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Protein

T-cell receptor alpha chain C region

Gene

TRAC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_12555. Downstream TCR signaling.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
REACT_19324. PD-1 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
T-cell receptor alpha chain C region
Gene namesi
Name:TRAC
Synonyms:TCRA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:12029. TRAC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei118 – 13720HelicalSequence AnalysisAdd
BLAST
Topological domaini138 – 1425CytoplasmicSequence Analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency 7 (IMD7)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA primary immunodeficiency disorder manifesting with recurrent respiratory infections, candidiasis, diarrhea, and failure to thrive. Patients show a clear predisposition to herpes viral infections, and features of immune dysregulation, including hypereosinophilia, vitiligo, and alopecia areata. Other features include lymphadenopathy and hepatosplenomegaly. CD3+ T-cells express TCR-gamma/delta, but little or no TCR-alpha/beta.

See also OMIM:615387

Organism-specific databases

MIMi615387. phenotype.
Orphaneti397959. TCR-alpha-beta-positive T-cell deficiency.

Polymorphism and mutation databases

DMDMi135511.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 142›142T-cell receptor alpha chain C regionPRO_0000184524Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 741 Publication
Glycosylationi34 – 341N-linked (GlcNAc...)1 Publication
Glycosylationi61 – 611N-linked (GlcNAc...); atypical1 Publication
Glycosylationi68 – 681N-linked (GlcNAc...)1 Publication
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP01848.
PRIDEiP01848.

Expressioni

Gene expression databases

GenevestigatoriP01848.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TRBC1P018501EBI-1034847,EBI-1034839

Protein-protein interaction databases

IntActiP01848. 2 interactions.
MINTiMINT-249869.
STRINGi9606.ENSP00000411560.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 2012Combined sources
Beta strandi22 – 287Combined sources
Beta strandi40 – 423Combined sources
Beta strandi43 – 453Combined sources
Beta strandi49 – 535Combined sources
Helixi54 – 563Combined sources
Beta strandi58 – 6811Combined sources
Beta strandi69 – 713Combined sources
Turni74 – 807Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FYTX-ray2.60D1-99[»]
1J8HX-ray2.40D1-99[»]
1KGCX-ray1.50D1-95[»]
1MI5X-ray2.50D1-91[»]
1OGAX-ray1.40D1-97[»]
1QRNX-ray2.80D1-91[»]
1QSFX-ray2.80D1-91[»]
1YMMX-ray3.50D2-96[»]
1ZGLX-ray2.80M/Q/S/U1-96[»]
2AK4X-ray2.50D/I/N/T1-95[»]
2BNQX-ray1.70D1-91[»]
2BNRX-ray1.90D1-91[»]
2BNUX-ray1.40A1-91[»]
2CDFX-ray2.25A1-80[»]
2CDGX-ray2.60A1-80[»]
2ESVX-ray2.60D1-91[»]
2EYRX-ray2.40A3-95[»]
2EYSX-ray2.21A3-95[»]
2EYTX-ray2.60A/C3-95[»]
2F53X-ray2.10D3-79[»]
2F54X-ray2.70D/K3-93[»]
2GJ6X-ray2.56D1-91[»]
2IALX-ray1.92A/C1-95[»]
2IAMX-ray2.80C1-95[»]
2IANX-ray2.80D/I/N/S1-95[»]
2NX5X-ray2.70D/I/N/T1-79[»]
2P5EX-ray1.89D1-81[»]
2P5WX-ray2.20D3-79[»]
2PO6X-ray3.20C/G3-92[»]
2PYEX-ray2.30D1-81[»]
2PYFX-ray2.20A3-93[»]
2VLJX-ray2.40D1-91[»]
2VLKX-ray2.50D1-91[»]
2VLMX-ray1.98D1-91[»]
2VLRX-ray2.30D/I1-91[»]
2XN9X-ray2.30A1-95[»]
2XNAX-ray2.10A1-95[»]
3ARBX-ray2.70C1-95[»]
3ARDX-ray3.01C1-95[»]
3AREX-ray2.80C1-95[»]
3ARFX-ray2.90C1-95[»]
3ARGX-ray3.00C1-95[»]
3D39X-ray2.81D1-91[»]
3DX9X-ray2.75A/C3-92[»]
3DXAX-ray3.50D/I/N3-93[»]
3FFCX-ray2.80D/I1-91[»]
3GSNX-ray2.80A1-91[»]
3HE7X-ray2.80C1-95[»]
3HG1X-ray3.00D1-87[»]
3KPRX-ray2.60D/I1-91[»]
3KPSX-ray2.70D1-91[»]
3KXFX-ray3.10D/G/M/N1-91[»]
3O4LX-ray2.54D1-92[»]
3O6FX-ray2.80C/G1-92[»]
3O8XX-ray2.74C1-95[»]
3O9WX-ray2.80C1-95[»]
3PWPX-ray2.69D1-91[»]
3QDGX-ray2.69D1-91[»]
3QDJX-ray2.30D1-91[»]
3QDMX-ray2.80D1-89[»]
3QEQX-ray2.59D1-88[»]
3QEUX-ray2.09A/D1-93[»]
3QIBX-ray2.70C1-95[»]
3QJFX-ray2.40A/C1-95[»]
3QUXX-ray2.91C1-95[»]
3SCMX-ray2.50C1-95[»]
3SDAX-ray2.80C1-95[»]
3SDCX-ray3.10C1-95[»]
3SDDX-ray3.00C1-95[»]
3SDXX-ray3.12E/G1-92[»]
3SJVX-ray3.10D/I/N/S1-95[»]
3SKNX-ray2.90A/C/E/G1-95[»]
3T0EX-ray4.00C1-96[»]
3TN0X-ray3.20C1-95[»]
3TVMX-ray2.80C/G1-95[»]
4APQX-ray3.00C1-95[»]
4C56X-ray2.90A/G2-95[»]
4G8EX-ray2.20A2-92[»]
4G8FX-ray2.10A2-95[»]
4IRSX-ray2.80C1-95[»]
4JFDX-ray2.46D1-88[»]
4JFEX-ray2.70D1-89[»]
4JFFX-ray2.43D1-89[»]
4JFHX-ray2.40D1-92[»]
4JRXX-ray2.30D1-91[»]
4JRYX-ray2.80D1-91[»]
4ONHX-ray3.01A1-95[»]
4PRHX-ray2.50D1-95[»]
4PRIX-ray2.40D1-91[»]
4PRPX-ray2.50D1-91[»]
ProteinModelPortaliP01848.
SMRiP01848. Positions 1-91.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01848.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 117117C regionAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG45691.
HOVERGENiHBG017898.
InParanoidiP01848.
PhylomeDBiP01848.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR015370. DUF1968.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF09291. DUF1968. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01848-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
PNIQNPDPAV YQLRDSKSSD KSVCLFTDFD SQTNVSQSKD SDVYITDKTV
60 70 80 90 100
LDMRSMDFKS NSAVAWSNKS DFACANAFNN SIIPEDTFFP SPESSCDVKL
110 120 130 140
VEKSFETDTN LNFQNLSVIG FRILLLKVAG FNLLMTLRLW SS
Length:142
Mass (Da):15,928
Last modified:July 21, 1986 - v1
Checksum:iD46B44171D5784EE
GO

Sequence cautioni

The sequence CAA26435.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02592 mRNA. Translation: CAA26435.1. Different initiation.
PIRiS18893. RWHUAC.
UniGeneiHs.74647.

Genome annotation databases

UCSCiuc001wdg.1. human.

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02592 mRNA. Translation: CAA26435.1. Different initiation.
PIRiS18893. RWHUAC.
UniGeneiHs.74647.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FYTX-ray2.60D1-99[»]
1J8HX-ray2.40D1-99[»]
1KGCX-ray1.50D1-95[»]
1MI5X-ray2.50D1-91[»]
1OGAX-ray1.40D1-97[»]
1QRNX-ray2.80D1-91[»]
1QSFX-ray2.80D1-91[»]
1YMMX-ray3.50D2-96[»]
1ZGLX-ray2.80M/Q/S/U1-96[»]
2AK4X-ray2.50D/I/N/T1-95[»]
2BNQX-ray1.70D1-91[»]
2BNRX-ray1.90D1-91[»]
2BNUX-ray1.40A1-91[»]
2CDFX-ray2.25A1-80[»]
2CDGX-ray2.60A1-80[»]
2ESVX-ray2.60D1-91[»]
2EYRX-ray2.40A3-95[»]
2EYSX-ray2.21A3-95[»]
2EYTX-ray2.60A/C3-95[»]
2F53X-ray2.10D3-79[»]
2F54X-ray2.70D/K3-93[»]
2GJ6X-ray2.56D1-91[»]
2IALX-ray1.92A/C1-95[»]
2IAMX-ray2.80C1-95[»]
2IANX-ray2.80D/I/N/S1-95[»]
2NX5X-ray2.70D/I/N/T1-79[»]
2P5EX-ray1.89D1-81[»]
2P5WX-ray2.20D3-79[»]
2PO6X-ray3.20C/G3-92[»]
2PYEX-ray2.30D1-81[»]
2PYFX-ray2.20A3-93[»]
2VLJX-ray2.40D1-91[»]
2VLKX-ray2.50D1-91[»]
2VLMX-ray1.98D1-91[»]
2VLRX-ray2.30D/I1-91[»]
2XN9X-ray2.30A1-95[»]
2XNAX-ray2.10A1-95[»]
3ARBX-ray2.70C1-95[»]
3ARDX-ray3.01C1-95[»]
3AREX-ray2.80C1-95[»]
3ARFX-ray2.90C1-95[»]
3ARGX-ray3.00C1-95[»]
3D39X-ray2.81D1-91[»]
3DX9X-ray2.75A/C3-92[»]
3DXAX-ray3.50D/I/N3-93[»]
3FFCX-ray2.80D/I1-91[»]
3GSNX-ray2.80A1-91[»]
3HE7X-ray2.80C1-95[»]
3HG1X-ray3.00D1-87[»]
3KPRX-ray2.60D/I1-91[»]
3KPSX-ray2.70D1-91[»]
3KXFX-ray3.10D/G/M/N1-91[»]
3O4LX-ray2.54D1-92[»]
3O6FX-ray2.80C/G1-92[»]
3O8XX-ray2.74C1-95[»]
3O9WX-ray2.80C1-95[»]
3PWPX-ray2.69D1-91[»]
3QDGX-ray2.69D1-91[»]
3QDJX-ray2.30D1-91[»]
3QDMX-ray2.80D1-89[»]
3QEQX-ray2.59D1-88[»]
3QEUX-ray2.09A/D1-93[»]
3QIBX-ray2.70C1-95[»]
3QJFX-ray2.40A/C1-95[»]
3QUXX-ray2.91C1-95[»]
3SCMX-ray2.50C1-95[»]
3SDAX-ray2.80C1-95[»]
3SDCX-ray3.10C1-95[»]
3SDDX-ray3.00C1-95[»]
3SDXX-ray3.12E/G1-92[»]
3SJVX-ray3.10D/I/N/S1-95[»]
3SKNX-ray2.90A/C/E/G1-95[»]
3T0EX-ray4.00C1-96[»]
3TN0X-ray3.20C1-95[»]
3TVMX-ray2.80C/G1-95[»]
4APQX-ray3.00C1-95[»]
4C56X-ray2.90A/G2-95[»]
4G8EX-ray2.20A2-92[»]
4G8FX-ray2.10A2-95[»]
4IRSX-ray2.80C1-95[»]
4JFDX-ray2.46D1-88[»]
4JFEX-ray2.70D1-89[»]
4JFFX-ray2.43D1-89[»]
4JFHX-ray2.40D1-92[»]
4JRXX-ray2.30D1-91[»]
4JRYX-ray2.80D1-91[»]
4ONHX-ray3.01A1-95[»]
4PRHX-ray2.50D1-95[»]
4PRIX-ray2.40D1-91[»]
4PRPX-ray2.50D1-91[»]
ProteinModelPortaliP01848.
SMRiP01848. Positions 1-91.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01848. 2 interactions.
MINTiMINT-249869.
STRINGi9606.ENSP00000411560.

Polymorphism and mutation databases

DMDMi135511.

Proteomic databases

PaxDbiP01848.
PRIDEiP01848.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc001wdg.1. human.

Organism-specific databases

GeneCardsiGC14P023790.
HGNCiHGNC:12029. TRAC.
MIMi186880. gene.
615387. phenotype.
neXtProtiNX_P01848.
Orphaneti397959. TCR-alpha-beta-positive T-cell deficiency.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG45691.
HOVERGENiHBG017898.
InParanoidiP01848.
PhylomeDBiP01848.

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_12555. Downstream TCR signaling.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
REACT_19324. PD-1 signaling.

Miscellaneous databases

EvolutionaryTraceiP01848.
PROiP01848.
SOURCEiSearch...

Gene expression databases

GenevestigatoriP01848.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR015370. DUF1968.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF09291. DUF1968. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The chromosomal location of T-cell receptor genes and a T cell rearranging gene: possible correlation with specific translocations in human T cell leukaemia."
    Rabbitts T.H., Lefranc M.P., Stinson M.A., Sims J.E., Schroder J., Steinmetz M., Spurr N.L., Solomon E., Goodfellow P.N.
    EMBO J. 4:1461-1465(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Analysis of cDNA clones specific for human T cells and the alpha and beta chains of the T-cell receptor heterodimer from a human T-cell line."
    Yanagi Y., Chan A., Chin B., Minden M., Mak T.W.
    Proc. Natl. Acad. Sci. U.S.A. 82:3430-3434(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (CLONE PY14).
  3. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-34; ASN-61 AND ASN-68.
    Tissue: Leukemic T-cell.
  4. "Mutation in the TCRalpha subunit constant gene (TRAC) leads to a human immunodeficiency disorder characterized by a lack of TCRalphabeta+ T cells."
    Morgan N.V., Goddard S., Cardno T.S., McDonald D., Rahman F., Barge D., Ciupek A., Straatman-Iwanowska A., Pasha S., Guckian M., Anderson G., Huissoon A., Cant A., Tate W.P., Hambleton S., Maher E.R.
    J. Clin. Invest. 121:695-702(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN IMD7.
  5. "The 1.5 A crystal structure of a highly selected antiviral T cell receptor provides evidence for a structural basis of immunodominance."
    Kjer-Nielsen L., Clements C.S., Brooks A.G., Purcell A.W., McCluskey J., Rossjohn J.
    Structure 10:1521-1532(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-95.
  6. "A structural basis for immunodominant human T cell receptor recognition."
    Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I., Jones E.Y.
    Nat. Immunol. 4:657-663(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-93 IN COMPLEX WITH HLA-A/B2M HETERODIMER AND TRBC1, DISULFIDE BOND.
  7. "Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule."
    Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A.
    EMBO J. 24:2968-2979(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 3-96 IN COMPLEX WITH HLA-DRA/HLA-DRB5 HETERODIMER AND MBP PEPTIDE.

Entry informationi

Entry nameiTCA_HUMAN
AccessioniPrimary (citable) accession number: P01848
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 27, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

This clone was isolated from a human leukemic T-cell line, Jurkat.
This alpha chain C region shows sequence homology to its beta chain counterpart.
The gene corresponding to this mRNA is rearranged specifically in T-cells; its organization is similar to an Ig gene, with V, D, J, and C regions.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.