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P01830 (THY1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thy-1 membrane glycoprotein
Alternative name(s):
Thy-1 antigen
CD_antigen=CD90
Gene names
Name:Thy1
Synonyms:Thy-1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Ref.8.

Tissue specificity

Abundant in lymphoid tissues.

Post-translational modification

Glycosylation is tissue specific. Sialylation of N-glycans at Asn-93 in brain and at Asn-42, Asn-93 and Asn-117 in thymus.

Sequence similarities

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainImmunoglobulin domain
Signal
   LigandSialic acid
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell receptor signaling pathway

Inferred from mutant phenotype PubMed 9285719. Source: UniProtKB

angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell adhesion

Inferred from mutant phenotype PubMed 9285719. Source: UniProtKB

cytoskeleton organization

Inferred from direct assay PubMed 15093746. Source: UniProtKB

focal adhesion assembly

Inferred from direct assay PubMed 15093746. Source: UniProtKB

mast cell activation

Non-traceable author statement PubMed 8666426. Source: UniProtKB

negative regulation of T cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Traceable author statement PubMed 9168818. Source: UniProtKB

negative regulation of axonogenesis

Inferred from direct assay PubMed 15547945. Source: UniProtKB

negative regulation of cell migration

Inferred from direct assay PubMed 15093746. Source: UniProtKB

negative regulation of fibroblast proliferation

Non-traceable author statement PubMed 10409250. Source: UniProtKB

negative regulation of protein kinase activity

Inferred from direct assay PubMed 15093746. Source: UniProtKB

positive regulation of GTPase activity

Inferred from direct assay PubMed 15093746. Source: UniProtKB

positive regulation of Rho GTPase activity

Inferred from direct assay PubMed 15093746. Source: GOC

positive regulation of T cell activation

Inferred from direct assay PubMed 7722293. Source: UniProtKB

positive regulation of peptidyl-tyrosine phosphorylation

Non-traceable author statement PubMed 12415741. Source: UniProtKB

positive regulation of release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 2873512. Source: UniProtKB

retinal cone cell development

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentanchored component of external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

anchored component of plasma membrane

Inferred from direct assay PubMed 10814697. Source: RGD

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 10814697. Source: RGD

cytosol

Inferred from direct assay PubMed 15547945. Source: UniProtKB

dendrite

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

growth cone

Inferred from direct assay PubMed 10601014. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 15547945. Source: UniProtKB

   Molecular_functionGPI anchor binding

Inferred from direct assay PubMed 16257296. Source: UniProtKB

Rho GTPase activator activity

Inferred from direct assay PubMed 15093746. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 8666426. Source: RGD

protein kinase binding

Inferred from physical interaction PubMed 8870703. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.5
Chain20 – 130111Thy-1 membrane glycoprotein
PRO_0000014979
Propeptide131 – 16131Removed in mature form
PRO_0000014980

Regions

Domain20 – 126107Ig-like V-type

Amino acid modifications

Modified residue201Pyrrolidone carboxylic acid
Lipidation1301GPI-anchor amidated cysteine Ref.8
Glycosylation421N-linked (GlcNAc...) (high mannose or complex); in thymus Ref.5
Glycosylation421N-linked (GlcNAc...) (high mannose); in brain Ref.5
Glycosylation931N-linked (GlcNAc...) (complex) Ref.5
Glycosylation1171N-linked (GlcNAc...) (complex); in thymus Ref.5
Glycosylation1171N-linked (GlcNAc...) (high mannose or hybrid); in brain Ref.5
Disulfide bond28 ↔ 130 Ref.5
Disulfide bond38 ↔ 104 Ref.5

Experimental info

Sequence conflict711E → Q in CAA26931. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P01830 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 3285748F3C2C5AB2

FASTA16118,172
        10         20         30         40         50         60 
MNPVISITLL LSVLQMSRGQ RVISLTACLV NQNLRLDCRH ENNTNLPIQH EFSLTREKKK 

        70         80         90        100        110        120 
HVLSGTLGVP EHTYRSRVNL FSDRFIKVLT LANFTTKDEG DYMCELRVSG QNPTSSNKTI 

       130        140        150        160 
NVIRDKLVKC GGISLLVQNT SWLLLLLLSL SFLQATDFIS L 

« Hide

References

[1]"Thy-1: a hydrophobic transmembrane segment at the carboxyl terminus."
Seki T., Chang H.-C., Moriuchi T., Denome R., Silver J.
Fed. Proc. 44:2865-2869(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Thy-1 cDNA sequence suggests a novel regulatory mechanism."
Moriuchi T., Chang H.-C., Denome R., Silver J.
Nature 301:80-82(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-122.
[3]"Structural organization of the rat thy-1 gene."
Seki T., Moriuchi T., Chang H.-C., Denome R., Silver J.
Nature 313:485-487(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-161.
[4]"Rat Thy-1 antigen has a hydrophobic segment at the carboxyl terminus."
Moriuchi T., Silver J.
FEBS Lett. 178:105-108(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 20-161.
[5]"Rat brain Thy-1 glycoprotein. The amino acid sequence, disulphide bonds and an unusual hydrophobic region."
Campbell D.G., Gagnon J., Reid K.B.M., Williams A.F.
Biochem. J. 195:15-30(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-130, GLYCOSYLATION AT ASN-42; ASN-93 AND ASN-117, DISULFIDE BONDS.
[6]Lubec G., Chen W.-Q., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 78-84 AND 119-124, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Hippocampus.
[7]"Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1."
Parekh R.B., Tse A.G.D., Dwek R.A., Williams A.F., Rademacher T.W.
EMBO J. 6:1233-1244(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
[8]"Complete structure of the glycosyl phosphatidylinositol membrane anchor of rat brain Thy-1 glycoprotein."
Homans S.W., Ferguson M.A., Dwek R.A., Rademacher T.W., Anand R., Williams A.F.
Nature 333:269-272(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF THE GPI-ANCHOR AT CYS-130.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03152 Genomic DNA. Translation: CAA26931.1.
X03150 mRNA. Translation: CAA26929.1.
X02002 Genomic DNA. Translation: CAA26033.1.
M18002 mRNA. Translation: AAA42243.1.
M10666 mRNA. Translation: AAA42242.1.
PIRTDRT. B45909.
RefSeqNP_036805.1. NM_012673.2.
UniGeneRn.108198.

3D structure databases

ProteinModelPortalP01830.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-1031N.
IntActP01830. 1 interaction.
MINTMINT-4996320.
STRING10116.ENSRNOP00000008685.

PTM databases

PhosphoSiteP01830.

Proteomic databases

PaxDbP01830.
PRIDEP01830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000008685; ENSRNOP00000008685; ENSRNOG00000006604.
GeneID24832.
KEGGrno:24832.
UCSCRGD:3860. rat.

Organism-specific databases

CTD7070.
RGD3860. Thy1.

Phylogenomic databases

eggNOGNOG43439.
GeneTreeENSGT00390000012352.
HOGENOMHOG000048719.
HOVERGENHBG002958.
InParanoidP01830.
KOK06514.
OMATCELRLS.
OrthoDBEOG789CCZ.
PhylomeDBP01830.
TreeFamTF336059.

Gene expression databases

GenevestigatorP01830.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
[Graphical view]
PfamPF00047. ig. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604560.
PROP01830.

Entry information

Entry nameTHY1_RAT
AccessionPrimary (citable) accession number: P01830
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families