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 27-MAR-2024, entry version 185. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 4. DR MINT; P01830; -. DR STRING; 10116.ENSRNOP00000008685; -. DR GlyCosmos; P01830; 3 sites, 25 glycans. DR GlyGen; P01830; 3 sites, 29 N-linked glycans (3 sites). DR iPTMnet; P01830; -. DR PhosphoSitePlus; P01830; -. DR SwissPalm; P01830; -. DR jPOST; P01830; -. DR PaxDb; 10116-ENSRNOP00000008685; -. DR Ensembl; ENSRNOT00055034179; ENSRNOP00055027724; ENSRNOG00055020020. DR Ensembl; ENSRNOT00060033186; ENSRNOP00060027161; ENSRNOG00060019171. DR Ensembl; ENSRNOT00065039071; ENSRNOP00065031726; ENSRNOG00065022864. DR GeneID; 24832; -. DR KEGG; rno:24832; -. DR UCSC; RGD:3860; rat. DR AGR; RGD:3860; -. 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 OrthoDB; 5304893at2759; -. 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 cell types or tissues. 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: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:0034113; P:heterotypic cell-cell adhesion; ISO:RGD. 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: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: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:0048678; P:response to axon injury; IEP:RGD. 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; 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; P01830; RN. 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 //