TVB51_HUMAN
ID TVB51_HUMAN Reviewed; 114 AA.
AC A0A578;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=T cell receptor beta variable 5-1 {ECO:0000303|Ref.3};
DE Flags: Precursor;
GN Name=TRBV5-1 {ECO:0000303|Ref.3};
GN Synonyms=TCRBV5S1A1T {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 TRBV5-1*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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRBV5-1*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 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 [5]
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 [6]
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 [7]
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 [8]
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 [9] {ECO:0007744|PDB:5BRZ, ECO:0007744|PDB:5BS0}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 21-113, 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).
CC -!- FUNCTION: V region of the variable domain of T cell receptor (TR) beta
CC chain that participates in the antigen recognition (PubMed:24600447).
CC Alpha-beta T cell receptors are antigen specific receptors which are
CC essential to the immune response and are present on the cell surface of
CC T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH)
CC complexes that are displayed by antigen presenting cells (APC), a
CC prerequisite for efficient T cell adaptive immunity against pathogens
CC (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates
CC TR-CD3 clustering on the cell surface and intracellular activation of
CC LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247
CC enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT,
CC which recruits numerous signaling molecules to form the LAT
CC signalosome. The LAT signalosome propagates signal branching to three
CC major signaling pathways, the calcium, the mitogen-activated protein
CC kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB)
CC pathways, leading to the mobilization of transcription factors that are
CC critical for gene expression and essential for T cell growth and
CC differentiation (PubMed:23524462). The T cell repertoire is generated
CC in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped
CC by intrathymic selection events to generate a peripheral T cell pool of
CC self-MH restricted, non-autoaggressive T cells. Post-thymic interaction
CC of alpha-beta TR with the pMH complexes shapes TR structural and
CC functional avidity (PubMed:15040585). {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 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 -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele TRBV5-1*01. {ECO:0000305}.
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DR EMBL; L36092; AAC80192.1; -; Genomic_DNA.
DR EMBL; AC231381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC245088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 5BRZ; X-ray; 2.62 A; E=21-113.
DR PDB; 5BS0; X-ray; 2.40 A; E=21-113.
DR PDBsum; 5BRZ; -.
DR PDBsum; 5BS0; -.
DR AlphaFoldDB; A0A578; -.
DR SMR; A0A578; -.
DR IMGT_GENE-DB; TRBV5-1; -.
DR GlyGen; A0A578; 1 site.
DR BioMuta; TRBV5-1; -.
DR PeptideAtlas; A0A578; -.
DR PRIDE; A0A578; -.
DR Ensembl; ENST00000390381.3; ENSP00000374904.3; ENSG00000211734.3.
DR Ensembl; ENST00000633384.1; ENSP00000488308.1; ENSG00000282803.1.
DR UCSC; uc033ajs.2; human.
DR GeneCards; TRBV5-1; -.
DR HGNC; HGNC:12218; TRBV5-1.
DR HPA; ENSG00000211734; Tissue enriched (lymphoid).
DR neXtProt; NX_A0A578; -.
DR VEuPathDB; HostDB:ENSG00000211734; -.
DR GeneTree; ENSGT00940000154270; -.
DR HOGENOM; CLU_077975_9_4_1; -.
DR OMA; REWDICK; -.
DR PhylomeDB; A0A578; -.
DR SignaLink; A0A578; -.
DR ChiTaRS; TRBV5-1; human.
DR Pharos; A0A578; Tdark.
DR PRO; PR:A0A578; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; A0A578; protein.
DR Bgee; ENSG00000211734; Expressed in lymph node and 80 other tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042101; C:T cell receptor complex; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
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; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Signal; T cell receptor.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..114
FT /note="T cell receptor beta variable 5-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5010490472"
FT DOMAIN 22..>114
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:26758806, ECO:0007744|PDB:5BRZ,
FT ECO:0007744|PDB:5BS0"
FT NON_TER 114
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:5BS0"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:5BS0"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5BS0"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:5BS0"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5BS0"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:5BS0"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5BS0"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:5BS0"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5BRZ"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:5BS0"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5BS0"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:5BS0"
SQ SEQUENCE 114 AA; 12600 MW; E91DD184A09483A6 CRC64;
MGSRLLCWVL LCLLGAGPVK AGVTQTPRYL IKTRGQQVTL SCSPISGHRS VSWYQQTPGQ
GLQFLFEYFS ETQRNKGNFP GRFSGRQFSN SRSEMNVSTL ELGDSALYLC ASSL
