THY1_RAT
ID THY1_RAT Reviewed; 161 AA.
AC P01830;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 177.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2864289;
RA Seki T., Chang H.-C., Moriuchi T., Denome R., Silver J.;
RT "Thy-1: a hydrophobic transmembrane segment at the carboxyl terminus.";
RL Fed. Proc. 44:2865-2869(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-122.
RX PubMed=6130472; DOI=10.1038/301080a0;
RA Moriuchi T., Chang H.-C., Denome R., Silver J.;
RT "Thy-1 cDNA sequence suggests a novel regulatory mechanism.";
RL Nature 301:80-82(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-161.
RX PubMed=2857477; DOI=10.1038/313485a0;
RA Seki T., Moriuchi T., Chang H.-C., Denome R., Silver J.;
RT "Structural organization of the rat thy-1 gene.";
RL Nature 313:485-487(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 20-161.
RX PubMed=6149956; DOI=10.1016/0014-5793(84)81250-8;
RA Moriuchi T., Silver J.;
RT "Rat Thy-1 antigen has a hydrophobic segment at the carboxyl terminus.";
RL FEBS Lett. 178:105-108(1984).
RN [5]
RP PROTEIN SEQUENCE OF 20-130, PYROGLUTAMATE FORMATION AT GLN-20,
RP GLYCOSYLATION AT ASN-42; ASN-93 AND ASN-117, AND DISULFIDE BONDS.
RX PubMed=6118137; DOI=10.1042/bj1950015;
RA Campbell D.G., Gagnon J., Reid K.B.M., Williams A.F.;
RT "Rat brain Thy-1 glycoprotein. The amino acid sequence, disulphide bonds
RT and an unusual hydrophobic region.";
RL Biochem. J. 195:15-30(1981).
RN [6]
RP PROTEIN SEQUENCE OF 78-84 AND 119-124, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=2886334; DOI=10.1002/j.1460-2075.1987.tb02359.x;
RA Parekh R.B., Tse A.G.D., Dwek R.A., Williams A.F., Rademacher T.W.;
RT "Tissue-specific N-glycosylation, site-specific oligosaccharide patterns
RT and lentil lectin recognition of rat Thy-1.";
RL EMBO J. 6:1233-1244(1987).
RN [8]
RP STRUCTURE OF THE GPI-ANCHOR AT CYS-130.
RX PubMed=2897081; DOI=10.1038/333269a0;
RA Homans S.W., Ferguson M.A., Dwek R.A., Rademacher T.W., Anand R.,
RA Williams A.F.;
RT "Complete structure of the glycosyl phosphatidylinositol membrane anchor of
RT rat brain Thy-1 glycoprotein.";
RL Nature 333:269-272(1988).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-42 AND ASN-93, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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 -!- TISSUE SPECIFICITY: Abundant in lymphoid tissues.
CC -!- PTM: Glycosylation is tissue specific. Sialylation of N-glycans at Asn-
CC 93 in brain and at Asn-42, Asn-93 and Asn-117 in thymus.
CC {ECO:0000269|PubMed:6118137}.
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DR EMBL; X03152; CAA26931.1; -; Genomic_DNA.
DR EMBL; X03150; CAA26929.1; -; mRNA.
DR EMBL; X02002; CAA26033.1; -; Genomic_DNA.
DR EMBL; M18002; AAA42243.1; -; mRNA.
DR EMBL; M10666; AAA42242.1; -; mRNA.
DR PIR; B45909; TDRT.
DR RefSeq; NP_036805.1; NM_012673.2.
DR AlphaFoldDB; P01830; -.
DR SMR; P01830; -.
DR BioGRID; 246951; 4.
DR DIP; DIP-1031N; -.
DR IntAct; P01830; 3.
DR MINT; P01830; -.
DR STRING; 10116.ENSRNOP00000008685; -.
DR GlyGen; P01830; 3 sites, 25 N-linked glycans (3 sites).
DR iPTMnet; P01830; -.
DR PhosphoSitePlus; P01830; -.
DR SwissPalm; P01830; -.
DR jPOST; P01830; -.
DR PaxDb; P01830; -.
DR PRIDE; P01830; -.
DR GeneID; 24832; -.
DR KEGG; rno:24832; -.
DR UCSC; RGD:3860; rat.
DR CTD; 7070; -.
DR RGD; 3860; Thy1.
DR VEuPathDB; HostDB:ENSRNOG00000006604; -.
DR eggNOG; ENOG502S18P; Eukaryota.
DR HOGENOM; CLU_136861_0_0_1; -.
DR InParanoid; P01830; -.
DR OMA; MNPAIGI; -.
DR OrthoDB; 1504363at2759; -.
DR PhylomeDB; P01830; -.
DR TreeFam; TF336059; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:P01830; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000006604; Expressed in thymus and 19 other tissues.
DR Genevisible; P01830; RN.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISO:RGD.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:RGD.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0030673; C:axolemma; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0032590; C:dendrite membrane; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:CAFA.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0034235; F:GPI anchor binding; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; IDA:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0045576; P:mast cell activation; NAS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0050771; P:negative regulation of axonogenesis; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; NAS: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; IDA:UniProtKB.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IDA: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; ISO:RGD.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; NAS:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:CACAO.
DR GO; GO:0043113; P:receptor clustering; IDA:UniProtKB.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; ISO:RGD.
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; IMP: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; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Sialic acid; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:6118137"
FT CHAIN 20..130
FT /note="Thy-1 membrane glycoprotein"
FT /id="PRO_0000014979"
FT PROPEP 131..161
FT /note="Removed in mature form"
FT /id="PRO_0000014980"
FT DOMAIN 20..126
FT /note="Ig-like V-type"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:6118137"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 130
FT /note="GPI-anchor amidated cysteine"
FT /evidence="ECO:0000269|PubMed:2897081"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:6118137"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:6118137"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine; alternate"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:6118137"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine; alternate"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) (high mannose) asparagine; in
FT brain; alternate"
FT /evidence="ECO:0000269|PubMed:6118137"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; in brain;
FT alternate"
FT /evidence="ECO:0000269|PubMed:6118137"
FT DISULFID 28..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6118137"
FT DISULFID 38..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6118137"
FT CONFLICT 71
FT /note="E -> Q (in Ref. 1; CAA26931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 18172 MW; 3285748F3C2C5AB2 CRC64;
MNPVISITLL LSVLQMSRGQ RVISLTACLV NQNLRLDCRH ENNTNLPIQH EFSLTREKKK
HVLSGTLGVP EHTYRSRVNL FSDRFIKVLT LANFTTKDEG DYMCELRVSG QNPTSSNKTI
NVIRDKLVKC GGISLLVQNT SWLLLLLLSL SFLQATDFIS L
