P01830 (THY1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thy-1 membrane glycoprotein

Alternative name(s):
Thy-1 antigen
CD_antigen=CD90

Gene names

Name:	Thy1
Synonyms:	Thy-1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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-anchor › GPI-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 component	Cell membrane Membrane
Domain	Immunoglobulin domain Signal
Ligand	Sialic acid
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein Pyrrolidone carboxylic acid
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	T cell receptor signaling pathway Inferred from mutant phenotype. Source: UniProtKB angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB cell-cell adhesion Inferred from mutant phenotype. Source: UniProtKB cytoskeleton organization Inferred from direct assay. Source: UniProtKB focal adhesion assembly Inferred from direct assay. Source: UniProtKB mast cell activation Non-traceable author statement. 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. Source: UniProtKB negative regulation of axonogenesis Inferred from direct assay. Source: UniProtKB negative regulation of cell migration Inferred from direct assay. Source: UniProtKB negative regulation of fibroblast proliferation Non-traceable author statement. Source: UniProtKB negative regulation of protein kinase activity Inferred from direct assay. Source: UniProtKB positive regulation of T cell activation Inferred from direct assay. Source: UniProtKB positive regulation of peptidyl-tyrosine phosphorylation Non-traceable author statement. Source: UniProtKB positive regulation of release of sequestered calcium ion into cytosol Inferred from direct assay. Source: UniProtKB retinal cone cell development Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB growth cone Inferred from direct assay. Source: UniProtKB
Molecular function	GPI anchor binding Inferred from direct assay. Source: UniProtKB Rho GTPase activator activity Inferred from direct assay. Source: UniProtKB protein kinase binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Ref.5
	Chain	20 – 130	111	Thy-1 membrane glycoprotein		PRO_0000014979
	Propeptide	131 – 161	31	Removed in mature form		PRO_0000014980
Regions
	Domain	20 – 126	107	Ig-like V-type
Amino acid modifications
	Modified residue	20	1	Pyrrolidone carboxylic acid
	Lipidation	130	1	GPI-anchor amidated cysteine Ref.8
	Glycosylation	42	1	N-linked (GlcNAc...) (high mannose or complex); in thymus Ref.5
	Glycosylation	42	1	N-linked (GlcNAc...) (high mannose); in brain Ref.5
	Glycosylation	93	1	N-linked (GlcNAc...) (complex) Ref.5
	Glycosylation	117	1	N-linked (GlcNAc...) (complex); in thymus Ref.5
	Glycosylation	117	1	N-linked (GlcNAc...) (high mannose or hybrid); in brain Ref.5
	Disulfide bond	28 ↔ 130		Ref.5
	Disulfide bond	38 ↔ 104		Ref.5
Experimental info
	Sequence conflict	71	1	E → Q in CAA26931. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P01830 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 3285748F3C2C5AB2	FASTA	161	18,172
	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

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: 2864289] [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: 6130472] [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: 2857477] [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: 6149956] [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: 6118137] [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, 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: 2886334] [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: 2897081] [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.
IPI	IPI00188956.
PIR	TDRT. B45909.
RefSeq	NP_036805.1. NM_012673.2.
UniGene	Rn.108198.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1031N.
STRING	P01830.
PTM databases
PhosphoSite	P01830.
Proteomic databases
PRIDE	P01830.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000008685; ENSRNOP00000008685; ENSRNOG00000006604.
GeneID	24832.
KEGG	rno:24832.
UCSC	NM_012673. rat.
Organism-specific databases
CTD	7070.
RGD	3860. Thy1.
Phylogenomic databases
eggNOG	roNOG17327.
GeneTree	ENSGT00390000012352.
HOVERGEN	HBG002958.
InParanoid	P01830.
OMA	TCELRLS.
OrthoDB	EOG4SF977.
PhylomeDB	P01830.
Gene expression databases
ArrayExpress	P01830.
Genevestigator	P01830.
GermOnline	ENSRNOG00000006604. Rattus norvegicus.
Family and domain databases
InterPro	IPR007110. Ig-like. IPR013783. Ig-like_fold. IPR003599. Ig_sub. IPR013151. Immunoglobulin. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
KO	K06514.
Pfam	PF00047. ig. 1 hit. [Graphical view]
SMART	SM00409. IG. 1 hit. [Graphical view]
PROSITE	PS50835. IG_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	604560.

Entry information

Entry name

THY1_RAT

Accession

Primary (citable) accession number: P01830

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 13, 1987
Last modified:	November 16, 2011
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program