ID   PTP61_DROME             Reviewed;         548 AA.
AC   Q9W0G1; Q27932; Q8SZY3; Q9W0G2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 61F;
DE            EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000269|PubMed:12014990, ECO:0000269|PubMed:8463208};
DE   AltName: Full=dPTP61F;
GN   Name=Ptp61F {ECO:0000312|FlyBase:FBgn0267487};
GN   Synonyms=PTP1B {ECO:0000312|FlyBase:FBgn0267487};
GN   ORFNames=CG9181 {ECO:0000312|FlyBase:FBgn0267487};
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] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B), FUNCTION,
RP   CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=Canton-S {ECO:0000269|PubMed:8463208};
RC   TISSUE=Head {ECO:0000269|PubMed:8463208};
RX   PubMed=8463208; DOI=10.1016/s0021-9258(18)53111-2;
RA   McLaughlin S., Dixon J.E.;
RT   "Alternative splicing gives rise to a nuclear protein tyrosine phosphatase
RT   in Drosophila.";
RL   J. Biol. Chem. 268:6839-6842(1993).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RA   Kung T.Y., Tian S.S., Zinn K.;
RT   "Identification of a Drosophila protein tyrosine phosphatase expressed in a
RT   pattern of segmental stripes in the germ band extended embryo.";
RL   Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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   [4] {ECO:0000305}
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   [5] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC   TISSUE=Larva {ECO:0000269|PubMed:12537569}, and Pupae
RC   {ECO:0000269|PubMed:12537569};
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   [6]
RP   INTERACTION WITH DOCK, DEVELOPMENTAL STAGE, AND DOMAIN.
RX   PubMed=8663600; DOI=10.1074/jbc.271.29.17002;
RA   Clemens J.C., Ursuliak Z., Clemens K.K., Price J.V., Dixon J.E.;
RT   "A Drosophila protein-tyrosine phosphatase associates with an adapter
RT   protein required for axonal guidance.";
RL   J. Biol. Chem. 271:17002-17005(1996).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=9256342; DOI=10.1016/s0925-4773(97)00046-4;
RA   Ursuliak Z., Clemens J.C., Dixon J.E., Price J.V.;
RT   "Differential accumulation of DPTP61F alternative transcripts: regulation
RT   of a protein tyrosine phosphatase by segmentation genes.";
RL   Mech. Dev. 65:19-30(1997).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12014990; DOI=10.1042/bj20020298;
RA   Muda M., Worby C.A., Simonson-Leff N., Clemens J.C., Dixon J.E.;
RT   "Use of double-stranded RNA-mediated interference to determine the
RT   substrates of protein tyrosine kinases and phosphatases.";
RL   Biochem. J. 366:73-77(2002).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND TYR-86, AND
RP   IDENTIFICATION BY 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 DOCK, AND MUTAGENESIS OF CYS-237.
RX   PubMed=21707536; DOI=10.1042/bj20110799;
RA   Wu C.L., Buszard B., Teng C.H., Chen W.L., Warr C.G., Tiganis T.,
RA   Meng T.C.;
RT   "Dock/Nck facilitates PTP61F/PTP1B regulation of insulin signalling.";
RL   Biochem. J. 439:151-159(2011).
CC   -!- FUNCTION: Non-receptor protein tyrosine phosphatase (PubMed:8463208).
CC       Required for maintaining dock/dreadlocks in its non-phosphorylated
CC       state (PubMed:12014990). Negative regulator of InR/insulin-like
CC       receptor signaling through dephosphorylation of tyrosines when
CC       recruited by dock/dreadlocks (PubMed:21707536).
CC       {ECO:0000269|PubMed:12014990, ECO:0000269|PubMed:21707536,
CC       ECO:0000269|PubMed:8463208}.
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, ECO:0000269|PubMed:12014990,
CC         ECO:0000269|PubMed:8463208};
CC   -!- SUBUNIT: Interacts (via C-terminus) with dock/dreadlocks; this
CC       interaction is independent of insulin stimulation and is required for
CC       dephosphorylation of the insulin-like receptor InR.
CC       {ECO:0000269|PubMed:21707536, ECO:0000269|PubMed:8663600}.
CC   -!- INTERACTION:
CC       Q9W0G1; Q24218: dock; NbExp=5; IntAct=EBI-74714, EBI-74727;
CC   -!- SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm. Membrane {ECO:0000255};
CC       Single-pass membrane protein {ECO:0000255}. Endomembrane system.
CC       Note=Associates with the membranes of the reticular network and the
CC       mitochondria.
CC   -!- SUBCELLULAR LOCATION: [Isoform B]: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=A {ECO:0000269|PubMed:8463208}; Synonyms=Cytoplasmic
CC       {ECO:0000269|PubMed:8463208}, Membrane {ECO:0000303|PubMed:8663600},
CC       DPTP61Fm;
CC         IsoId=Q9W0G1-1; Sequence=Displayed;
CC       Name=B {ECO:0000269|PubMed:8463208}; Synonyms=Nuclear
CC       {ECO:0000269|PubMed:8463208, ECO:0000303|PubMed:8663600}, DPTP61Fn;
CC         IsoId=Q9W0G1-2; Sequence=VSP_050259;
CC       Name=C {ECO:0000303|PubMed:10731132};
CC         IsoId=Q9W0G1-3; Sequence=VSP_050733, VSP_050259;
CC   -!- DEVELOPMENTAL STAGE: Detected in embryonic protein extracts (at protein
CC       level) (PubMed:8663600). Expressed during oogenesis and embryogenesis
CC       (PubMed:9256342). Expressed at low levels in the central nervous system
CC       of stage 14 embryos (PubMed:8663600). High levels of expression in 0-12
CC       hour old embryos, pupae and adults with very low levels late in
CC       embryogenesis and in larvae (PubMed:8663600).
CC       {ECO:0000269|PubMed:8663600, ECO:0000269|PubMed:9256342}.
CC   -!- DEVELOPMENTAL STAGE: [Isoform A]: Accumulates in 16 segmentally
CC       repeated stripes in the ectoderm during germband extension
CC       (PubMed:9256342). These stripes are flanked by, and adjacent to, the
CC       domains of engrailed and wingless gene expression in the
CC       anterior/posterior axis (PubMed:9256342). In stage 10 embryos, isoform
CC       A colocalizes with the area lateral to the denticle belts that will
CC       give rise to naked cuticle (PubMed:9256342). Also expressed later in
CC       the central nervous system of embryos (PubMed:9256342).
CC       {ECO:0000269|PubMed:9256342}.
CC   -!- DEVELOPMENTAL STAGE: [Isoform B]: Expressed in the mesoderm and
CC       neuroblast layer during germband extension and later in the gut
CC       epithelia. {ECO:0000269|PubMed:9256342}.
CC   -!- DOMAIN: Contains 5 Potential PXXP motifs that may mediate interaction
CC       with the SH3 domains of dock/dreadlocks. {ECO:0000269|PubMed:8663600}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class 1 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; L11250; AAA75348.1; -; Genomic_DNA.
DR   EMBL; L11249; AAA75348.1; JOINED; Genomic_DNA.
DR   EMBL; L11251; AAA75349.1; -; Genomic_DNA.
DR   EMBL; L11249; AAA75349.1; JOINED; Genomic_DNA.
DR   EMBL; L11250; AAA75349.1; JOINED; Genomic_DNA.
DR   EMBL; L11252; AAA75338.1; -; mRNA.
DR   EMBL; L11253; AAA75339.1; -; mRNA.
DR   EMBL; L14849; AAA28748.1; -; mRNA.
DR   EMBL; AE014296; AAF47486.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF47487.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAN11475.1; -; Genomic_DNA.
DR   EMBL; AY069713; AAL39858.1; -; mRNA.
DR   PIR; A46101; A46101.
DR   PIR; B46101; B46101.
DR   RefSeq; NP_476687.1; NM_057339.5. [Q9W0G1-1]
DR   RefSeq; NP_476688.1; NM_057340.4. [Q9W0G1-2]
DR   RefSeq; NP_728600.1; NM_167874.2. [Q9W0G1-3]
DR   AlphaFoldDB; Q9W0G1; -.
DR   SMR; Q9W0G1; -.
DR   BioGRID; 63702; 20.
DR   IntAct; Q9W0G1; 11.
DR   STRING; 7227.FBpp0072602; -.
DR   iPTMnet; Q9W0G1; -.
DR   PaxDb; 7227-FBpp0072602; -.
DR   DNASU; 38160; -.
DR   EnsemblMetazoa; FBtr0072716; FBpp0072600; FBgn0267487. [Q9W0G1-3]
DR   EnsemblMetazoa; FBtr0072717; FBpp0072601; FBgn0267487. [Q9W0G1-2]
DR   EnsemblMetazoa; FBtr0072718; FBpp0072602; FBgn0267487. [Q9W0G1-1]
DR   GeneID; 38160; -.
DR   KEGG; dme:Dmel_CG9181; -.
DR   AGR; FB:FBgn0267487; -.
DR   CTD; 38160; -.
DR   FlyBase; FBgn0267487; Ptp61F.
DR   VEuPathDB; VectorBase:FBgn0267487; -.
DR   eggNOG; KOG0789; Eukaryota.
DR   GeneTree; ENSGT00940000154686; -.
DR   InParanoid; Q9W0G1; -.
DR   OMA; PVRAFNE; -.
DR   OrthoDB; 2911650at2759; -.
DR   PhylomeDB; Q9W0G1; -.
DR   Reactome; R-DME-210688; Dephosphorylation by PTP61F phosphatases. [Q9W0G1-1]
DR   Reactome; R-DME-210693; STAT92E dimer dephosphorylated in the nucleus and transported to the cytosol. [Q9W0G1-2]
DR   Reactome; R-DME-354192; Integrin signaling. [Q9W0G1-2]
DR   Reactome; R-DME-77387; Insulin receptor recycling. [Q9W0G1-2]
DR   Reactome; R-DME-877312; Regulation of IFNG signaling. [Q9W0G1-2]
DR   Reactome; R-DME-9833482; PKR-mediated signaling. [Q9W0G1-2]
DR   SignaLink; Q9W0G1; -.
DR   BioGRID-ORCS; 38160; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Ptp61F; fly.
DR   GenomeRNAi; 38160; -.
DR   PRO; PR:Q9W0G1; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0267487; Expressed in egg cell and 36 other cell types or tissues.
DR   ExpressionAtlas; Q9W0G1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005740; C:mitochondrial envelope; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR   GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IDA:FlyBase.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0140311; F:protein sequestering activity; IPI:FlyBase.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:FlyBase.
DR   GO; GO:0007411; P:axon guidance; IPI:FlyBase.
DR   GO; GO:0071456; P:cellular response to hypoxia; IMP:FlyBase.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:FlyBase.
DR   GO; GO:0007377; P:germ-band extension; IDA:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:FlyBase.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IGI:FlyBase.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IGI:FlyBase.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:FlyBase.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; IGI:FlyBase.
DR   GO; GO:0046621; P:negative regulation of organ growth; IMP:FlyBase.
DR   GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IGI:FlyBase.
DR   GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IMP:FlyBase.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:FlyBase.
DR   GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IGI:FlyBase.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:FlyBase.
DR   GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; TAS:Reactome.
DR   GO; GO:0032880; P:regulation of protein localization; IDA:FlyBase.
DR   GO; GO:0031647; P:regulation of protein stability; IMP:FlyBase.
DR   CDD; cd14545; PTPc-N1_2; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46047; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 61F; 1.
DR   PANTHER; PTHR46047:SF3; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 61F; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
DR   Genevisible; Q9W0G1; DM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Membrane; Nucleus;
KW   Phosphoprotein; Protein phosphatase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..548
FT                   /note="Tyrosine-protein phosphatase non-receptor type 61F"
FT                   /id="PRO_0000094853"
FT   TOPO_DOM        1..525
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        526..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        546..548
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          33..296
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          46..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           327..330
FT                   /note="PXXP motif (SH3-binding) 1"
FT                   /evidence="ECO:0000269|PubMed:8663600"
FT   MOTIF           339..342
FT                   /note="PXXP motif (SH3-binding) 2"
FT                   /evidence="ECO:0000269|PubMed:8663600"
FT   MOTIF           394..397
FT                   /note="PXXP motif (SH3-binding) 3"
FT                   /evidence="ECO:0000269|PubMed:8663600"
FT   MOTIF           459..462
FT                   /note="PXXP motif (SH3-binding) 4"
FT                   /evidence="ECO:0000269|PubMed:8663600"
FT   MOTIF           480..483
FT                   /note="PXXP motif (SH3-binding) 5"
FT                   /evidence="ECO:0000269|PubMed:8663600"
FT   COMPBIAS        407..430
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        237
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P18031,
FT                   ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-
FT                   ProRule:PRU10044"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         237..243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         86
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         1..34
FT                   /note="MSEQKTSGSGSAAAARLQIEAEYKDKGPQWHRFY -> MTKFAQRSKKTCEI
FT                   RGTMDVCVCVCVSMW (in isoform C)"
FT                   /evidence="ECO:0000303|PubMed:10731132,
FT                   ECO:0000303|PubMed:12537569"
FT                   /id="VSP_050733"
FT   VAR_SEQ         525..548
FT                   /note="SLLTYIAAGVVVGVICAYAYTKLG -> RGNRLKKSKTK (in isoform
FT                   B and isoform C)"
FT                   /evidence="ECO:0000303|PubMed:12537569,
FT                   ECO:0000303|PubMed:8463208"
FT                   /id="VSP_050259"
FT   MUTAGEN         237
FT                   /note="C->S: Abolishes phosphatase activity."
FT                   /evidence="ECO:0000269|PubMed:21707536"
FT   CONFLICT        274
FT                   /note="S -> T (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="I -> F (in Ref. 1;
FT                   AAA75348/AAA75349/AAA75338/AAA75339)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   548 AA;  62105 MW;  C6AF630E2DE3F11C CRC64;
     MSEQKTSGSG SAAAARLQIE AEYKDKGPQW HRFYKEICET CDREAKEKQF STSESERHTN
     RGLNRYRDVN PYDHSRIVLK RGSVDYINAN LVQLERAERQ YILTQGPLVD TVGHFWLMVW
     EQKSRAVLML NKLMEKKQIK CHLYWPNEMG ADKALKLPHV KLTVELVRLE TYQNFVRRWF
     KLTDLETQQS REVMQFHYTT WPDFGIPSSP NAFLKFLQQV RDSGCLSRDV GPAVVHCSAG
     IGRSGTFCLV DCCLVLIDKY GECNVSKVLC ELRSYRMGLI QTADQLDFSY QAIIEGIKKL
     HDPTFLDAEE PLISNDTETH TLDELPPPLP PRVQSLNLPL APNSGGILSL NMRAAQANGA
     ESIGKELSKD ALNNFINQHD MIHDAEVADS RPLPPLPVRA FNDSDSDEDY LLDDDDEDDT
     DEDEEYETIN EHDADPVNGH VPATTQPHAD DVNANNEKPA VPVDEQHKAN GIDPIPGQLP
     ASPENELKRR KRNEYQASLE QKVNDMKRKQ RENEDKQLAA KKRRSLLTYI AAGVVVGVIC
     AYAYTKLG
//