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Database: UniProt
Entry: Q6ISU1
LinkDB: Q6ISU1
Original site: Q6ISU1 
ID   PTCRA_HUMAN             Reviewed;         281 AA.
AC   Q6ISU1; Q5TFZ7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   10-FEB-2021, entry version 128.
DE   RecName: Full=Pre T-cell antigen receptor alpha;
DE            Short=pT-alpha;
DE            Short=pTa;
DE   AltName: Full=pT-alpha-TCR;
DE   Flags: Precursor;
GN   Name=PTCRA;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Thymus;
RX   PubMed=8618853; DOI=10.1073/pnas.92.26.12105;
RA   Del Porto P., Bruno L., Mattei M.-G., von Boehmer H., Saint-Ruf C.;
RT   "Cloning and comparative analysis of the human pre-T-cell receptor alpha-
RT   chain gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:12105-12109(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Lymphoblast;
RX   PubMed=9842925;
RX   DOI=10.1002/(sici)1521-4141(199811)28:11<3824::aid-immu3824>3.0.co;2-9;
RA   Saint-Ruf C., Lechner O., Feinberg J., von Boehmer H.;
RT   "Genomic structure of the human pre-T cell receptor alpha chain and
RT   expression of two mRNA isoforms.";
RL   Eur. J. Immunol. 28:3824-3831(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RA   Ramiro A.R., Toribio M.L.;
RT   "Alternatively spliced human pre-T alpha chain, mRNA.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-106.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-281 (ISOFORM 1), SUBUNIT, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Thymus;
RX   PubMed=8760805; DOI=10.1084/jem.184.2.519;
RA   Ramiro A.R., Trigueros C., Marquez C., San Millan J.L., Toribio M.L.;
RT   "Regulation of pre-T cell receptor (pT alpha-TCR beta) gene expression
RT   during human thymic development.";
RL   J. Exp. Med. 184:519-530(1996).
RN   [7]
RP   INTERACTION WITH RHBDD1.
RX   PubMed=22795130; DOI=10.1016/j.molcel.2012.06.008;
RA   Fleig L., Bergbold N., Sahasrabudhe P., Geiger B., Kaltak L., Lemberg M.K.;
RT   "Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of
RT   membrane proteins.";
RL   Mol. Cell 47:558-569(2012).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 17-135, SUBUNIT, DISULFIDE BOND,
RP   AND GLYCOSYLATION AT ASN-67.
RX   PubMed=20944746; DOI=10.1038/nature09448;
RA   Pang S.S., Berry R., Chen Z., Kjer-Nielsen L., Perugini M.A., King G.F.,
RA   Wang C., Chew S.H., La Gruta N.L., Williams N.K., Beddoe T., Tiganis T.,
RA   Cowieson N.P., Godfrey D.I., Purcell A.W., Wilce M.C., McCluskey J.,
RA   Rossjohn J.;
RT   "The structural basis for autonomous dimerization of the pre-T-cell antigen
RT   receptor.";
RL   Nature 467:844-848(2010).
CC   -!- FUNCTION: The pre-T-cell receptor complex (composed of PTCRA, TCRB and
CC       the CD3 complex) regulates early T-cell development. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with TCRB; disulfide linked. This heterodimer
CC       assembles with CD3 proteins into a signaling-competent pre-T-cell
CC       receptor complex. Interacts with RHBDD1. {ECO:0000269|PubMed:20944746,
CC       ECO:0000269|PubMed:22795130, ECO:0000269|PubMed:8760805}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=pTalpha-1;
CC         IsoId=Q6ISU1-1; Sequence=Displayed;
CC       Name=2; Synonyms=pTalpha-2;
CC         IsoId=Q6ISU1-2; Sequence=VSP_031445;
CC       Name=3;
CC         IsoId=Q6ISU1-3; Sequence=VSP_031446;
CC   -!- TISSUE SPECIFICITY: Expressed in immature but not mature T-cells. Also
CC       found in CD34+ cells from peripheral blood, CD34+ precursors from
CC       umbilical cord blood and adult bone marrow.
CC       {ECO:0000269|PubMed:8618853, ECO:0000269|PubMed:8760805}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal life in CD34+ progenitors
CC       present in the liver at 18 weeks of gestation but is absent in CD34+
CC       precursors from fetal bone marrow at any developmental stage up to 22
CC       weeks. {ECO:0000269|PubMed:8760805}.
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DR   EMBL; U36759; AAB06194.1; -; mRNA.
DR   EMBL; AF084941; AAC83346.1; -; Genomic_DNA.
DR   EMBL; AF101436; AAF21890.1; -; mRNA.
DR   EMBL; AF165312; AAF89556.1; -; mRNA.
DR   EMBL; AL035587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC069336; AAH69336.1; -; mRNA.
DR   EMBL; BC100771; AAI00772.1; -; mRNA.
DR   EMBL; BC100772; AAI00773.1; -; mRNA.
DR   EMBL; BC100773; AAI00774.1; -; mRNA.
DR   EMBL; BC100774; AAI00775.1; -; mRNA.
DR   EMBL; BC153829; AAI53830.1; -; mRNA.
DR   EMBL; U38996; AAB18373.1; -; mRNA.
DR   CCDS; CCDS4874.1; -. [Q6ISU1-1]
DR   CCDS; CCDS59019.1; -. [Q6ISU1-3]
DR   CCDS; CCDS59020.1; -. [Q6ISU1-2]
DR   RefSeq; NP_001230097.1; NM_001243168.1.
DR   RefSeq; NP_001230098.1; NM_001243169.1. [Q6ISU1-3]
DR   RefSeq; NP_001230099.1; NM_001243170.1. [Q6ISU1-2]
DR   RefSeq; NP_612153.2; NM_138296.2. [Q6ISU1-1]
DR   PDB; 3OF6; X-ray; 2.80 A; D/E/F=17-135.
DR   PDBsum; 3OF6; -.
DR   SMR; Q6ISU1; -.
DR   BioGRID; 128144; 10.
DR   IntAct; Q6ISU1; 4.
DR   MINT; Q6ISU1; -.
DR   STRING; 9606.ENSP00000477815; -.
DR   GlyGen; Q6ISU1; 1 site.
DR   iPTMnet; Q6ISU1; -.
DR   PhosphoSitePlus; Q6ISU1; -.
DR   BioMuta; PTCRA; -.
DR   DMDM; 74736631; -.
DR   PaxDb; Q6ISU1; -.
DR   PRIDE; Q6ISU1; -.
DR   ProteomicsDB; 66497; -. [Q6ISU1-1]
DR   ProteomicsDB; 66498; -. [Q6ISU1-2]
DR   ProteomicsDB; 66499; -. [Q6ISU1-3]
DR   Antibodypedia; 57244; 119 antibodies.
DR   Ensembl; ENST00000304672; ENSP00000304447; ENSG00000171611. [Q6ISU1-1]
DR   Ensembl; ENST00000441198; ENSP00000409550; ENSG00000171611. [Q6ISU1-3]
DR   Ensembl; ENST00000446507; ENSP00000392288; ENSG00000171611. [Q6ISU1-2]
DR   GeneID; 171558; -.
DR   KEGG; hsa:171558; -.
DR   UCSC; uc003osx.4; human. [Q6ISU1-1]
DR   CTD; 171558; -.
DR   DisGeNET; 171558; -.
DR   GeneCards; PTCRA; -.
DR   HGNC; HGNC:21290; PTCRA.
DR   HPA; ENSG00000171611; Group enriched (blood, lymphoid tissue).
DR   MIM; 606817; gene.
DR   neXtProt; NX_Q6ISU1; -.
DR   OpenTargets; ENSG00000171611; -.
DR   PharmGKB; PA134993184; -.
DR   VEuPathDB; HostDB:ENSG00000171611.9; -.
DR   eggNOG; ENOG502SAGI; Eukaryota.
DR   GeneTree; ENSGT00390000007712; -.
DR   HOGENOM; CLU_082600_0_0_1; -.
DR   InParanoid; Q6ISU1; -.
DR   OrthoDB; 1383750at2759; -.
DR   PhylomeDB; Q6ISU1; -.
DR   TreeFam; TF337868; -.
DR   PathwayCommons; Q6ISU1; -.
DR   Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
DR   SIGNOR; Q6ISU1; -.
DR   BioGRID-ORCS; 171558; 5 hits in 874 CRISPR screens.
DR   EvolutionaryTrace; Q6ISU1; -.
DR   GenomeRNAi; 171558; -.
DR   Pharos; Q6ISU1; Tbio.
DR   PRO; PR:Q6ISU1; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q6ISU1; protein.
DR   Bgee; ENSG00000171611; Expressed in cingulate cortex and 196 other tissues.
DR   ExpressionAtlas; Q6ISU1; baseline and differential.
DR   Genevisible; Q6ISU1; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR027834; PTCRA.
DR   PANTHER; PTHR37866; PTHR37866; 1.
DR   Pfam; PF15028; PTCRA; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW   Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..281
FT                   /note="Pre T-cell antigen receptor alpha"
FT                   /id="PRO_0000319108"
FT   TOPO_DOM        24..146
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..281
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:20944746"
FT   DISULFID        47..107
FT                   /evidence="ECO:0000269|PubMed:20944746"
FT   DISULFID        135
FT                   /note="Interchain (with TCRB)"
FT                   /evidence="ECO:0000305|PubMed:20944746"
FT   VAR_SEQ         20..126
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_031445"
FT   VAR_SEQ         21..59
FT                   /note="VGGTPFPSLAPPIMLLVDGKQQMVVVCLVLDVAPPGLDS -> PVSFPSSPE
FT                   AATTG (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_031446"
FT   VARIANT         106
FT                   /note="V -> I (in dbSNP:rs9471966)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_038957"
FT   VARIANT         183
FT                   /note="A -> T (in dbSNP:rs36111725)"
FT                   /id="VAR_038958"
FT   CONFLICT        256
FT                   /note="A -> R (in Ref. 1; AAB06194, 2; AAC83346, 3;
FT                   AAF89556 and 6; AAB18373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        269
FT                   /note="A -> R (in Ref. 1; AAB06194)"
FT                   /evidence="ECO:0000305"
FT   STRAND          33..52
FT                   /evidence="ECO:0000244|PDB:3OF6"
FT   STRAND          62..64
FT                   /evidence="ECO:0000244|PDB:3OF6"
FT   STRAND          66..68
FT                   /evidence="ECO:0000244|PDB:3OF6"
FT   STRAND          79..81
FT                   /evidence="ECO:0000244|PDB:3OF6"
FT   TURN            82..84
FT                   /evidence="ECO:0000244|PDB:3OF6"
FT   STRAND          85..95
FT                   /evidence="ECO:0000244|PDB:3OF6"
FT   HELIX           96..100
FT                   /evidence="ECO:0000244|PDB:3OF6"
FT   STRAND          104..109
FT                   /evidence="ECO:0000244|PDB:3OF6"
SQ   SEQUENCE   281 AA;  29266 MW;  A49B86A151619B9F CRC64;
     MAGTWLLLLL ALGCPALPTG VGGTPFPSLA PPIMLLVDGK QQMVVVCLVL DVAPPGLDSP
     IWFSAGNGSA LDAFTYGPSP ATDGTWTNLA HLSLPSEELA SWEPLVCHTG PGAEGHSRST
     QPMHLSGEAS TARTCPQEPL RGTPGGALWL GVLRLLLFKL LLFDLLLTCS CLCDPAGPLP
     SPATTTRLRA LGSHRLHPAT ETGGREATSS PRPQPRDRRW GDTPPGRKPG SPVWGEGSYL
     SSYPTCPAQA WCSRSALRAP SSSLGAFFAG DLPPPLQAGA A
//
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