CSW_DROME
ID CSW_DROME Reviewed; 845 AA.
AC P29349; Q24032; Q24033; Q8I074; Q8I0H8; Q8I0S4; Q8ISD5; Q8ISD6; Q9V3H1;
AC Q9W524;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Tyrosine-protein phosphatase corkscrew;
DE EC=3.1.3.48;
GN Name=csw; ORFNames=CG3954;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=1638629; DOI=10.1016/0092-8674(92)90098-w;
RA Perkins L.A., Larsen I., Perrimon N.;
RT "Corkscrew encodes a putative protein tyrosine phosphatase that functions
RT to transduce the terminal signal from the receptor tyrosine kinase torso.";
RL Cell 70:225-236(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 4).
RC STRAIN=DP CN BW;
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 (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 2 AND 4), AND VARIANTS THR-119 AND SER-749.
RC STRAIN=10A, Ann Arbor1, Ann Arbor20, Ann Arbor3, Ann Arbor6, Kakamega-b1,
RC Kakamega-b3, Kakamega-b4, Kenya-HLa3, Kenya-HLa6, Kenya-HLb1, M2,
RC Makindu-b1, Makindu-b5, Nairobi-a, PYR2, Reids2, and Sapporo;
RX PubMed=12694293; DOI=10.1046/j.1365-294x.2003.01741.x;
RA Riley R.M., Jin W., Gibson G.;
RT "Contrasting selection pressures on components of the Ras-mediated signal
RT transduction pathway in Drosophila.";
RL Mol. Ecol. 12:1315-1323(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2 AND 4).
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 4).
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP FUNCTION.
RX PubMed=8948575; DOI=10.1006/dbio.1996.0285;
RA Perkins L.A., Johnson M.R., Melnick M.B., Perrimon N.;
RT "The nonreceptor protein tyrosine phosphatase corkscrew functions in
RT multiple receptor tyrosine kinase pathways in Drosophila.";
RL Dev. Biol. 180:63-81(1996).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [10]
RP FUNCTION, INTERACTION WITH DRPR, AND DISRUPTION PHENOTYPE.
RX PubMed=22426252; DOI=10.1038/nn.3066;
RA Logan M.A., Hackett R., Doherty J., Sheehan A., Speese S.D., Freeman M.R.;
RT "Negative regulation of glial engulfment activity by Draper terminates
RT glial responses to axon injury.";
RL Nat. Neurosci. 15:722-730(2012).
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.
CC Dephosphorylates drpr isoform A which is required for the inhibition by
CC drpr isoform A of glial cell engulfment of axonal debris produced
CC following axonal injury (PubMed:22426252). {ECO:0000269|PubMed:1638629,
CC ECO:0000269|PubMed:22426252, ECO:0000269|PubMed:8948575}.
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 -!- SUBUNIT: Interacts with drpr isoform A. {ECO:0000269|PubMed:22426252}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=2;
CC IsoId=P29349-1; Sequence=Displayed;
CC Name=1; Synonyms=Y1229, A;
CC IsoId=P29349-2; Sequence=VSP_005141;
CC Name=3; Synonyms=C;
CC IsoId=P29349-3; Sequence=VSP_005139, VSP_005141;
CC Name=4; Synonyms=4A, B;
CC IsoId=P29349-4; Sequence=VSP_005140;
CC -!- TISSUE SPECIFICITY: Expressed uniformly throughout all tissues during
CC embryogenesis. {ECO:0000269|PubMed:1638629}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:1638629}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in glia results in
CC significantly reduced inhibitory activity of drpr isoform A on glial
CC cell engulfment of axonal debris. {ECO:0000269|PubMed:22426252}.
CC -!- MISCELLANEOUS: The PTPase domain is interrupted by a PTPase insert
CC which shares no homologies with other PTPase proteins. This PTPase
CC insert is reminiscent of the kinase insert within the kinase catalytic
CC domains of several receptor tyrosine kinases.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
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DR EMBL; M94730; AAA28433.1; -; mRNA.
DR EMBL; U19909; AAB02543.1; -; Genomic_DNA.
DR EMBL; U19909; AAB02544.1; -; Genomic_DNA.
DR EMBL; AY135117; AAN17607.1; -; Genomic_DNA.
DR EMBL; AY135117; AAN17608.1; -; Genomic_DNA.
DR EMBL; AY135118; AAN17609.1; -; Genomic_DNA.
DR EMBL; AY135118; AAN17610.1; -; Genomic_DNA.
DR EMBL; AY135119; AAN17611.1; -; Genomic_DNA.
DR EMBL; AY135119; AAN17612.1; -; Genomic_DNA.
DR EMBL; AY135120; AAN17613.1; -; Genomic_DNA.
DR EMBL; AY135120; AAN17614.1; -; Genomic_DNA.
DR EMBL; AY135121; AAN17615.1; -; Genomic_DNA.
DR EMBL; AY135121; AAN17616.1; -; Genomic_DNA.
DR EMBL; AY135122; AAN17617.1; -; Genomic_DNA.
DR EMBL; AY135122; AAN17618.1; -; Genomic_DNA.
DR EMBL; AY135123; AAN17619.1; -; Genomic_DNA.
DR EMBL; AY135123; AAN17620.1; -; Genomic_DNA.
DR EMBL; AY135124; AAN17621.1; -; Genomic_DNA.
DR EMBL; AY135124; AAN17622.1; -; Genomic_DNA.
DR EMBL; AY135125; AAN17623.1; -; Genomic_DNA.
DR EMBL; AY135125; AAN17624.1; -; Genomic_DNA.
DR EMBL; AY135126; AAN17625.1; -; Genomic_DNA.
DR EMBL; AY135126; AAN17626.1; -; Genomic_DNA.
DR EMBL; AY135127; AAN17627.1; -; Genomic_DNA.
DR EMBL; AY135127; AAN17628.1; -; Genomic_DNA.
DR EMBL; AY135128; AAN17629.1; -; Genomic_DNA.
DR EMBL; AY135128; AAN17630.1; -; Genomic_DNA.
DR EMBL; AY135129; AAN17631.1; -; Genomic_DNA.
DR EMBL; AY135129; AAN17632.1; -; Genomic_DNA.
DR EMBL; AY135130; AAN17633.1; -; Genomic_DNA.
DR EMBL; AY135130; AAN17634.1; -; Genomic_DNA.
DR EMBL; AY135131; AAN17635.1; -; Genomic_DNA.
DR EMBL; AY135131; AAN17636.1; -; Genomic_DNA.
DR EMBL; AY135132; AAN17637.1; -; Genomic_DNA.
DR EMBL; AY135132; AAN17638.1; -; Genomic_DNA.
DR EMBL; AY135133; AAN17639.1; -; Genomic_DNA.
DR EMBL; AY135133; AAN17640.1; -; Genomic_DNA.
DR EMBL; AY135134; AAN17641.1; -; Genomic_DNA.
DR EMBL; AY135134; AAN17642.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45724.2; -; Genomic_DNA.
DR EMBL; AE014298; AAG22389.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF45725.1; -; Genomic_DNA.
DR EMBL; AL132797; CAB65870.1; -; Genomic_DNA.
DR EMBL; AL132797; CAB65871.1; -; Genomic_DNA.
DR EMBL; BT001484; AAN71239.1; -; mRNA.
DR PIR; A43254; A43254.
DR RefSeq; NP_477130.1; NM_057782.5. [P29349-2]
DR RefSeq; NP_477131.1; NM_057783.3. [P29349-4]
DR RefSeq; NP_726793.1; NM_166928.2. [P29349-3]
DR AlphaFoldDB; P29349; -.
DR SMR; P29349; -.
DR BioGRID; 69557; 67.
DR IntAct; P29349; 3.
DR STRING; 7227.FBpp0070363; -.
DR iPTMnet; P29349; -.
DR PaxDb; P29349; -.
DR DNASU; 45278; -.
DR EnsemblMetazoa; FBtr0070378; FBpp0070362; FBgn0000382. [P29349-2]
DR EnsemblMetazoa; FBtr0070379; FBpp0070363; FBgn0000382. [P29349-4]
DR EnsemblMetazoa; FBtr0070380; FBpp0070364; FBgn0000382. [P29349-3]
DR GeneID; 45278; -.
DR KEGG; dme:Dmel_CG3954; -.
DR CTD; 45278; -.
DR FlyBase; FBgn0000382; csw.
DR VEuPathDB; VectorBase:FBgn0000382; -.
DR eggNOG; KOG0790; Eukaryota.
DR GeneTree; ENSGT00940000167235; -.
DR HOGENOM; CLU_001645_9_10_1; -.
DR InParanoid; P29349; -.
DR OMA; VIFQQNT; -.
DR PhylomeDB; P29349; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; P29349; -.
DR BioGRID-ORCS; 45278; 2 hits in 3 CRISPR screens.
DR GenomeRNAi; 45278; -.
DR PRO; PR:P29349; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000382; Expressed in spermathecum and 21 other tissues.
DR ExpressionAtlas; P29349; baseline and differential.
DR Genevisible; P29349; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IDA:FlyBase.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:FlyBase.
DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IPI:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IMP:FlyBase.
DR GO; GO:0008069; P:dorsal/ventral axis specification, ovarian follicular epithelium; IMP:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:FlyBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007444; P:imaginal disc development; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IEA:UniProt.
DR GO; GO:0007498; P:mesoderm development; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IGI:FlyBase.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:FlyBase.
DR GO; GO:0042461; P:photoreceptor cell development; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
DR GO; GO:0007465; P:R7 cell fate commitment; IGI:FlyBase.
DR GO; GO:0045314; P:regulation of compound eye photoreceptor development; IMP:FlyBase.
DR GO; GO:0045500; P:sevenless signaling pathway; IDA:FlyBase.
DR GO; GO:0007362; P:terminal region determination; IMP:UniProtKB.
DR GO; GO:0008293; P:torso signaling pathway; IMP:FlyBase.
DR GO; GO:0007418; P:ventral midline development; IMP:FlyBase.
DR Gene3D; 3.30.505.10; -; 2.
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; 2.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Hydrolase;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Repeat;
KW SH2 domain.
FT CHAIN 1..845
FT /note="Tyrosine-protein phosphatase corkscrew"
FT /id="PRO_0000094850"
FT DOMAIN 6..101
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 111..205
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 227..645
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 289..444
FT /note="PTPase insert (Cys/Ser-rich)"
FT REGION 362..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 583
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 545
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 583..589
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 630
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005139"
FT VAR_SEQ 1..110
FT /note="MSSRRWFHPTISGIEAEKLLQEQGFDGSFLARLSSSNPGAFTLSVRRGNEVT
FT HIKIQNNGDFFDLYGGEKFATLPELVQYYMENGELKEKNGQAIELKQPLICAEPTTER
FT -> MLFNKCLEKLSSSLGNVVNHKLQEKQVYNNNNINNNNNNTLNNNNAYNNQRNFEYE
FT RAIQAHYGSKGRRSEERERSGKFKASKGRKAKVTPPTETPEAQEPACKNCMTHDELAQI
FT IKGVAKGADAQRNRDNRLQRRRRPLSAQPSAAASASTSTESLHRLTPSPQASYPATPTS
FT WTATPPQFPAAFGGASCSNSTLSLLATMRVQLHGYT (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005140"
FT VAR_SEQ 810..845
FT /note="GKMQQPAPPLRPRPGILKLLTSPVIFQQNSKTFPKT -> AKFKNIPKDMIG
FT LRPPSHAPALPPPPTPPRKT (in isoform 1 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1638629"
FT /id="VSP_005141"
FT VARIANT 119
FT /note="K -> T (in strain: Kenya-HLa3, Kenya-HLa6, Kakamega-
FT b1 and Makindu-b1)"
FT /evidence="ECO:0000269|PubMed:12694293"
FT VARIANT 749
FT /note="G -> S (in strain: Ann Arbor1, DP CN BW, Kakamega-
FT b1, Kakamega-b3, Kakamega-b4, Kenya-HLa3, Kenya-HLa6,
FT Makindu-b5 and Reids2)"
FT /evidence="ECO:0000269|PubMed:12694293"
FT CONFLICT 815
FT /note="P -> S (in Ref. 2; AAB02544)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 845 AA; 92975 MW; 2147F0F2576202CC CRC64;
MSSRRWFHPT ISGIEAEKLL QEQGFDGSFL ARLSSSNPGA FTLSVRRGNE VTHIKIQNNG
DFFDLYGGEK FATLPELVQY YMENGELKEK NGQAIELKQP LICAEPTTER WFHGNLSGKE
AEKLILERGK NGSFLVRESQ SKPGDFVLSV RTDDKVTHVM IRWQDKKYDV GGGESFGTLS
ELIDHYKRNP MVETCGTVVH LRQPFNATRI TAAGINARVE QLVKGGFWEE FESLQQDSRD
TFSRNEGYKQ ENRLKNRYRN ILPYDHTRVK LLDVEHSVAG AEYINANYIR LPTDGDLYNM
SSSSESLNSS VPSCPACTAA QTQRNCSNCQ LQNKTCVQCA VKSAILPYSN CATCSRKSDS
LSKHKRSESS ASSSPSSGSG SGPGSSGTSG VSSVNGPGTP TNLTSGTAGC LVGLLKRHSN
DSSGAVSISM AERERERERE MFKTYIATQG CLLTQQVNTV TDFWNMVWQE NTRVIVMTTK
EYERGKEKCA RYWPDEGRSE QFGHARIQCV SENSTSDYTL REFLVSWRDQ PARRIFHYHF
QVWPDHGVPA DPGCVLNFLQ DVNTRQSHLA QAGEKPGPIC VHCSAGIGRT GTFIVIDMIL
DQIVRNGLDT EIDIQRTIQM VRSQRSGLVQ TEAQYKFVYY AVQHYIQTLI ARKRAEEQSL
QVGREYTNIK YTGEIGNDSQ RSPLPPAISS ISLVPSKTPL TPTSADLGTG MGLSMGVGMG
VGNKHASKQQ PPLPVVNCNN NNNGIGNSGC SNGGGSSTTS SSNGSSNGNI NALLGGIGLG
LGGNMRKSNF YSDSLKQQQQ REEQAPAGAG KMQQPAPPLR PRPGILKLLT SPVIFQQNSK
TFPKT
