TRBR1_HUMAN
ID TRBR1_HUMAN Reviewed; 310 AA.
AC P0DSE2;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=M1-specific T cell receptor beta chain {ECO:0000303|PubMed:29997621};
DE AltName: Full=TR beta chain TRBV19*01J2S7*01C*02 {ECO:0000303|PubMed:29997621, ECO:0000303|PubMed:8550091};
DE Flags: Precursor;
GN Name=TRB {ECO:0000312|HGNC:HGNC:12155};
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] OF 22-132, CDR3 DOMAIN, AND FUNCTION.
RX PubMed=1833769; DOI=10.1073/pnas.88.20.8987;
RA Moss P.A., Moots R.J., Rosenberg W.M., Rowland-Jones S.J., Bodmer H.C.,
RA McMichael A.J., Bell J.I.;
RT "Extensive conservation of alpha and beta chains of the human T-cell
RT antigen receptor recognizing HLA-A2 and influenza A matrix peptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8987-8990(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-132, CDR3 DOMAIN, FUNCTION, AND VARIANT
RP SER-114.
RX PubMed=7807026; DOI=10.1084/jem.181.1.79;
RA Lehner P.J., Wang E.C., Moss P.A., Williams S., Platt K., Friedman S.M.,
RA Bell J.I., Borysiewicz L.K.;
RT "Human HLA-A0201-restricted cytotoxic T lymphocyte recognition of influenza
RT A is dominated by T cells bearing the V beta 17 gene segment.";
RL J. Exp. Med. 181:79-91(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-132, CDR3 DOMAIN, FUNCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=29997621; DOI=10.3389/fimmu.2018.01453;
RA Sant S., Grzelak L., Wang Z., Pizzolla A., Koutsakos M., Crowe J.,
RA Loudovaris T., Mannering S.I., Westall G.P., Wakim L.M., Rossjohn J.,
RA Gras S., Richards M., Xu J., Thomas P.G., Loh L., Nguyen T.H.O.,
RA Kedzierska K.;
RT "Single-Cell Approach to Influenza-Specific CD8+ T Cell Receptor
RT Repertoires Across Different Age Groups, Tissues, and Following Influenza
RT Virus Infection.";
RL Front. Immunol. 9:1453-1453(2018).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRBV19*01 AND
RP IMGT ALLELE TRBJ2-7*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 [6]
RP NOMENCLATURE.
RX PubMed=8550091; DOI=10.1007/bf00172175;
RG WHO-IUIS Nomenclature Sub-Committee on TCR Designation.;
RT "Nomenclature for T-cell receptor (TCR) gene segments of the immune
RT system.";
RL Immunogenetics 42:451-453(1995).
RN [7]
RP CDR1 AND CDR2 DOMAINS.
RX PubMed=11096259; DOI=10.1159/000019140;
RA Folch G., Scaviner D., Contet V., Lefranc M.P.;
RT "Protein displays of the human T cell receptor alpha, beta, gamma and delta
RT variable and joining regions.";
RL Exp. Clin. Immunogenet. 17:205-215(2000).
RN [8]
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 [9]
RP NOMENCLATURE.
RX PubMed=19568742; DOI=10.1007/s00251-009-0383-x;
RA Yassai M.B., Naumov Y.N., Naumova E.N., Gorski J.;
RT "A clonotype nomenclature for T cell receptors.";
RL Immunogenetics 61:493-502(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 19-261, INTERACTION WITH
RP PEPTIDE-HLA-A*02-B2M, FUNCTION, DOMAIN, AND VARIANT SER-114.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 19-261, INTERACTION WITH
RP PEPTIDE-HLA-A*02-B2M, FUNCTION, MUTAGENESIS OF ASP-49; GLN-69; ILE-70 AND
RP ARG-115, DOMAIN, AND VARIANT SER-114.
RX PubMed=18275829; DOI=10.1016/j.immuni.2007.12.018;
RA Ishizuka J., Stewart-Jones G.B., van der Merwe A., Bell J.I.,
RA McMichael A.J., Jones E.Y.;
RT "The structural dynamics and energetics of an immunodominant T cell
RT receptor are programmed by its Vbeta domain.";
RL Immunity 28:171-182(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 21-261, INTERACTION WITH
RP PEPTIDE-HLA-A*02-B2M, DISULFIDE BOND, FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT SER-114.
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).
CC -!- FUNCTION: The beta chain of TRAV27*01J42*01C*01/TRBV19*01J2S7*01C*02
CC alpha-beta T cell receptor (TR) clonotype that is specific for HLA-
CC A*02:01-restricted M/matrix protein 1 immunodominant epitope GILGFVFTL
CC of influenza A virus (IAV). Classified as a public TCR clonotype, it is
CC preferentially selected in effector memory CD8-positive T cells among
CC multiple HLA-A*02:01 carriers/individuals and confers long-lived
CC immunity against IAV infection. Can cross-recognize sporadically
CC emerging IAV variants by molecular mimicry, inducing immunity toward
CC different influenza strains (PubMed:1833769, PubMed:7807026,
CC PubMed:29997621, PubMed:27036003, PubMed:12796775, PubMed:18275829).
CC Antigen recognition 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 differentiation into effector/memory T cells (By similarity).
CC {ECO:0000250|UniProtKB:A0A075B6N1, ECO:0000269|PubMed:12796775,
CC ECO:0000269|PubMed:18275829, ECO:0000269|PubMed:1833769,
CC ECO:0000269|PubMed:27036003, ECO:0000269|PubMed:29997621,
CC ECO:0000269|PubMed:7807026}.
CC -!- SUBUNIT: Disulfide-linked heterodimer with TRAV27*01J42*01C*01 alpha
CC chain. The TR primarily interacts via its CDR3-beta domain with
CC M/matrix protein 1-derived peptide (GILGFVFTL) displayed by HLA-A*02.01
CC in a 'peg-notch' recognition mode (PubMed:27036003, PubMed:12796775,
CC PubMed:18275829). The alpha-beta TR associates with the transmembrane
CC signaling CD3 coreceptor proteins to form the TR-CD3 (TCR). The
CC assembly of alpha-beta TR heterodimers with CD3 occurs in the
CC 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 (via TM domain), respectively. The association of the
CC CD247 homodimer is the last step of TCR assembly in the endoplasmic
CC reticulum and is required for transport to the cell surface (By
CC similarity). {ECO:0000250|UniProtKB:A0A075B6N1,
CC ECO:0000269|PubMed:12796775, ECO:0000269|PubMed:18275829,
CC ECO:0000269|PubMed:27036003}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29997621}.
CC -!- TISSUE SPECIFICITY: Expressed in M/matrix protein 1-specific effector
CC memory CD8-positive T cells readily detectable in the peripheral blood,
CC secondary lymphoid organs and lung (primary site of infection) of IAV
CC infected individuals. {ECO:0000269|PubMed:29997621}.
CC -!- DOMAIN: The complementarity-determining region CDR1 confers specificity
CC to the peptide antigen. Assumes a loop structure that recognizes the
CC peptide-HLA-A*02-B2M complex. {ECO:0000269|PubMed:12796775,
CC ECO:0000269|PubMed:18275829, ECO:0000305|PubMed:11096259}.
CC -!- DOMAIN: The complementarity-determining region CDR2 confers specificity
CC to the peptide antigen. Assumes a loop structure that recognizes the
CC peptide-HLA-A*02-B2M complex. {ECO:0000269|PubMed:12796775,
CC ECO:0000269|PubMed:18275829, ECO:0000305|PubMed:11096259}.
CC -!- DOMAIN: The complementarity-determining region CDR3 confers specificity
CC to the peptide antigen. Assumes a loop structure that recognizes the
CC peptide-HLA-A*02-B2M complex. Recognizes M/matrix protein 1-derived
CC peptide mainly via its xRSx motif. {ECO:0000269|PubMed:12796775,
CC ECO:0000269|PubMed:18275829, ECO:0000269|PubMed:1833769,
CC ECO:0000269|PubMed:29997621, ECO:0000269|PubMed:7807026}.
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 -!- MISCELLANEOUS: The JM22 clone described as a variant of the public
CC clonotype differs by one amino acid in the CDR3-beta domain.
CC {ECO:0000305|PubMed:12796775, ECO:0000305|PubMed:18275829,
CC ECO:0000305|PubMed:27036003, ECO:0000305|PubMed:7807026}.
CC -!- CAUTION: This sequence is an example of a full-length TR beta chain.
CC M/matrix protein 1-specific TRBV19*01J2S7*01C*02 TCR beta chain is
CC generated by somatic recombination of variable TRBV19 (AC A0A075B6N1),
CC diversity (AC P0DPI4) and joining TRBJ2-7 (AC A0A0A0MT78) gene segments
CC spliced to constant TRBC2 (AC A0A5B9) gene segment (PubMed:1833769,
CC PubMed:7807026, PubMed:29997621, PubMed:27036003). CDR3-beta clonotype
CC identifier: sIRSSy.1456B19S1B27L11 (PubMed:19568742).
CC {ECO:0000269|PubMed:1833769, ECO:0000269|PubMed:27036003,
CC ECO:0000269|PubMed:29997621, ECO:0000269|PubMed:7807026,
CC ECO:0000303|PubMed:19568742}.
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DR EMBL; AAB20045; CAA84752.1; -; mRNA.
DR EMBL; M12888; AAA60662.1; -; Genomic_DNA.
DR EMBL; AC244472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC239618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 1OGA; X-ray; 1.40 A; -.
DR PDB; 2VLJ; X-ray; 2.40 A; -.
DR PDB; 2VLK; X-ray; 2.50 A; -.
DR PDB; 2VLR; X-ray; 2.30 A; -.
DR PDB; 5HHM; X-ray; 2.50 A; -.
DR PDB; 5HHO; X-ray; 2.95 A; -.
DR PDB; 6JXR; EM; 3.70 A; n=119-310.
DR PDBsum; 1OGA; -.
DR PDBsum; 2VLJ; -.
DR PDBsum; 2VLK; -.
DR PDBsum; 2VLR; -.
DR PDBsum; 5HHM; -.
DR PDBsum; 5HHO; -.
DR PDBsum; 6JXR; -.
DR AlphaFoldDB; P0DSE2; -.
DR SMR; P0DSE2; -.
DR PeptideAtlas; P0DSE2; -.
DR GeneCards; TRB; -.
DR HGNC; HGNC:12155; TRB.
DR MalaCards; TRB; -.
DR PathwayCommons; P0DSE2; -.
DR ChiTaRS; TRB; human.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042101; C:T cell receptor complex; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IDA:UniProtKB.
DR GO; GO:0002286; P:T cell activation involved in immune response; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
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 InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Membrane; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..310
FT /note="M1-specific T cell receptor beta chain"
FT /id="PRO_0000447045"
FT TRANSMEM 277..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..131
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 140..249
FT /note="Ig-like C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 22..114
FT /note="T cell receptor beta variable 19"
FT /evidence="ECO:0000305|PubMed:1833769"
FT REGION 46..50
FT /note="CDR1"
FT /evidence="ECO:0000305|PubMed:11096259"
FT REGION 68..73
FT /note="CDR2"
FT /evidence="ECO:0000305|PubMed:11096259"
FT REGION 110..122
FT /note="CDR3"
FT /evidence="ECO:0000269|PubMed:1833769,
FT ECO:0000269|PubMed:29997621, ECO:0000269|PubMed:7807026"
FT REGION 117..131
FT /note="T cell receptor beta joining 2-7"
FT /evidence="ECO:0000305|PubMed:1833769"
FT REGION 133..310
FT /note="T cell receptor beta constant 2"
FT /evidence="ECO:0000305|PubMed:27036003"
FT REGION 262..276
FT /note="Connecting peptide"
FT /evidence="ECO:0000250|UniProtKB:P01850"
FT BINDING 49
FT /ligand="a peptide antigen"
FT /ligand_id="ChEBI:CHEBI:166823"
FT /ligand_note="M/matrix protein 1 peptide antigen"
FT /evidence="ECO:0000269|PubMed:27036003"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 42..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:27036003"
FT DISULFID 162..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:27036003"
FT DISULFID 262
FT /note="Interchain (with C-224 in TRAC)"
FT /evidence="ECO:0000250|UniProtKB:P01850"
FT VARIANT 114
FT /note="I -> S"
FT /evidence="ECO:0000305|PubMed:12796775,
FT ECO:0000305|PubMed:18275829, ECO:0000305|PubMed:27036003,
FT ECO:0000305|PubMed:7807026"
FT /id="VAR_081651"
FT MUTAGEN 49
FT /note="D->A,S: Abolishes binding to M/matrix protein 1
FT peptide antigen."
FT /evidence="ECO:0000269|PubMed:18275829"
FT MUTAGEN 69
FT /note="Q->A,E: Abolishes binding to M/matrix protein 1
FT peptide antigen."
FT /evidence="ECO:0000269|PubMed:18275829"
FT MUTAGEN 70
FT /note="I->A,G,N: Abolishes binding to M/matrix protein 1
FT peptide antigen."
FT /evidence="ECO:0000269|PubMed:18275829"
FT MUTAGEN 115
FT /note="R->A,H: Abolishes binding to M/matrix protein 1
FT peptide antigen."
FT /evidence="ECO:0000269|PubMed:18275829"
SQ SEQUENCE 310 AA; 34792 MW; 12666199D0630D69 CRC64;
MSNQVLCCVV LCLLGANTVD GGITQSPKYL FRKEGQNVTL SCEQNLNHDA MYWYRQDPGQ
GLRLIYYSQI VNDFQKGDIA EGYSVSREKK ESFPLTVTSA QKNPTAFYLC ASSIRSSYEQ
YFGPGTRLTV TEDLKNVFPP KVAVFEPSEA EISHTQKATL VCLATGFYPD HVELSWWVNG
KEVHSGVSTD PQPLKEQPAL NDSRYCLSSR LRVSATFWQN PRNHFRCQVQ FYGLSENDEW
TQDRAKPVTQ IVSAEAWGRA DCGFTSESYQ QGVLSATILY EILLGKATLY AVLVSALVLM
AMVKRKDSRG
