ID   THY1_MOUSE              Reviewed;         162 AA.
AC   P01831;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Thy-1 membrane glycoprotein;
DE   AltName: Full=Thy-1 antigen;
DE   AltName: CD_antigen=CD90;
DE   Flags: Precursor;
GN   Name=Thy1; Synonyms=Thy-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POLYMORPHISM.
RX   PubMed=2857501; DOI=10.1126/science.2857501;
RA   Seki T., Chang H.-C., Moriuchi T., Denome R., Ploegh H., Silver J.;
RT   "A hydrophobic transmembrane segment at the carboxyl terminus of thy-1.";
RL   Science 227:649-651(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (THY-1.2 ALLOTYPE), AND POLYMORPHISM.
RC   STRAIN=BALB/cJ;
RX   PubMed=2866091; DOI=10.1002/j.1460-2075.1985.tb03886.x;
RA   Giguere V., Isobe K., Grosveld F.;
RT   "Structure of the murine Thy-1 gene.";
RL   EMBO J. 4:2017-2024(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (THY-1.2 ALLOTYPE), AND POLYMORPHISM.
RX   PubMed=2582427; DOI=10.1073/pnas.82.11.3819;
RA   Chang H.-C., Seki T., Moriuchi T., Silver J.;
RT   "Isolation and characterization of mouse Thy-1 genomic clones.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:3819-3823(1985).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (THY-1.2 ALLOTYPE), AND POLYMORPHISM.
RX   PubMed=2868059;
RA   Ingraham H.A., Lawless G.M., Evans G.A.;
RT   "The mouse Thy-1.2 glycoprotein gene: complete sequence and identification
RT   of an unusual promoter.";
RL   J. Immunol. 136:1482-1489(1986).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
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   PROTEIN SEQUENCE OF 20-131, PYROGLUTAMATE FORMATION AT GLN-20, AND
RP   GPI-ANCHOR AT CYS-131.
RX   PubMed=6177036; DOI=10.1126/science.6177036;
RA   Williams A.F., Gagnon J.;
RT   "Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin.";
RL   Science 216:696-703(1982).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Lung, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May play a role in cell-cell or cell-ligand interactions
CC       during synaptogenesis and other events in the brain.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- POLYMORPHISM: There are two major alleles; Thy-1.1 (CD90.1) and Thy-1.2
CC       (CD90.2). {ECO:0000305|PubMed:2582427, ECO:0000305|PubMed:2857501,
CC       ECO:0000305|PubMed:2866091, ECO:0000305|PubMed:2868059}.
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DR   EMBL; X03151; CAA26930.1; -; Genomic_DNA.
DR   EMBL; X02771; CAA26548.1; -; Genomic_DNA.
DR   EMBL; X02772; CAA26549.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X02773; CAA26550.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M10246; AAA40440.1; -; Genomic_DNA.
DR   EMBL; M11160; AAA40441.1; -; Genomic_DNA.
DR   EMBL; M12379; AAA40443.1; -; Genomic_DNA.
DR   EMBL; BC054436; AAH54436.1; -; mRNA.
DR   CCDS; CCDS23093.1; -.
DR   PIR; A94278; TDMS.
DR   RefSeq; NP_033408.1; NM_009382.3.
DR   AlphaFoldDB; P01831; -.
DR   SMR; P01831; -.
DR   BioGRID; 204188; 11.
DR   IntAct; P01831; 6.
DR   MINT; P01831; -.
DR   STRING; 10090.ENSMUSP00000110489; -.
DR   GlyConnect; 2769; 44 N-Linked glycans (3 sites).
DR   GlyCosmos; P01831; 3 sites, 42 glycans.
DR   GlyGen; P01831; 4 sites, 42 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P01831; -.
DR   PhosphoSitePlus; P01831; -.
DR   SwissPalm; P01831; -.
DR   EPD; P01831; -.
DR   jPOST; P01831; -.
DR   MaxQB; P01831; -.
DR   PaxDb; 10090-ENSMUSP00000110489; -.
DR   PeptideAtlas; P01831; -.
DR   ProteomicsDB; 262986; -.
DR   Pumba; P01831; -.
DR   Antibodypedia; 671; 2433 antibodies from 47 providers.
DR   DNASU; 21838; -.
DR   Ensembl; ENSMUST00000114840.2; ENSMUSP00000110489.2; ENSMUSG00000032011.6.
DR   GeneID; 21838; -.
DR   KEGG; mmu:21838; -.
DR   UCSC; uc009pbl.1; mouse.
DR   AGR; MGI:98747; -.
DR   CTD; 7070; -.
DR   MGI; MGI:98747; Thy1.
DR   VEuPathDB; HostDB:ENSMUSG00000032011; -.
DR   eggNOG; ENOG502S18P; Eukaryota.
DR   GeneTree; ENSGT00390000012352; -.
DR   HOGENOM; CLU_136861_0_0_1; -.
DR   InParanoid; P01831; -.
DR   OMA; MNPAIGI; -.
DR   OrthoDB; 5304893at2759; -.
DR   PhylomeDB; P01831; -.
DR   TreeFam; TF336059; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   BioGRID-ORCS; 21838; 5 hits in 78 CRISPR screens.
DR   ChiTaRS; Thy1; mouse.
DR   PRO; PR:P01831; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P01831; Protein.
DR   Bgee; ENSMUSG00000032011; Expressed in thymus and 226 other cell types or tissues.
DR   ExpressionAtlas; P01831; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0030673; C:axolemma; ISS:UniProtKB.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0032590; C:dendrite membrane; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; IDA: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; ISO:MGI.
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; IMP: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; IDA:UniProtKB.
DR   GO; GO:0002693; P:positive regulation of cellular extravasation; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:2000298; P:regulation of Rho-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0046549; P:retinal cone cell development; IMP:UniProtKB.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
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; P01831; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW   Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:6177036"
FT   CHAIN           20..131
FT                   /note="Thy-1 membrane glycoprotein"
FT                   /id="PRO_0000014977"
FT   PROPEP          132..162
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000014978"
FT   DOMAIN          20..127
FT                   /note="Ig-like V-type"
FT   MOD_RES         20
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:6177036"
FT   LIPID           131
FT                   /note="GPI-anchor amidated cysteine; alternate"
FT                   /evidence="ECO:0000269|PubMed:6177036"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:6177036"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:6177036"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:6177036"
FT   DISULFID        28..131
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:6177036"
FT   DISULFID        38..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:6177036"
FT   VARIANT         108
FT                   /note="Q -> R (in allele Thy-1.1)"
SQ   SEQUENCE   162 AA;  18080 MW;  397BF7D3A9F2C77B CRC64;
     MNPAISVALL LSVLQVSRGQ KVTSLTACLV NQNLRLDCRH ENNTKDNSIQ HEFSLTREKR
     KHVLSGTLGI PEHTYRSRVT LSNQPYIKVL TLANFTTKDE GDYFCELQVS GANPMSSNKS
     ISVYRDKLVK CGGISLLVQN TSWMLLLLLS LSLLQALDFI SL
//