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P01830

- THY1_RAT

UniProt

P01830 - THY1_RAT

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Protein

Thy-1 membrane glycoprotein

Gene

Thy1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. enzyme binding Source: RGD
  2. GPI anchor binding Source: UniProtKB
  3. protein kinase binding Source: RGD
  4. Rho GTPase activator activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. cytoskeleton organization Source: UniProtKB
  3. focal adhesion assembly Source: UniProtKB
  4. mast cell activation Source: UniProtKB
  5. negative regulation of apoptotic process Source: UniProtKB
  6. negative regulation of axonogenesis Source: UniProtKB
  7. negative regulation of cell migration Source: UniProtKB
  8. negative regulation of fibroblast proliferation Source: UniProtKB
  9. negative regulation of protein kinase activity Source: UniProtKB
  10. negative regulation of T cell receptor signaling pathway Source: UniProtKB
  11. positive regulation of GTPase activity Source: UniProtKB
  12. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  13. positive regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
  14. positive regulation of Rho GTPase activity Source: GOC
  15. positive regulation of T cell activation Source: UniProtKB
  16. retinal cone cell development Source: UniProtKB
  17. single organismal cell-cell adhesion Source: UniProtKB
  18. T cell receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Sialic acid

Names & Taxonomyi

Protein namesi
Recommended name:
Thy-1 membrane glycoprotein
Alternative name(s):
Thy-1 antigen
CD_antigen: CD90
Gene namesi
Name:Thy1
Synonyms:Thy-1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 8

Organism-specific databases

RGDi3860. Thy1.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of external side of plasma membrane Source: Ensembl
  2. anchored component of plasma membrane Source: RGD
  3. apical plasma membrane Source: Ensembl
  4. cell surface Source: RGD
  5. cytosol Source: UniProtKB
  6. dendrite Source: Ensembl
  7. endoplasmic reticulum Source: Ensembl
  8. external side of plasma membrane Source: UniProtKB
  9. extracellular vesicular exosome Source: Ensembl
  10. growth cone Source: UniProtKB
  11. membrane raft Source: Ensembl
  12. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 130111Thy-1 membrane glycoproteinPRO_0000014979Add
BLAST
Propeptidei131 – 16131Removed in mature formPRO_0000014980Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Pyrrolidone carboxylic acid1 Publication
Disulfide bondi28 ↔ 1301 PublicationPROSITE-ProRule annotation
Disulfide bondi38 ↔ 1041 PublicationPROSITE-ProRule annotation
Glycosylationi42 – 421N-linked (GlcNAc...) (high mannose or complex)1 Publication
Glycosylationi93 – 931N-linked (GlcNAc...) (complex)1 Publication
Glycosylationi117 – 1171N-linked (GlcNAc...) (high mannose or hybrid); in brain1 Publication
Lipidationi130 – 1301GPI-anchor amidated cysteine

Post-translational modificationi

Glycosylation is tissue specific. Sialylation of N-glycans at Asn-93 in brain and at Asn-42, Asn-93 and Asn-117 in thymus.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP01830.
PRIDEiP01830.

PTM databases

PhosphoSiteiP01830.

Expressioni

Tissue specificityi

Abundant in lymphoid tissues.

Gene expression databases

GenevestigatoriP01830.

Interactioni

Protein-protein interaction databases

BioGridi246951. 1 interaction.
DIPiDIP-1031N.
IntActiP01830. 1 interaction.
MINTiMINT-4996320.
STRINGi10116.ENSRNOP00000008685.

Structurei

3D structure databases

ProteinModelPortaliP01830.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 126107Ig-like V-typeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal

Phylogenomic databases

eggNOGiNOG43439.
GeneTreeiENSGT00390000012352.
HOGENOMiHOG000048719.
HOVERGENiHBG002958.
InParanoidiP01830.
KOiK06514.
OMAiTCELRLS.
OrthoDBiEOG789CCZ.
PhylomeDBiP01830.
TreeFamiTF336059.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01830-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPVISITLL LSVLQMSRGQ RVISLTACLV NQNLRLDCRH ENNTNLPIQH
60 70 80 90 100
EFSLTREKKK HVLSGTLGVP EHTYRSRVNL FSDRFIKVLT LANFTTKDEG
110 120 130 140 150
DYMCELRVSG QNPTSSNKTI NVIRDKLVKC GGISLLVQNT SWLLLLLLSL
160
SFLQATDFIS L
Length:161
Mass (Da):18,172
Last modified:August 13, 1987 - v1
Checksum:i3285748F3C2C5AB2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711E → Q in CAA26931. (PubMed:2864289)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiB45909. TDRT.
RefSeqiNP_036805.1. NM_012673.2.
UniGeneiRn.108198.

Genome annotation databases

EnsembliENSRNOT00000008685; ENSRNOP00000008685; ENSRNOG00000006604.
GeneIDi24832.
KEGGirno:24832.
UCSCiRGD:3860. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi B45909. TDRT.
RefSeqi NP_036805.1. NM_012673.2.
UniGenei Rn.108198.

3D structure databases

ProteinModelPortali P01830.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246951. 1 interaction.
DIPi DIP-1031N.
IntActi P01830. 1 interaction.
MINTi MINT-4996320.
STRINGi 10116.ENSRNOP00000008685.

PTM databases

PhosphoSitei P01830.

Proteomic databases

PaxDbi P01830.
PRIDEi P01830.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000008685 ; ENSRNOP00000008685 ; ENSRNOG00000006604 .
GeneIDi 24832.
KEGGi rno:24832.
UCSCi RGD:3860. rat.

Organism-specific databases

CTDi 7070.
RGDi 3860. Thy1.

Phylogenomic databases

eggNOGi NOG43439.
GeneTreei ENSGT00390000012352.
HOGENOMi HOG000048719.
HOVERGENi HBG002958.
InParanoidi P01830.
KOi K06514.
OMAi TCELRLS.
OrthoDBi EOG789CCZ.
PhylomeDBi P01830.
TreeFami TF336059.

Miscellaneous databases

NextBioi 604560.
PROi P01830.

Gene expression databases

Genevestigatori P01830.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
[Graphical view ]
Pfami PF00047. ig. 1 hit.
[Graphical view ]
SMARTi SM00409. IG. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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, PYROGLUTAMATE FORMATION AT GLN-20, 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.

Entry informationi

Entry nameiTHY1_RAT
AccessioniPrimary (citable) accession number: P01830
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3