THY1_HUMAN
ID THY1_HUMAN Reviewed; 161 AA.
AC P04216; Q16008; Q9NSP1;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Thy-1 membrane glycoprotein;
DE AltName: Full=CDw90;
DE AltName: Full=Thy-1 antigen;
DE AltName: CD_antigen=CD90;
DE Flags: Precursor;
GN Name=THY1;
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].
RX PubMed=2864690; DOI=10.1073/pnas.82.19.6657;
RA Seki T., Spurr N., Obata F., Goyert S., Goodfellow P., Silver J.;
RT "The human Thy-1 gene: structure and chromosomal location.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6657-6661(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10944468; DOI=10.1006/bbrc.2000.3282;
RA Ye Z., Connor J.R.;
RT "cDNA cloning by amplification of circularized first strand cDNAs reveals
RT non-IRE-regulated iron-responsive mRNAs.";
RL Biochem. Biophys. Res. Commun. 275:223-227(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-55.
RX PubMed=7683034; DOI=10.1084/jem.177.5.1331;
RA Craig W., Kay R., Cutler R.L., Lansdorp P.M.;
RT "Expression of Thy-1 on human hematopoietic progenitor cells.";
RL J. Exp. Med. 177:1331-1342(1993).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-42 AND ASN-119.
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).
CC -!- FUNCTION: May play a role in cell-cell or cell-ligand interactions
CC during synaptogenesis and other events in the brain.
CC -!- INTERACTION:
CC P04216; P05067: APP; NbExp=3; IntAct=EBI-9071715, EBI-77613;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/THY1ID45672ch11q23.html";
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DR EMBL; M11749; AAA61180.1; -; Genomic_DNA.
DR EMBL; AF261093; AAG13904.1; -; mRNA.
DR EMBL; AL161958; CAB82306.1; -; mRNA.
DR EMBL; BC065559; AAH65559.1; -; mRNA.
DR EMBL; S59749; AAB26353.2; -; mRNA.
DR CCDS; CCDS8424.1; -.
DR PIR; A02106; TDHU.
DR PIR; T47130; T47130.
DR RefSeq; NP_001298089.1; NM_001311160.1.
DR RefSeq; NP_001298091.1; NM_001311162.1.
DR RefSeq; NP_006279.2; NM_006288.4.
DR AlphaFoldDB; P04216; -.
DR SMR; P04216; -.
DR BioGRID; 112926; 41.
DR IntAct; P04216; 9.
DR MINT; P04216; -.
DR STRING; 9606.ENSP00000284240; -.
DR GlyConnect; 1808; 3 N-Linked glycans (3 sites).
DR GlyGen; P04216; 4 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; P04216; -.
DR PhosphoSitePlus; P04216; -.
DR SwissPalm; P04216; -.
DR BioMuta; THY1; -.
DR DMDM; 20455514; -.
DR CPTAC; CPTAC-1511; -.
DR EPD; P04216; -.
DR jPOST; P04216; -.
DR MassIVE; P04216; -.
DR MaxQB; P04216; -.
DR PaxDb; P04216; -.
DR PeptideAtlas; P04216; -.
DR PRIDE; P04216; -.
DR ProteomicsDB; 51683; -.
DR ABCD; P04216; 1 sequenced antibody.
DR Antibodypedia; 671; 2107 antibodies from 47 providers.
DR DNASU; 7070; -.
DR Ensembl; ENST00000284240.10; ENSP00000284240.6; ENSG00000154096.14.
DR Ensembl; ENST00000528522.5; ENSP00000431301.1; ENSG00000154096.14.
DR GeneID; 7070; -.
DR KEGG; hsa:7070; -.
DR MANE-Select; ENST00000284240.10; ENSP00000284240.6; NM_006288.5; NP_006279.2.
DR UCSC; uc001pwr.4; human.
DR CTD; 7070; -.
DR DisGeNET; 7070; -.
DR GeneCards; THY1; -.
DR HGNC; HGNC:11801; THY1.
DR HPA; ENSG00000154096; Tissue enhanced (brain, smooth muscle, urinary bladder).
DR MIM; 188230; gene.
DR neXtProt; NX_P04216; -.
DR OpenTargets; ENSG00000154096; -.
DR PharmGKB; PA36510; -.
DR VEuPathDB; HostDB:ENSG00000154096; -.
DR eggNOG; ENOG502S18P; Eukaryota.
DR GeneTree; ENSGT00390000012352; -.
DR HOGENOM; CLU_136861_0_0_1; -.
DR InParanoid; P04216; -.
DR OMA; MNPAIGI; -.
DR OrthoDB; 1504363at2759; -.
DR PhylomeDB; P04216; -.
DR TreeFam; TF336059; -.
DR PathwayCommons; P04216; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; P04216; -.
DR SIGNOR; P04216; -.
DR BioGRID-ORCS; 7070; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; THY1; human.
DR GeneWiki; CD90; -.
DR GenomeRNAi; 7070; -.
DR Pharos; P04216; Tbio.
DR PRO; PR:P04216; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P04216; protein.
DR Bgee; ENSG00000154096; Expressed in prefrontal cortex and 188 other tissues.
DR ExpressionAtlas; P04216; baseline and differential.
DR Genevisible; P04216; HS.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
DR GO; GO:0030673; C:axolemma; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0032590; C:dendrite membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0034235; F:GPI anchor binding; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IMP:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0070571; P:negative regulation of neuron projection regeneration; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; IDA:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0043113; P:receptor clustering; ISS:UniProtKB.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:2000298; P:regulation of Rho-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0046549; P:retinal cone cell development; ISS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
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 InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR033292; THY1.
DR PANTHER; PTHR19226; PTHR19226; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT SIGNAL 1..19
FT CHAIN 20..130
FT /note="Thy-1 membrane glycoprotein"
FT /id="PRO_0000014973"
FT PROPEP 131..161
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000014974"
FT DOMAIN 20..126
FT /note="Ig-like V-type"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P01831"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01830"
FT LIPID 130
FT /note="GPI-anchor amidated cysteine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 28..130
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 38..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 54..55
FT /note="LT -> AP (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="N -> H (in Ref. 1; AAA61180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 17935 MW; 2B6796DA8EE7454B CRC64;
MNLAISIALL LTVLQVSRGQ KVTSLTACLV DQSLRLDCRH ENTSSSPIQY EFSLTRETKK
HVLFGTVGVP EHTYRSRTNF TSKYNMKVLY LSAFTSKDEG TYTCALHHSG HSPPISSQNV
TVLRDKLVKC EGISLLAQNT SWLLLLLLSL SLLQATDFMS L
