[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1126/science.2857501; PubMed=2857501 [NCBI, ExPASy, EBI, Israel, Japan] Seki T., Chang H.-C., Moriuchi T., Denome R., Ploegh H., Silver J.; "A hydrophobic transmembrane segment at the carboxyl terminus of thy-1."; Science 227:649-651(1985).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (THY-1.2 ALLOTYPE). STRAIN=BALB/c; PubMed=2866091 [NCBI, ExPASy, EBI, Israel, Japan] Giguere V., Isobe K., Grosveld F.; "Structure of the murine Thy-1 gene."; EMBO J. 4:2017-2024(1985).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (THY-1.2 ALLOTYPE). DOI=10.1073/pnas.82.11.3819; PubMed=2582427 [NCBI, ExPASy, EBI, Israel, Japan] Chang H.-C., Seki T., Moriuchi T., Silver J.; "Isolation and characterization of mouse Thy-1 genomic clones."; Proc. Natl. Acad. Sci. U.S.A. 82:3819-3823(1985).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (THY-1.2 ALLOTYPE). PubMed=2868059 [NCBI, ExPASy, EBI, Israel, Japan] Ingraham H.A., Lawless G.M., Evans G.A.; "The mouse Thy-1.2 glycoprotein gene: complete sequence and identification of an unusual promoter."; J. Immunol. 136:1482-1489(1986).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Olfactory epithelium; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	PROTEIN SEQUENCE OF 20-131, PYROGLUTAMATE FORMATION AT GLN-20, AND GPI-ANCHOR AT CYS-131. DOI=10.1126/science.6177036; PubMed=6177036 [NCBI, ExPASy, EBI, Israel, Japan] Williams A.F., Gagnon J.; "Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin."; Science 216:696-703(1982).

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.
POLYMORPHISM: There are two major alleles; Thy-1.1 (CD90.1) and Thy-1.2 (CD90.2).
SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X03151; CAA26930.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02771; CAA26548.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02772; CAA26549.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02773; CAA26550.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M10246; AAA40440.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11160; AAA40441.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M12379; AAA40443.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC054436; AAH54436.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00109727; -.

A94278; TDMS.

NP_033408.1; -.

3D structure databases

ModBase

P01831.

Organism-specific databases

MGI

MGI:98747; Thy1.

Gene expression databases

P01831; -.

P01831; -.

MM_THY1; -.

ENSMUSG00000032011; Mus musculus.

Ontologies

GO:0031362;	Cellular component: anchored to external side of plasma membrane (inferred from direct assay from MGI).
GO:0030425;	Cellular component: dendrite (inferred from direct assay from MGI).
GO:0030426;	Cellular component: growth cone (inferred from sequence or structural similarity from UniProtKB).
GO:0045121;	Cellular component: membrane raft (inferred from direct assay from MGI).
GO:0034235;	Molecular function: GPI anchor binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005100;	Molecular function: Rho GTPase activator activity (inferred from sequence or structural similarity from UniProtKB).
GO:0001525;	Biological process: angiogenesis (inferred from direct assay from UniProtKB).
GO:0016337;	Biological process: cell-cell adhesion (inferred from sequence or structural similarity from UniProtKB).
GO:0007010;	Biological process: cytoskeleton organization (inferred from sequence or structural similarity from UniProtKB).
GO:0048041;	Biological process: focal adhesion formation (inferred from sequence or structural similarity from UniProtKB).
GO:0050771;	Biological process: negative regulation of axonogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0030336;	Biological process: negative regulation of cell migration (inferred from sequence or structural similarity from UniProtKB).
GO:0006469;	Biological process: negative regulation of protein kinase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0050860;	Biological process: negative regulation of T cell receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0043547;	Biological process: positive regulation of GTPase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0051281;	Biological process: positive regulation of release of sequestered calcium ion into cytosol (inferred from sequence or structural similarity from UniProtKB).
GO:0050870;	Biological process: positive regulation of T cell activation (inferred from sequence or structural similarity from UniProtKB).
GO:0046549;	Biological process: retinal cone cell development (inferred from mutant phenotype from UniProtKB).
GO:0050852;	Biological process: T cell receptor signaling pathway (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR013151; Ig.
IPR007110; Ig-like.
IPR003596; Ig_V-set_sub.
Graphical view of domain structure.

Pfam

PF00047; ig; 1.
Pfam graphical view of domain structure.

SMART

SM00406; IGv; 1.
SMART graphical view of domain structure.

PROSITE

PS50835; IG_LIKE; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P01831; -.

Genome annotation databases

Ensembl

ENSMUSG00000032011; Mus musculus. [Contig view]

GeneID

21838; -.

KEGG

mmu:21838; -.

Phylogenomic databases

HOGENOM

P01831; -.

HOVERGEN

P01831; -.

OMA

P01831; LPIQYEF.

Other

301298; -.

Thy1; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane; Polymorphism; Pyrrolidone carboxylic acid; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`
`CHAIN`	`20 131`	`112`	`Thy-1 membrane glycoprotein.`	`PRO_0000014977`
`PROPEP`	`132 162`	`31`	`Removed in mature form.`	`PRO_0000014978`
`DOMAIN`	`20 127`	`108`	`Ig-like V-type.`
`MOD_RES`	`20 20`		`Pyrrolidone carboxylic acid.`
`LIPID`	`131 131`		`GPI-anchor amidated cysteine.`
`CARBOHYD`	`42 42`		`N-linked (GlcNAc...).`
`CARBOHYD`	`94 94`		`N-linked (GlcNAc...).`
`CARBOHYD`	`118 118`		`N-linked (GlcNAc...).`
`DISULFID`	`28 131`
`DISULFID`	`38 105`
`VARIANT`	`108 108`	`1`	`Q -> R (in allele Thy-1.1).`

Sequence information

Length: 162 AA [This is the length of the unprocessed precursor]

Molecular weight: 18080 Da [This is the MW of the unprocessed precursor]

CRC64: 397BF7D3A9F2C77B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNPAISVALL LSVLQVSRGQ KVTSLTACLV NQNLRLDCRH ENNTKDNSIQ HEFSLTREKR 

        70         80         90        100        110        120 
KHVLSGTLGI PEHTYRSRVT LSNQPYIKVL TLANFTTKDE GDYFCELQVS GANPMSSNKS 

       130        140        150        160 
ISVYRDKLVK CGGISLLVQN TSWMLLLLLS LSLLQALDFI SL

P01831 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools