NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SIM31;
DOI=10.1046/j.1365-294X.2003.01741.x; PubMed=12694293 [NCBI, ExPASy, EBI, Israel, Japan]
Riley R.M., Jin W., Gibson G.;
"Contrasting selection pressures on components of the Ras-mediated signal transduction pathway in Drosophila.";
Mol. Ecol. 12:1315-1323(2003).

Comments

FUNCTION: Required in all receptor tyrosine kinase signaling pathways. Functions downstream of the receptor tyrosine kinase torso, acting in concert with D-Raf via tailless. Also functions downstream of Egfr (epidermal growth factor receptor) and btl (fibroblast growth factor receptor). The SH2 domain suggests that csw effects its role by mediating heteromeric protein interactions. Maternally required for normal determination of cell fates at the termini of the embryo. Required for cell fate specification of the ventral ectoderm, in the developing embryonic CNS and for embryonic tracheal cell migration. Functions during imaginal development for proper formation of adult structures such as eyes, aristae, L5 wing vein and the tarsal claw (By similarity).
CATALYTIC ACTIVITY: Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.
SIMILARITY: Contains 1 tyrosine-protein phosphatase 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

AY135142; AAN17645.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q06124; 2SHP. [HSSP ENTRY / PDB]

ModBase

Q8ISC9.

Organism-specific databases

FlyBase

FBgn0063985; Dsim\csw.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0004725;	Molecular function: protein tyrosine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0006470;	Biological process: protein amino acid dephosphorylation (inferred from electronic annotation from InterPro).
GO:0007362;	Biological process: terminal region determination (inferred from sequence or structural similarity from UniProtKB).
GO:0008293;	Biological process: torso signaling pathway (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000387; Tyr_Pase.
IPR016130; Tyr_Pase_AS.
IPR000242; Tyr_Pase_rcpt/non-rcpt.
Graphical view of domain structure.

Pfam

PF00102; Y_phosphatase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00700; PRTYPHPHTASE.

SMART

SM00194; PTPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00383; TYR_PHOSPHATASE_1; 1.
PS50056; TYR_PHOSPHATASE_2; 1.
PS50055; TYR_PHOSPHATASE_PTP; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

Q8ISC9.

UniRef

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

Keywords

Cytoplasm; Developmental protein; Hydrolase; Protein phosphatase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 555`	`>555`	`Tyrosine-protein phosphatase corkscrew.`	`PRO_0000094851`
`DOMAIN`	`85 355`	`271`	`Tyrosine-protein phosphatase.`
`REGION`	`11 103`	`93`	`PTPase insert (Cys/Ser-rich).`
`COMPBIAS`	`447 481`	`35`	`Asn-rich.`
`COMPBIAS`	`507 510`	`4`	`Poly-Gln.`
`ACT_SITE`	`293 293`		`Phosphocysteine intermediate (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 555 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 59841 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 801534C03AE9DCFD [This is a checksum on the sequence]

        10         20         30         40         50         60 
LPTDGDLYNM SSSSESLNSS VPSCPACTAA QTQRNCSNCQ LMNKTCVQCA VKSAILPYSN 

        70         80         90        100        110        120 
CATCSRKSDS LSKHKRSESS ASSSPSSGSG SGPGSSGTSG VSSVNGPGTP TNLTSGTAGC 

       130        140        150        160        170        180 
LAGLLKRHSN DSSGAVSISM AERERERERE MFKTYIATQG CLLTQQVNTV TDFWNMVWQE 

       190        200        210        220        230        240 
NTRVIVMTTK EYERGKEKCA RYWPDEGRSE QFGHARIQCV SENSTSDYTL REFLVSWRDQ 

       250        260        270        280        290        300 
PARRIFHYHF QVWPDHGVPA DPGCVLNFLQ DVNTRQSHLA QAGEKPGPIC VHCSAGIGRT 

       310        320        330        340        350        360 
GTFIVIDMIL DQIVRNGLDT EIDIQRTIQM VRSQRSGLVQ TEAQYKFVYY AVQHYIQTLI 

       370        380        390        400        410        420 
ARKRAEEQSL QVGREYTNIK YTGEIGNDSQ RSPLPPAISS ISLVPSKTPL TPTSADLGTG 

       430        440        450        460        470        480 
MGLSMGVGMG VGNKHASKQQ PPLPVVNCNN NNNGIGNSSC SNGGGSSNTS SSNGSSNGNI 

       490        500        510        520        530        540 
NALLGGIGLG LGGNMRKSNF YSDSLKQQQQ REEQAPAGAG KMQQPAPPLR PRPGILKLLT 

       550 
SPVIFQQNSK TFPKT

Q8ISC9 in FASTA format

View entry in original UniProtKB/Swiss-Prot 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