[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1073/pnas.82.19.6657; PubMed=2864690 [NCBI, ExPASy, EBI, Israel, Japan] Seki T., Spurr N., Obata F., Goyert S., Goodfellow P., Silver J.; "The human Thy-1 gene: structure and chromosomal location."; Proc. Natl. Acad. Sci. U.S.A. 82:6657-6661(1985).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; DOI=10.1006/bbrc.2000.3282; PubMed=10944468 [NCBI, ExPASy, EBI, Israel, Japan] Ye Z., Connor J.R.; "cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs."; Biochem. Biophys. Res. Commun. 275:223-227(2000).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Amygdala; DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan] Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.; "The full-ORF clone resource of the German cDNA consortium."; BMC Genomics 8:399-399(2007).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Eye; 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).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-55. DOI=10.1084/jem.177.5.1331; PubMed=7683034 [NCBI, ExPASy, EBI, Israel, Japan] Craig W., Kay R., Cutler R.L., Lansdorp P.M.; "Expression of Thy-1 on human hematopoietic progenitor cells."; J. Exp. Med. 177:1331-1342(1993).
[6]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan] Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."; J. Proteome Res. 8:651-661(2009).

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 (By similarity).
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

M11749; AAA61180.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF261093; AAG13904.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161958; CAB82306.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065559; AAH65559.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S59749; AAB26353.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00022892; -.

PIR

A02106; TDHU.
T47130; T47130.

RefSeq

NP_006279.2; -.

UniGene

Hs.644697

3D structure databases

ModBase

P04216.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway; amb2 Integrin signaling.
il4_2pathway; IL4-mediated signaling events.

Organism-specific databases

GC11M118795; -.

HIX0010195; -.

HGNC:11801; THY1.

HPA003733; -.

188230; gene. [NCBI / EBI]

PharmGKB

PA36510; -.

Gene expression databases

P04216; -.

P04216; -.

HS_THY1; -.

ENSG00000154096; Homo sapiens.

Ontologies

GO:0005783;	Cellular component: endoplasmic reticulum (inferred from direct assay from LIFEdb).
GO:0030426;	Cellular component: growth cone (inferred from sequence or structural similarity from UniProtKB).
GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0045121;	Cellular component: membrane raft (non-traceable author statement from UniProtKB).
GO:0034235;	Molecular function: GPI anchor binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005178;	Molecular function: integrin binding (inferred from physical interaction 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 sequence or structural similarity 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 sequence or structural similarity 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 sequence or structural similarity 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.
IPR003599; Ig_sub.
Graphical view of domain structure.

Pfam

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

SMART

SM00409; IG; 1.
SMART graphical view of domain structure.

PROSITE

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

Proteomic databases

PRIDE

P04216; -.

Genome annotation databases

Ensembl

ENSG00000154096; Homo sapiens. [Contig view]

GeneID

7070; -.

KEGG

hsa:7070; -.

Phylogenomic databases

HOGENOM

P04216; -.

HOVERGEN

P04216; -.

OMA

P04216; LPIQYEF.

Other

27645; -.

THY1; Homo sapiens.

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`
`CHAIN`	`20 130`	`111`	`Thy-1 membrane glycoprotein.`	`PRO_0000014973`
`PROPEP`	`131 161`	`31`	`Removed in mature form (By similarity).`	`PRO_0000014974`
`DOMAIN`	`20 126`	`107`	`Ig-like V-type.`
`MOD_RES`	`20 20`		`Pyrrolidone carboxylic acid (By similarity).`
`LIPID`	`130 130`		`GPI-anchor amidated cysteine (By similarity).`
`CARBOHYD`	`42 42`		`N-linked (GlcNAc...).`
`CARBOHYD`	`79 79`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`119 119`		`N-linked (GlcNAc...).`
`CARBOHYD`	`139 139`		`N-linked (GlcNAc...).`
`DISULFID`	`28 130`		`By similarity.`
`DISULFID`	`38 104`		`By similarity.`
`CONFLICT`	`54 55`		`LT -> AP (in Ref. 5).`
`CONFLICT`	`85 85`		`N -> H (in Ref. 1; AAA61180).`

Sequence information

Length: 161 AA [This is the length of the unprocessed precursor]

Molecular weight: 17935 Da [This is the MW of the unprocessed precursor]

CRC64: 2B6796DA8EE7454B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNLAISIALL LTVLQVSRGQ KVTSLTACLV DQSLRLDCRH ENTSSSPIQY EFSLTRETKK 

        70         80         90        100        110        120 
HVLFGTVGVP EHTYRSRTNF TSKYNMKVLY LSAFTSKDEG TYTCALHHSG HSPPISSQNV 

       130        140        150        160 
TVLRDKLVKC EGISLLAQNT SWLLLLLLSL SLLQATDFMS L

P04216 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