THY1_MOUSE
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 03-AUG-2022, entry version 183.
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; 10.
DR IntAct; P01831; 6.
DR MINT; P01831; -.
DR STRING; 10090.ENSMUSP00000110489; -.
DR GlyConnect; 2769; 44 N-Linked glycans (3 sites).
DR GlyGen; P01831; 3 sites, 42 N-linked glycans (3 sites).
DR iPTMnet; P01831; -.
DR PhosphoSitePlus; P01831; -.
DR SwissPalm; P01831; -.
DR EPD; P01831; -.
DR jPOST; P01831; -.
DR MaxQB; P01831; -.
DR PaxDb; P01831; -.
DR PeptideAtlas; P01831; -.
DR PRIDE; P01831; -.
DR ProteomicsDB; 262986; -.
DR Antibodypedia; 671; 2107 antibodies from 47 providers.
DR DNASU; 21838; -.
DR Ensembl; ENSMUST00000114840; ENSMUSP00000110489; ENSMUSG00000032011.
DR GeneID; 21838; -.
DR KEGG; mmu:21838; -.
DR UCSC; uc009pbl.1; mouse.
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; 1504363at2759; -.
DR PhylomeDB; P01831; -.
DR TreeFam; TF336059; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 21838; 4 hits in 73 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 223 other tissues.
DR ExpressionAtlas; P01831; baseline and differential.
DR Genevisible; P01831; MM.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:MGI.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:MGI.
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: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:0061099; P:negative regulation of protein tyrosine 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:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:MGI.
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; ISO:MGI.
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; -; 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; 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
