PTP61_DROME
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 03-AUG-2022, entry version 173.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 61F;
DE EC=3.1.3.48;
DE AltName: Full=dPTP61F;
GN Name=Ptp61F; ORFNames=CG9181;
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, AND
RP 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 (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
RC Pupae {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.
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 TISSUE SPECIFICITY.
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.
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).
CC -!- FUNCTION: Non-receptor protein tyrosine phosphatase required for
CC maintaining Dock in its non-phosphorylated state.
CC {ECO:0000269|PubMed:12014990, 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:8463208};
CC -!- INTERACTION:
CC Q9W0G1; Q24218: dock; NbExp=5; IntAct=EBI-74714, EBI-74727;
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm. 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}, DPTP61Fm;
CC IsoId=Q9W0G1-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:8463208}; Synonyms=Nuclear
CC {ECO:0000269|PubMed:8463208}, 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 -!- TISSUE SPECIFICITY: Expressed during oogenesis and embryogenesis.
CC Isoform A and isoform B are expressed in distinct patterns. Isoform B
CC is expressed in the mesoderm and neuroblast layer during germband
CC extension and later in the gut epithelia. Isoform A accumulates in 16
CC segmentally repeated stripes in the ectoderm during germband extension.
CC These stripes are flanked by, and adjacent to, the domains of engrailed
CC and wingless gene expression in the anterior/posterior axis. In stage
CC 10 embryos, isoform A colocalizes with the area lateral to the denticle
CC belts that will give rise to naked cuticle. Isoform A is also expressed
CC later in embryogenesis in the central nervous system.
CC {ECO:0000269|PubMed:9256342}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 1 subfamily. {ECO:0000305}.
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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; Q9W0G1; -.
DR PRIDE; Q9W0G1; -.
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 CTD; 38160; -.
DR FlyBase; FBgn0267487; Ptp61F.
DR VEuPathDB; VectorBase:FBgn0267487; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000154686; -.
DR InParanoid; Q9W0G1; -.
DR OMA; PVRAFNE; -.
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-877312; Regulation of IFNG 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 tissues.
DR ExpressionAtlas; Q9W0G1; baseline and differential.
DR Genevisible; Q9W0G1; DM.
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-KW.
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: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: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; IGI:FlyBase.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IGI:FlyBase.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IGI:FlyBase.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; 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:0018108; P:peptidyl-tyrosine phosphorylation; IDA: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 Gene3D; 3.90.190.10; -; 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 Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
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; Hydrolase; Membrane; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..548
FT /note="Tyrosine-protein phosphatase non-receptor type 61F"
FT /id="PRO_0000094853"
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 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 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; AAA75348/AAA75349/AAA75338/
FT 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
