TRAC_HUMAN
ID TRAC_HUMAN Reviewed; 140 AA.
AC P01848; A0A087WWC6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=T cell receptor alpha chain constant {ECO:0000303|Ref.4};
GN Name=TRAC {ECO:0000303|Ref.4}; Synonyms=TCRA;
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 TRAC*01).
RX PubMed=3875483; DOI=10.1002/j.1460-2075.1985.tb03803.x;
RA Rabbitts T.H., Lefranc M.P., Stinson M.A., Sims J.E., Schroder J.,
RA Steinmetz M., Spurr N.L., Solomon E., Goodfellow P.N.;
RT "The chromosomal location of T-cell receptor genes and a T cell rearranging
RT gene: possible correlation with specific translocations in human T cell
RT leukaemia.";
RL EMBO J. 4:1461-1465(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (IMGT ALLELE TRAC*01).
RX PubMed=3873654; DOI=10.1073/pnas.82.10.3430;
RA Yanagi Y., Chan A., Chin B., Minden M., Mak T.W.;
RT "Analysis of cDNA clones specific for human T cells and the alpha and beta
RT chains of the T-cell receptor heterodimer from a human T-cell line.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3430-3434(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE TRAC*01).
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
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 [5]
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-32 AND ASN-66.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
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]
RP DISULFIDE BOND, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASN-130.
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 [12]
RP INVOLVEMENT IN IMD7.
RX PubMed=21206088; DOI=10.1172/jci41931;
RA Morgan N.V., Goddard S., Cardno T.S., McDonald D., Rahman F., Barge D.,
RA Ciupek A., Straatman-Iwanowska A., Pasha S., Guckian M., Anderson G.,
RA Huissoon A., Cant A., Tate W.P., Hambleton S., Maher E.R.;
RT "Mutation in the TCRalpha subunit constant gene (TRAC) leads to a human
RT immunodeficiency disorder characterized by a lack of TCRalphabeta+ T
RT cells.";
RL J. Clin. Invest. 121:695-702(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-93.
RX PubMed=12429093; DOI=10.1016/s0969-2126(02)00878-x;
RA Kjer-Nielsen L., Clements C.S., Brooks A.G., Purcell A.W., McCluskey J.,
RA Rossjohn J.;
RT "The 1.5 A crystal structure of a highly selected antiviral T cell receptor
RT provides evidence for a structural basis of immunodominance.";
RL Structure 10:1521-1532(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-91 IN COMPLEX WITH HLA-A/B2M
RP HETERODIMER AND TRBC1, AND DISULFIDE BOND.
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 1-94 IN COMPLEX WITH
RP HLA-DRA/HLA-DRB5 HETERODIMER AND MBP PEPTIDE.
RX PubMed=16079912; DOI=10.1038/sj.emboj.7600771;
RA Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A.;
RT "Structure of a human autoimmune TCR bound to a myelin basic protein self-
RT peptide and a multiple sclerosis-associated MHC class II molecule.";
RL EMBO J. 24:2968-2979(2005).
CC -!- FUNCTION: Constant region of T cell receptor (TR) alpha 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 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 contributes to the TR-CD3
CC assembly and signal transduction. {ECO:0000305|PubMed:27791034}.
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 TRAC*01. {ECO:0000305}.
CC -!- DISEASE: Immunodeficiency 7 (IMD7) [MIM:615387]: A primary
CC immunodeficiency disorder manifesting with recurrent respiratory
CC infections, candidiasis, diarrhea, and failure to thrive. Patients show
CC a clear predisposition to herpes viral infections, and features of
CC immune dysregulation, including hypereosinophilia, vitiligo, and
CC alopecia areata. Other features include lymphadenopathy and
CC hepatosplenomegaly. CD3+ T-cells express TCR-gamma/delta, but little or
CC no TCR-alpha/beta. {ECO:0000269|PubMed:21206088}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26435.1; Type=Miscellaneous discrepancy; Note=Chimeric mRNA corresponding to regions V, J and C of T cell receptor (TR) alpha chain.; Evidence={ECO:0000305};
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DR EMBL; X02592; CAA26435.1; ALT_SEQ; mRNA.
DR EMBL; AC243965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S18893; RWHUAC.
DR PDB; 1AO7; X-ray; 2.60 A; D=1-93.
DR PDB; 1BD2; X-ray; 2.50 A; D=1-93.
DR PDB; 1FYT; X-ray; 2.60 A; D=1-97.
DR PDB; 1J8H; X-ray; 2.40 A; D=1-97.
DR PDB; 1KGC; X-ray; 1.50 A; D=1-93.
DR PDB; 1MI5; X-ray; 2.50 A; D=1-89.
DR PDB; 1OGA; X-ray; 1.40 A; D=1-95.
DR PDB; 1QRN; X-ray; 2.80 A; D=1-89.
DR PDB; 1QSF; X-ray; 2.80 A; D=1-89.
DR PDB; 1YMM; X-ray; 3.50 A; D=1-94.
DR PDB; 1ZGL; X-ray; 2.80 A; M/Q/S/U=1-94.
DR PDB; 2AK4; X-ray; 2.50 A; D/I/N/T=1-93.
DR PDB; 2BNQ; X-ray; 1.70 A; D=1-89.
DR PDB; 2BNR; X-ray; 1.90 A; D=1-89.
DR PDB; 2BNU; X-ray; 1.40 A; A=1-89.
DR PDB; 2CDF; X-ray; 2.25 A; A=1-78.
DR PDB; 2CDG; X-ray; 2.60 A; A=1-78.
DR PDB; 2ESV; X-ray; 2.60 A; D=1-89.
DR PDB; 2EYR; X-ray; 2.40 A; A=1-93.
DR PDB; 2EYS; X-ray; 2.21 A; A=1-93.
DR PDB; 2EYT; X-ray; 2.60 A; A/C=1-93.
DR PDB; 2F53; X-ray; 2.10 A; D=1-77.
DR PDB; 2F54; X-ray; 2.70 A; D/K=1-91.
DR PDB; 2GJ6; X-ray; 2.56 A; D=1-89.
DR PDB; 2IAL; X-ray; 1.92 A; A/C=1-93.
DR PDB; 2IAM; X-ray; 2.80 A; C=1-93.
DR PDB; 2IAN; X-ray; 2.80 A; D/I/N/S=1-93.
DR PDB; 2NX5; X-ray; 2.70 A; D/I/N/T=1-77.
DR PDB; 2P5E; X-ray; 1.89 A; D=1-79.
DR PDB; 2P5W; X-ray; 2.20 A; D=1-77.
DR PDB; 2PO6; X-ray; 3.20 A; C/G=1-90.
DR PDB; 2PYE; X-ray; 2.30 A; D=1-79.
DR PDB; 2PYF; X-ray; 2.20 A; A=1-91.
DR PDB; 2VLJ; X-ray; 2.40 A; D=1-89.
DR PDB; 2VLK; X-ray; 2.50 A; D=1-89.
DR PDB; 2VLM; X-ray; 1.98 A; D=1-89.
DR PDB; 2VLR; X-ray; 2.30 A; D/I=1-89.
DR PDB; 2XN9; X-ray; 2.30 A; A=1-93.
DR PDB; 2XNA; X-ray; 2.10 A; A=1-93.
DR PDB; 3ARB; X-ray; 2.70 A; C=1-93.
DR PDB; 3ARD; X-ray; 3.01 A; C=1-93.
DR PDB; 3ARE; X-ray; 2.80 A; C=1-93.
DR PDB; 3ARF; X-ray; 2.90 A; C=1-93.
DR PDB; 3ARG; X-ray; 3.00 A; C=1-93.
DR PDB; 3D39; X-ray; 2.81 A; D=1-89.
DR PDB; 3DX9; X-ray; 2.75 A; A/C=1-90.
DR PDB; 3DXA; X-ray; 3.50 A; D/I/N=1-91.
DR PDB; 3FFC; X-ray; 2.80 A; D/I=1-89.
DR PDB; 3GSN; X-ray; 2.80 A; A=1-89.
DR PDB; 3HE7; X-ray; 2.80 A; C=1-93.
DR PDB; 3HG1; X-ray; 3.00 A; D=1-85.
DR PDB; 3KPR; X-ray; 2.60 A; D/I=1-89.
DR PDB; 3KPS; X-ray; 2.70 A; D=1-89.
DR PDB; 3KXF; X-ray; 3.10 A; D/G/M/N=1-89.
DR PDB; 3O4L; X-ray; 2.54 A; D=1-90.
DR PDB; 3O6F; X-ray; 2.80 A; C/G=1-90.
DR PDB; 3O8X; X-ray; 2.74 A; C=1-93.
DR PDB; 3O9W; X-ray; 2.80 A; C=1-93.
DR PDB; 3PWP; X-ray; 2.69 A; D=1-89.
DR PDB; 3QDG; X-ray; 2.69 A; D=1-89.
DR PDB; 3QDJ; X-ray; 2.30 A; D=1-89.
DR PDB; 3QDM; X-ray; 2.80 A; D=1-87.
DR PDB; 3QEQ; X-ray; 2.59 A; D=1-86.
DR PDB; 3QEU; X-ray; 2.09 A; A/D=1-91.
DR PDB; 3QIB; X-ray; 2.70 A; C=1-93.
DR PDB; 3QJF; X-ray; 2.40 A; A/C=1-93.
DR PDB; 3QUX; X-ray; 2.91 A; C=1-93.
DR PDB; 3SCM; X-ray; 2.50 A; C=1-93.
DR PDB; 3SDA; X-ray; 2.80 A; C=1-93.
DR PDB; 3SDC; X-ray; 3.10 A; C=1-93.
DR PDB; 3SDD; X-ray; 3.00 A; C=1-93.
DR PDB; 3SDX; X-ray; 3.12 A; E/G=1-90.
DR PDB; 3SJV; X-ray; 3.10 A; D/I/N/S=1-93.
DR PDB; 3SKN; X-ray; 2.90 A; A/C/E/G=1-93.
DR PDB; 3T0E; X-ray; 4.00 A; C=1-94.
DR PDB; 3TN0; X-ray; 3.20 A; C=1-93.
DR PDB; 3TVM; X-ray; 2.80 A; C/G=1-93.
DR PDB; 4APQ; X-ray; 3.00 A; C=1-93.
DR PDB; 4C56; X-ray; 2.90 A; A/G=1-93.
DR PDB; 4G8E; X-ray; 2.20 A; A=1-90.
DR PDB; 4G8F; X-ray; 2.10 A; A=1-93.
DR PDB; 4IRS; X-ray; 2.80 A; C=1-93.
DR PDB; 4JFD; X-ray; 2.46 A; D=1-86.
DR PDB; 4JFE; X-ray; 2.70 A; D=1-87.
DR PDB; 4JFF; X-ray; 2.43 A; D=1-87.
DR PDB; 4JFH; X-ray; 2.40 A; D=1-90.
DR PDB; 4JRX; X-ray; 2.30 A; D=1-89.
DR PDB; 4JRY; X-ray; 2.80 A; D=1-89.
DR PDB; 4MVB; X-ray; 3.09 A; A=1-93.
DR PDB; 4MXQ; X-ray; 2.60 A; C=1-93.
DR PDB; 4N0C; X-ray; 2.90 A; C/G=1-93.
DR PDB; 4N5E; X-ray; 3.06 A; C=1-93.
DR PDB; 4NHU; X-ray; 2.90 A; A/C=1-93.
DR PDB; 4ONH; X-ray; 3.01 A; A=1-93.
DR PDB; 4P4K; X-ray; 2.80 A; C/G=1-93.
DR PDB; 4PRH; X-ray; 2.50 A; D=1-93.
DR PDB; 4PRI; X-ray; 2.40 A; D=1-89.
DR PDB; 4PRP; X-ray; 2.50 A; D=1-89.
DR PDB; 4UDT; X-ray; 1.35 A; A=1-93.
DR PDB; 4UDU; X-ray; 2.50 A; A=1-93.
DR PDB; 4WW1; X-ray; 1.38 A; A=1-93.
DR PDB; 4WW2; X-ray; 2.48 A; A=1-93.
DR PDB; 4WWK; X-ray; 3.10 A; A=1-93.
DR PDB; 4X6B; X-ray; 2.10 A; A/C=1-93.
DR PDB; 4X6C; X-ray; 2.80 A; E/G=1-93.
DR PDB; 4X6D; X-ray; 2.98 A; E/G=1-93.
DR PDB; 4Y16; X-ray; 2.60 A; C=1-93.
DR PDB; 4Y2D; X-ray; 3.05 A; C/G=1-93.
DR PDB; 4Y4F; X-ray; 3.19 A; C/G=1-93.
DR PDB; 4Y4H; X-ray; 3.10 A; C/G=1-93.
DR PDB; 4Y4K; X-ray; 2.90 A; C=1-93.
DR PDB; 4ZDH; X-ray; 2.10 A; A=1-91.
DR PDB; 5BRZ; X-ray; 2.62 A; D=2-82.
DR PDB; 5BS0; X-ray; 2.40 A; D=1-82.
DR PDB; 5C07; X-ray; 2.11 A; D/I=1-88.
DR PDB; 5C08; X-ray; 2.33 A; D/I=1-80.
DR PDB; 5C09; X-ray; 2.48 A; D/I=1-90.
DR PDB; 5C0A; X-ray; 2.46 A; D/I=1-87.
DR PDB; 5C0B; X-ray; 2.03 A; D/I=1-89.
DR PDB; 5C0C; X-ray; 1.97 A; D/I=1-89.
DR PDB; 5EU6; X-ray; 2.02 A; D=1-87.
DR PDB; 5FK9; X-ray; 3.10 A; A=1-93.
DR PDB; 5FKA; X-ray; 2.40 A; A=1-93.
DR PDB; 5HHM; X-ray; 2.50 A; D/I=1-89.
DR PDB; 5HHO; X-ray; 2.95 A; D=1-89.
DR PDB; 5HYJ; X-ray; 3.06 A; D/I=1-82.
DR PDB; 5JZI; X-ray; 2.50 A; G/I=1-93.
DR PDB; 5KS9; X-ray; 2.55 A; E/G=1-93.
DR PDB; 5KSA; X-ray; 2.00 A; C=1-93.
DR PDB; 5KSB; X-ray; 2.90 A; E/G=1-93.
DR PDB; 5NQK; X-ray; 3.25 A; A=1-91.
DR PDB; 6DKP; X-ray; 2.97 A; D=1-89.
DR PDB; 6JXR; EM; 3.70 A; m=1-140.
DR PDB; 7NDT; X-ray; 3.00 A; DDD/III=1-85.
DR PDBsum; 1AO7; -.
DR PDBsum; 1BD2; -.
DR PDBsum; 1FYT; -.
DR PDBsum; 1J8H; -.
DR PDBsum; 1KGC; -.
DR PDBsum; 1MI5; -.
DR PDBsum; 1OGA; -.
DR PDBsum; 1QRN; -.
DR PDBsum; 1QSF; -.
DR PDBsum; 1YMM; -.
DR PDBsum; 1ZGL; -.
DR PDBsum; 2AK4; -.
DR PDBsum; 2BNQ; -.
DR PDBsum; 2BNR; -.
DR PDBsum; 2BNU; -.
DR PDBsum; 2CDF; -.
DR PDBsum; 2CDG; -.
DR PDBsum; 2ESV; -.
DR PDBsum; 2EYR; -.
DR PDBsum; 2EYS; -.
DR PDBsum; 2EYT; -.
DR PDBsum; 2F53; -.
DR PDBsum; 2F54; -.
DR PDBsum; 2GJ6; -.
DR PDBsum; 2IAL; -.
DR PDBsum; 2IAM; -.
DR PDBsum; 2IAN; -.
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; 3DX9; -.
DR PDBsum; 3DXA; -.
DR PDBsum; 3FFC; -.
DR PDBsum; 3GSN; -.
DR PDBsum; 3HE7; -.
DR PDBsum; 3HG1; -.
DR PDBsum; 3KPR; -.
DR PDBsum; 3KPS; -.
DR PDBsum; 3KXF; -.
DR PDBsum; 3O4L; -.
DR PDBsum; 3O6F; -.
DR PDBsum; 3O8X; -.
DR PDBsum; 3O9W; -.
DR PDBsum; 3PWP; -.
DR PDBsum; 3QDG; -.
DR PDBsum; 3QDJ; -.
DR PDBsum; 3QDM; -.
DR PDBsum; 3QEQ; -.
DR PDBsum; 3QEU; -.
DR PDBsum; 3QIB; -.
DR PDBsum; 3QJF; -.
DR PDBsum; 3QUX; -.
DR PDBsum; 3SCM; -.
DR PDBsum; 3SDA; -.
DR PDBsum; 3SDC; -.
DR PDBsum; 3SDD; -.
DR PDBsum; 3SDX; -.
DR PDBsum; 3SJV; -.
DR PDBsum; 3SKN; -.
DR PDBsum; 3T0E; -.
DR PDBsum; 3TN0; -.
DR PDBsum; 3TVM; -.
DR PDBsum; 4APQ; -.
DR PDBsum; 4C56; -.
DR PDBsum; 4G8E; -.
DR PDBsum; 4G8F; -.
DR PDBsum; 4IRS; -.
DR PDBsum; 4JFD; -.
DR PDBsum; 4JFE; -.
DR PDBsum; 4JFF; -.
DR PDBsum; 4JFH; -.
DR PDBsum; 4JRX; -.
DR PDBsum; 4JRY; -.
DR PDBsum; 4MVB; -.
DR PDBsum; 4MXQ; -.
DR PDBsum; 4N0C; -.
DR PDBsum; 4N5E; -.
DR PDBsum; 4NHU; -.
DR PDBsum; 4ONH; -.
DR PDBsum; 4P4K; -.
DR PDBsum; 4PRH; -.
DR PDBsum; 4PRI; -.
DR PDBsum; 4PRP; -.
DR PDBsum; 4UDT; -.
DR PDBsum; 4UDU; -.
DR PDBsum; 4WW1; -.
DR PDBsum; 4WW2; -.
DR PDBsum; 4WWK; -.
DR PDBsum; 4X6B; -.
DR PDBsum; 4X6C; -.
DR PDBsum; 4X6D; -.
DR PDBsum; 4Y16; -.
DR PDBsum; 4Y2D; -.
DR PDBsum; 4Y4F; -.
DR PDBsum; 4Y4H; -.
DR PDBsum; 4Y4K; -.
DR PDBsum; 4ZDH; -.
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; 5JZI; -.
DR PDBsum; 5KS9; -.
DR PDBsum; 5KSA; -.
DR PDBsum; 5KSB; -.
DR PDBsum; 5NQK; -.
DR PDBsum; 6DKP; -.
DR PDBsum; 6JXR; -.
DR PDBsum; 7NDT; -.
DR AlphaFoldDB; P01848; -.
DR SMR; P01848; -.
DR ComplexPortal; CPX-6482; Alpha-beta T cell receptor complex, TRBC2 variant.
DR ComplexPortal; CPX-6581; Alpha-beta T cell receptor complex, TRBC1 variant.
DR IntAct; P01848; 13.
DR ChEMBL; CHEMBL3580506; -.
DR DrugBank; DB02740; 3-Indolebutyric Acid.
DR IMGT_GENE-DB; TRAC; -.
DR GlyGen; P01848; 4 sites.
DR iPTMnet; P01848; -.
DR PhosphoSitePlus; P01848; -.
DR BioMuta; TRAC; -.
DR DMDM; 135511; -.
DR jPOST; P01848; -.
DR MassIVE; P01848; -.
DR PeptideAtlas; P01848; -.
DR PRIDE; P01848; -.
DR ProteomicsDB; 51491; -.
DR UCSC; uc058zhj.1; human.
DR GeneCards; TRAC; -.
DR HGNC; HGNC:12029; TRAC.
DR MalaCards; TRAC; -.
DR MIM; 186880; gene.
DR MIM; 615387; phenotype.
DR neXtProt; NX_P01848; -.
DR Orphanet; 397959; TCR-alpha-beta-positive T-cell deficiency.
DR HOGENOM; CLU_092098_1_0_1; -.
DR InParanoid; P01848; -.
DR OMA; DFPCNAT; -.
DR PhylomeDB; P01848; -.
DR PathwayCommons; P01848; -.
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; P01848; -.
DR SIGNOR; P01848; -.
DR ChiTaRS; TRAC; human.
DR EvolutionaryTrace; P01848; -.
DR Pharos; P01848; Tdark.
DR PRO; PR:P01848; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P01848; protein.
DR GO; GO:0042105; C:alpha-beta T cell receptor complex; IPI:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
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:0009617; P:response to bacterium; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IC:ComplexPortal.
DR CDD; cd07688; IgC_TCR_alpha; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015370; TCR_alpha_C.
DR Pfam; PF09291; DUF1968; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Membrane; Receptor; Reference proteome;
KW T cell receptor; Transmembrane; Transmembrane helix.
FT CHAIN <1..140
FT /note="T cell receptor alpha chain constant"
FT /id="PRO_0000184524"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:27791034"
FT TOPO_DOM 139..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..107
FT /note="Ig-like C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 94..115
FT /note="Connecting peptide"
FT /evidence="ECO:0000305|PubMed:27791034"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 22..72
FT /evidence="ECO:0000269|PubMed:12796775"
FT DISULFID 94
FT /note="Interchain (with C-130 in TRBC1 or TRBC2)"
FT /evidence="ECO:0000305|PubMed:27791034"
FT MUTAGEN 130
FT /note="N->L,F: Impairs TR-CD3 complex assembly."
FT /evidence="ECO:0000269|PubMed:27791034"
FT NON_TER 1
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:4N0C"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5C0C"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:4UDT"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:4UDT"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2BNU"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:4UDT"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:4UDT"
SQ SEQUENCE 140 AA; 15717 MW; CF6B38A0F653035D CRC64;
IQNPDPAVYQ LRDSKSSDKS VCLFTDFDSQ TNVSQSKDSD VYITDKTVLD MRSMDFKSNS
AVAWSNKSDF ACANAFNNSI IPEDTFFPSP ESSCDVKLVE KSFETDTNLN FQNLSVIGFR
ILLLKVAGFN LLMTLRLWSS
