CSW_DROVI
ID CSW_DROVI Reviewed; 764 AA.
AC Q24708;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Tyrosine-protein phosphatase corkscrew;
DE EC=3.1.3.48;
DE Flags: Fragment;
GN Name=csw;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Melnick M.B., Melnick C.B., Larsen I., Perrimon N., Perkins L.A.;
RT "The role of the Drosophila corkscrew protein as a transducer downstream of
RT receptor tyrosine kinases is functionally conserved.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required in all receptor tyrosine kinase signaling pathways.
CC Functions downstream of the receptor tyrosine kinase torso, acting in
CC concert with D-Raf via tailless. Also functions downstream of Egfr
CC (epidermal growth factor receptor) and btl (fibroblast growth factor
CC receptor). The SH2 domain suggests that csw effects its role by
CC mediating heteromeric protein interactions. Maternally required for
CC normal determination of cell fates at the termini of the embryo.
CC Required for cell fate specification of the ventral ectoderm, in the
CC developing embryonic CNS and for embryonic tracheal cell migration.
CC Functions during imaginal development for proper formation of adult
CC structures such as eyes, aristae, L5 wing vein and the tarsal claw (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U22356; AAB02545.1; -; Genomic_DNA.
DR AlphaFoldDB; Q24708; -.
DR SMR; Q24708; -.
DR STRING; 7244.FBpp0231355; -.
DR PRIDE; Q24708; -.
DR eggNOG; KOG0790; Eukaryota.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0040011; P:locomotion; IEA:UniProt.
DR GO; GO:0048666; P:neuron development; IEA:UniProt.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR GO; GO:0007362; P:terminal region determination; ISS:UniProtKB.
DR GO; GO:0008293; P:torso signaling pathway; ISS:UniProtKB.
DR Gene3D; 3.30.505.10; -; 1.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Developmental protein; Hydrolase; Protein phosphatase;
KW SH2 domain.
FT CHAIN <1..764
FT /note="Tyrosine-protein phosphatase corkscrew"
FT /id="PRO_0000094852"
FT DOMAIN 1..95
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 117..522
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 174..325
FT /note="PTPase insert (Cys/Ser-rich)"
FT REGION 246..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 460
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 422
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 460..466
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 507
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 764 AA; 82126 MW; 66008EA8560A2F7D CRC64;
WFHGNLSGKE AEKLILERGK NGSFLVRESQ SKPGDFVLSV RTDDKVTHVM IRWQDKKYDV
GGGESFATLS ELIEHYKRHP MVETCGTVVH LRQPFNATRI TAAGINARVE QLVKGGFWEE
FESLQQDSRD TFSRHEGYKD ENRLKNRYHD HTRVKLQDVE RSAPGAEYIN ANYIRLPTDG
DLYNMSSSSE SLNSTVAACP ACTAAQTQRN CPNCHLLNKT CVKCAVKSAT LPTNCATCNR
KSDSLSKHKR SESMSASANA SAAGTGPGTP TAAGNTSAAA ALNGCLAVLL KKHCGDASPP
PSTTSSCSGP LTGSLLNGEG NQFKTYIATQ GCLANTKTDF WNMIWQENTR VIVMTTKEIE
RGKTKCERYW PDEGQCKQFG HAKVHCIKEN STNDYTLREF LFSWRDKPER RIYHYHFQVW
PDHGVPADPG CVLNFLQDVN TKQSSLAQAG EKPGPICVHC SAGIGRTGTF IVIDMILDQI
VRNGLDTEID IQRTIQMVRS QRSGMVQTEA QYKFVYYAVQ HYIQTLIARK RAEEQSLQVG
REYTNIKYTG EIGNDSQRSP LPPAISNLSL VSCKSAVAEP LTAAAAAAAV AANAGNKHAA
KLQPPLPPLG ASNNNNSSGN SGSYCNSSSS TSTAQHNGVV SSSNNCSSGS GSANSSNANG
NGNILGNGSN MRKSNFYSDS LAALKLQQQQ LHDAATAAAA AALASAAAPA ATTTAASASA
AAAAAAAAKY KNIPKDMNSL RQPHAAYVAA APALPPPPTP PRKT
