DR PDBsum; 2BNU; -.
DR PDBsum; 2CDE; -.
DR PDBsum; 2CDF; -.
DR PDBsum; 2CDG; -.
DR PDBsum; 2ESV; -.
DR PDBsum; 2F53; -.
DR PDBsum; 2F54; -.
DR PDBsum; 2GJ6; -.
DR PDBsum; 2IAL; -.
DR PDBsum; 2IAM; -.
DR PDBsum; 2IAN; -.
DR PDBsum; 2NTS; -.
DR PDBsum; 2NW2; -.
DR PDBsum; 2NX5; -.
DR PDBsum; 2P5E; -.
DR PDBsum; 2P5W; -.
DR PDBsum; 2PO6; -.
DR PDBsum; 2PYE; -.
DR PDBsum; 2PYF; -.
DR PDBsum; 2VLJ; -.
DR PDBsum; 2VLK; -.
DR PDBsum; 2VLM; -.
DR PDBsum; 2VLR; -.
DR PDBsum; 2XN9; -.
DR PDBsum; 2XNA; -.
DR PDBsum; 3ARB; -.
DR PDBsum; 3ARD; -.
DR PDBsum; 3ARE; -.
DR PDBsum; 3ARF; -.
DR PDBsum; 3ARG; -.
DR PDBsum; 3D39; -.
DR PDBsum; 3D3V; -.
DR PDBsum; 3DX9; -.
DR PDBsum; 3DXA; -.
DR PDBsum; 3FFC; -.
DR PDBsum; 3HE6; -.
DR PDBsum; 3HG1; -.
DR PDBsum; 3KPR; -.
DR PDBsum; 3KPS; -.
DR PDBsum; 3O4L; -.
DR PDBsum; 3TN0; -.
DR PDBsum; 4G8E; -.
DR PDBsum; 4G8F; -.
DR PDBsum; 4GG6; -.
DR PDBsum; 4GG8; -.
DR PDBsum; 4IIQ; -.
DR PDBsum; 4JFD; -.
DR PDBsum; 4JFE; -.
DR PDBsum; 4JFF; -.
DR PDBsum; 4JFH; -.
DR PDBsum; 4JRX; -.
DR PDBsum; 4JRY; -.
DR PDBsum; 4L4T; -.
DR PDBsum; 4L4V; -.
DR PDBsum; 4L9L; -.
DR PDBsum; 4LCC; -.
DR PDBsum; 4LCW; -.
DR PDBsum; 4MJI; -.
DR PDBsum; 4MNQ; -.
DR PDBsum; 4NQC; -.
DR PDBsum; 4NQD; -.
DR PDBsum; 4NQE; -.
DR PDBsum; 4OZF; -.
DR PDBsum; 4OZG; -.
DR PDBsum; 4OZH; -.
DR PDBsum; 4OZI; -.
DR PDBsum; 4P46; -.
DR PDBsum; 4PRH; -.
DR PDBsum; 4PRI; -.
DR PDBsum; 4PRP; -.
DR PDBsum; 4X6B; -.
DR PDBsum; 4X6C; -.
DR PDBsum; 4X6D; -.
DR PDBsum; 4ZDH; -.
DR AlphaFoldDB; P01850; -.
DR SMR; P01850; -.
DR ComplexPortal; CPX-6581; Alpha-beta T cell receptor complex, TRBC1 variant.
DR IntAct; P01850; 3.
DR DrugBank; DB02740; 3-Indolebutyric Acid.
DR IMGT_GENE-DB; TRBC1; -.
DR GlyGen; P01850; 1 site.
DR iPTMnet; P01850; -.
DR PhosphoSitePlus; P01850; -.
DR BioMuta; ENSG00000211751; -.
DR BioMuta; HGNC:12156; -.
DR DMDM; 294862488; -.
DR jPOST; P01850; -.
DR MassIVE; P01850; -.
DR PeptideAtlas; P01850; -.
DR PRIDE; P01850; -.
DR ProteomicsDB; 51492; -.
DR ABCD; P01850; 10 sequenced antibodies.
DR GeneCards; TRBC1; -.
DR HGNC; HGNC:12156; TRBC1.
DR MIM; 186930; gene.
DR neXtProt; NX_P01850; -.
DR InParanoid; P01850; -.
DR OMA; NISASAW; -.
DR PhylomeDB; P01850; -.
DR PathwayCommons; P01850; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
DR Reactome; R-HSA-202433; Generation of second messenger molecules.
DR Reactome; R-HSA-389948; PD-1 signaling.
DR SignaLink; P01850; -.
DR SIGNOR; P01850; -.
DR ChiTaRS; TRBC1; human.
DR EvolutionaryTrace; P01850; -.
DR Pharos; P01850; Tdark.
DR PRO; PR:P01850; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P01850; protein.
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:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042101; C:T cell receptor complex; IEA:UniProtKB-KW.
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:0006955; P:immune response; NAS:UniProtKB.
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..176
FT /note="T cell receptor beta constant 1"
FT /id="PRO_0000184526"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..176
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:0000305|PubMed:27791034,
FT ECO:0000305|PubMed:9382891"
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:19167249"
FT DISULFID 130
FT /note="Interchain (with C-94 in TRAC)"
FT /evidence="ECO:0000269|PubMed:27791034"
FT MUTAGEN 139
FT /note="Q->F: Impairs signal transduction in response to
FT antigenic stimulation."
FT /evidence="ECO:0000269|PubMed:9382891"
FT MUTAGEN 162
FT /note="V->F: Reduces TR-CD3 complex assembly."
FT /evidence="ECO:0000269|PubMed:27791034"
FT NON_TER 1
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:1OGA"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1OGA"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:1OGA"
FT STRAND 24..38
FT /evidence="ECO:0007829|PDB:1OGA"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1OGA"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1OGA"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1OGA"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1OGA"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4JRX"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:1OGA"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1OGA"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1ZGL"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1OGA"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4G8F"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1OGA"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:1OGA"
SQ SEQUENCE 176 AA; 19769 MW; F029F045A6FC73C5 CRC64;
DLNKVFPPEV AVFEPSEAEI SHTQKATLVC LATGFFPDHV ELSWWVNGKE VHSGVSTDPQ
PLKEQPALND SRYCLSSRLR VSATFWQNPR NHFRCQVQFY GLSENDEWTQ DRAKPVTQIV
SAEAWGRADC GFTSVSYQQG VLSATILYEI LLGKATLYAV LVSALVLMAM VKRKDF
