ID TVB65_HUMAN Reviewed; 114 AA. AC A0A0K0K1A5; A0A075B6M0; A0A0A6YYR1; A0A585; DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2016, sequence version 3. DT 16-JAN-2019, entry version 35. DE RecName: Full=T cell receptor beta variable 6-5 {ECO:0000303|Ref.2}; DE Flags: Precursor; GN Name=TRBV6-5 {ECO:0000303|Ref.2}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE RP TRBV6-5*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., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA 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., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [2] 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. RL (2001). RN [3] 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 [4] RP REVIEW ON T CELL RECEPTOR-CD3 COMPLEX ASSEMBLY, AND SUBCELLULAR RP 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 [5] 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 RT bounded."; RL Nat. Rev. Immunol. 13:257-269(2013). 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 RT Rise of Immunoinformatics."; RL Front. Immunol. 5:22-22(2014). RN [7] 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., RA McCluskey J.; RT "T cell antigen receptor recognition of antigen-presenting RT molecules."; RL Annu. Rev. Immunol. 33:169-200(2015). RN [8] {ECO:0000244|PDB:1AO7} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-114, 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 RT and HLA-A2."; RL Nature 384:134-141(1996). RN [9] {ECO:0000244|PDB:1BD2} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 20-114, 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., RA Wiley D.C.; RT "Two human T cell receptors bind in a similar diagonal mode to the RT HLA-A2/Tax peptide complex using different TCR amino acids."; RL Immunity 8:403-411(1998). RN [10] {ECO:0000244|PDB:2BNQ, ECO:0000244|PDB:2BNR, ECO:0000244|PDB:2BNU} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 22-114, AND DISULFIDE BONDS. RX PubMed=15837811; DOI=10.1084/jem.20042323; RA Chen J.-L., Stewart-Jones G., Bossi G., Lissin N.M., Wooldridge L., RA Choi E.M.L., Held G., Dunbar P.R., Esnouf R.M., Sami M., Boulter J.M., RA Rizkallah P., Renner C., Sewell A., van der Merwe P.A., Jakobsen B.K., RA Griffiths G., Jones E.Y., Cerundolo V.; RT "Structural and kinetic basis for heightened immunogenicity of T cell RT vaccines."; RL J. Exp. Med. 201:1243-1255(2005). RN [11] {ECO:0000244|PDB:4WWK} RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 19-113 IN COMPLEX WITH ALPHA RP CHAIN AND CD1D, DISULFIDE BONDS, AND FUNCTION. 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., RA Gras S., 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). CC -!- FUNCTION: V region of the variable domain of T cell receptor (TR) CC beta chain that participates in the antigen recognition CC (PubMed:24600447). Alpha-beta T cell receptors are antigen CC specific receptors which are essential to the immune response and CC are present on the cell surface of T lymphocytes. Recognize CC peptide-major histocompatibility (MH) (pMH) complexes that are CC displayed by antigen presenting cells (APC), a prerequisite for CC efficient T cell adaptive immunity against pathogens CC (PubMed:25493333). Binding of alpha-beta TR to pMH complex CC initiates TR-CD3 clustering on the cell surface and intracellular CC activation of LCK that phosphorylates the ITAM motifs of CD3G, CC CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn CC ZAP70 phosphorylates LAT, which recruits numerous signaling CC molecules to form the LAT signalosome. The LAT signalosome CC propagates signal branching to three major signaling pathways, the CC calcium, the mitogen-activated protein kinase (MAPK) kinase and CC the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the CC mobilization of transcription factors that are critical for gene CC expression and essential for T cell growth and differentiation CC (PubMed:23524462). The T cell repertoire is generated in the CC thymus, by V-(D)-J rearrangement. This repertoire is then shaped CC by intrathymic selection events to generate a peripheral T cell CC pool of self-MH restricted, non-autoaggressive T cells. Post- CC thymic interaction of alpha-beta TR with the pMH complexes shapes CC TR structural and functional avidity (PubMed:15040585). CC {ECO:0000269|PubMed:26875526, ECO:0000303|PubMed:15040585, CC ECO:0000303|PubMed:23524462, ECO:0000303|PubMed:24600447, CC ECO:0000303|PubMed:25493333}. CC -!- SUBUNIT: Alpha-beta TR is a heterodimer composed of an alpha and CC beta chain; disulfide-linked (PubMed:26875526). The alpha-beta TR CC is associated with the transmembrane signaling CD3 coreceptor CC proteins to form the TR-CD3 (TcR or TCR). The assembly of alpha- CC beta TR heterodimers with CD3 occurs in the endoplasmic reticulum CC where a single alpha-beta TR heterodimer associates with one CD3D- CC CD3E heterodimer, one CD3G-CD3E heterodimer and one CD247 CC homodimer forming a stable octomeric structure. CD3D-CD3E and CC CD3G-CD3E heterodimers preferentially associate with TR alpha and CC TR beta chains, respectively. The association of the CD247 CC homodimer is the last step of TcR assembly in the endoplasmic CC reticulum and is required for transport to the cell surface CC (PubMed:20452950). {ECO:0000269|PubMed:26875526, CC ECO:0000303|PubMed:20452950}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:20452950}. CC -!- POLYMORPHISM: There are several alleles. The sequence shown is CC that of IMGT allele TRBV6-5*01. {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; AC244196; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR UniGene; Hs.382212; -. DR PDB; 1AO7; X-ray; 2.60 A; E=20-114. DR PDB; 1BD2; X-ray; 2.50 A; E=20-114. DR PDB; 2BNQ; X-ray; 1.70 A; E=22-114. DR PDB; 2BNR; X-ray; 1.90 A; E=22-114. DR PDB; 2BNU; X-ray; 1.40 A; B=22-114. DR PDB; 4WWK; X-ray; 3.10 A; B=19-113. DR PDBsum; 1AO7; -. DR PDBsum; 1BD2; -. DR PDBsum; 2BNQ; -. DR PDBsum; 2BNR; -. DR PDBsum; 2BNU; -. DR PDBsum; 4WWK; -. DR ProteinModelPortal; A0A0K0K1A5; -. DR SMR; A0A0K0K1A5; -. DR IMGT_GENE-DB; TRBV6-5; -. DR BioMuta; TRBV6-5; -. DR Ensembl; ENST00000390368; ENSP00000374891; ENSG00000211721. DR Ensembl; ENST00000633072; ENSP00000488123; ENSG00000277110. DR UCSC; uc064isk.1; human. DR EuPathDB; HostDB:ENSG00000211721.2; -. DR GeneCards; TRBV6-5; -. DR HGNC; HGNC:12230; TRBV6-5. DR neXtProt; NX_A0A0K0K1A5; -. DR GeneTree; ENSGT00940000154542; -. DR HOGENOM; HOG000168489; -. DR HOVERGEN; HBG100543; -. DR OMA; DMNHDCM; -. DR PhylomeDB; A0A0K0K1A5; -. DR ChiTaRS; TRBV6-5; human. DR PRO; PR:A0A0K0K1A5; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000211721; Expressed in 66 organ(s), highest expression level in leukocyte. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. 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; IPR013106; Ig_V-set. DR Pfam; PF07686; V-set; 1. DR SMART; SM00406; IGv; 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; Complete proteome; KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; KW Membrane; Polymorphism; Receptor; Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 114 T cell receptor beta variable 6-5. FT {ECO:0000255}. FT /FTId=PRO_5011354908. FT DOMAIN 22 >114 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT CARBOHYD 84 84 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 42 110 {ECO:0000244|PDB:1AO7, FT ECO:0000244|PDB:1BD2, FT ECO:0000244|PDB:2BNQ, FT ECO:0000244|PDB:2BNR, FT ECO:0000244|PDB:2BNU, FT ECO:0000244|PDB:4WWK, FT ECO:0000269|PubMed:15837811, FT ECO:0000269|PubMed:26875526, FT ECO:0000269|PubMed:8906788, FT ECO:0000269|PubMed:9586631}. FT NON_TER 114 114 FT STRAND 23 26 {ECO:0000244|PDB:2BNU}. FT STRAND 28 33 {ECO:0000244|PDB:2BNU}. FT STRAND 38 46 {ECO:0000244|PDB:2BNU}. FT STRAND 49 57 {ECO:0000244|PDB:2BNU}. FT TURN 58 60 {ECO:0000244|PDB:2BNU}. FT STRAND 61 70 {ECO:0000244|PDB:2BNU}. FT STRAND 73 76 {ECO:0000244|PDB:2BNU}. FT STRAND 83 85 {ECO:0000244|PDB:1BD2}. FT STRAND 88 92 {ECO:0000244|PDB:2BNU}. FT STRAND 95 99 {ECO:0000244|PDB:2BNU}. FT HELIX 102 104 {ECO:0000244|PDB:2BNU}. FT STRAND 106 113 {ECO:0000244|PDB:2BNU}. SQ SEQUENCE 114 AA; 12402 MW; B7BB73ACD3FC006D CRC64; MSIGLLCCAA LSLLWAGPVN AGVTQTPKFQ VLKTGQSMTL QCAQDMNHEY MSWYRQDPGM GLRLIHYSVG AGITDQGEVP NGYNVSRSTT EDFPLRLLSA APSQTSVYFC ASSY //