PPAC2_DROME
ID PPAC2_DROME Reviewed; 164 AA.
AC P82891; Q0KI75; Q9VFR9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Low molecular weight phosphotyrosine protein phosphatase 2;
DE EC=3.1.3.48 {ECO:0000305|PubMed:10675607};
DE AltName: Full=Low molecular weight cytosolic acid phosphatase 2;
DE EC=3.1.3.2 {ECO:0000269|PubMed:10675607};
DE AltName: Full=PTPase 2;
GN Name=primo-2; ORFNames=CG31311;
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], MUTAGENESIS OF CYS-14, FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND CATALYTIC ACTIVITY.
RC TISSUE=Embryo, and Pupae;
RX PubMed=10675607; DOI=10.1016/s0378-1119(99)00553-3;
RA Miller D.T., Read R., Rusconi J., Cagan R.L.;
RT "The Drosophila primo locus encodes two low-molecular-weight tyrosine
RT phosphatases.";
RL Gene 243:1-9(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [3]
RP GENOME REANNOTATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
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).
CC -!- FUNCTION: Catalyzes the dephosphorylation of tyrosine phosphorylated
CC proteins and low-MW aryl phosphates (PubMed:10675607). Can contribute
CC to the regulation of a variety of developmental processes
CC (PubMed:10675607). {ECO:0000269|PubMed:10675607,
CC ECO:0000303|PubMed:10675607}.
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;
CC Evidence={ECO:0000305|PubMed:10675607};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC Evidence={ECO:0000305|PubMed:10675607};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000269|PubMed:10675607};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC Evidence={ECO:0000269|PubMed:10675607};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Cone cells and primary pigment cells in developing
CC pupal retina. {ECO:0000269|PubMed:10675607}.
CC -!- DEVELOPMENTAL STAGE: Embryo and adult. {ECO:0000269|PubMed:10675607}.
CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC phosphatase family. {ECO:0000305}.
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DR EMBL; AE014297; AAF54981.3; -; Genomic_DNA.
DR EMBL; AY089477; AAL90215.1; -; mRNA.
DR RefSeq; NP_001027188.1; NM_001032017.2.
DR AlphaFoldDB; P82891; -.
DR SMR; P82891; -.
DR STRING; 7227.FBpp0100064; -.
DR PaxDb; P82891; -.
DR PRIDE; P82891; -.
DR DNASU; 3772427; -.
DR EnsemblMetazoa; FBtr0091746; FBpp0100064; FBgn0040076.
DR GeneID; 3772427; -.
DR KEGG; dme:Dmel_CG33747; -.
DR UCSC; CG33747-RB; d. melanogaster.
DR CTD; 3772427; -.
DR FlyBase; FBgn0040076; primo-2.
DR VEuPathDB; VectorBase:FBgn0040076; -.
DR eggNOG; KOG3217; Eukaryota.
DR GeneTree; ENSGT00940000167505; -.
DR HOGENOM; CLU_071415_2_0_1; -.
DR InParanoid; P82891; -.
DR OMA; QGEWHVE; -.
DR PhylomeDB; P82891; -.
DR BioGRID-ORCS; 3772427; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 3772427; -.
DR PRO; PR:P82891; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0040076; Expressed in testis and 13 other tissues.
DR Genevisible; P82891; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
DR InterPro; IPR023485; Ptyr_pPase.
DR InterPro; IPR036196; Ptyr_pPase_sf.
DR InterPro; IPR002115; Tyr_Pase_low_mol_wt_mml.
DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR Pfam; PF01451; LMWPc; 1.
DR PRINTS; PR00719; LMWPTPASE.
DR PRINTS; PR00720; MAMMALPTPASE.
DR SMART; SM00226; LMWPc; 1.
DR SUPFAM; SSF52788; SSF52788; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..164
FT /note="Low molecular weight phosphotyrosine protein
FT phosphatase 2"
FT /id="PRO_0000046563"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT ACT_SITE 20
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT MUTAGEN 14
FT /note="C->S: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:10675607"
FT CONFLICT 31
FT /note="L -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="A -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 164 AA; 18541 MW; 320485DF557E4CCD CRC64;
MGKRSQKSSV LMVCVGNLCR SPIAEAVMRD LVARAGLQGE WHVESAGIED WHSGHQPDER
ALNVLARHNI EYNGKARVLA PEDFLEFDYI FAMDLSNLAA LRRMAPKGTT AKLLILGNFG
LKPDERIIED PYYDIGEASF EEIYRQCSIA CRNFLKQARL KQIM
