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   27-MAR-2024, entry version 220.
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="https://atlasgeneticsoncology.org/gene/45672/THY1";
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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; 44.
DR   IntAct; P04216; 10.
DR   MINT; P04216; -.
DR   STRING; 9606.ENSP00000284240; -.
DR   GlyConnect; 1808; 3 N-Linked glycans (3 sites).
DR   GlyCosmos; P04216; 4 sites, 2 glycans.
DR   GlyGen; P04216; 5 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
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; 9606-ENSP00000284240; -.
DR   PeptideAtlas; P04216; -.
DR   ProteomicsDB; 51683; -.
DR   Pumba; P04216; -.
DR   ABCD; P04216; 3 sequenced antibodies.
DR   Antibodypedia; 671; 2433 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   AGR; HGNC:11801; -.
DR   CTD; 7070; -.
DR   DisGeNET; 7070; -.
DR   GeneCards; THY1; -.
DR   HGNC; HGNC:11801; THY1.
DR   HPA; ENSG00000154096; Tissue enhanced (brain, smooth muscle).
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; 5304893at2759; -.
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 1152 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 190 other cell types or tissues.
DR   ExpressionAtlas; P04216; baseline and differential.
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: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: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:0034113; P:heterotypic cell-cell adhesion; IDA: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: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: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: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   CDD; cd20948; IgC2_CEACAM5-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; THY-1 MEMBRANE GLYCOPROTEIN; 1.
DR   PANTHER; PTHR19226:SF2; THY-1 MEMBRANE GLYCOPROTEIN; 1.
DR   Pfam; PF00047; ig; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   Genevisible; P04216; HS.
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
//