ID   PPAC1_DROME             Reviewed;         155 AA.
AC   P82890; A4V2V3; Q9VFR9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Low molecular weight phosphotyrosine protein phosphatase 1;
DE            EC=3.1.3.48;
DE   AltName: Full=Low molecular weight cytosolic acid phosphatase 1;
DE            EC=3.1.3.2;
DE   AltName: Full=PTPase 1;
GN   Name=primo-1; 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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
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).
CC   -!- FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl
CC       phosphates and natural and synthetic acyl phosphates. {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;
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Cone cells and primary pigment cells in developing
CC       pupal retina. {ECO:0000269|PubMed:10675607}.
CC   -!- DEVELOPMENTAL STAGE: Larvae, pupae and adults.
CC       {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; AAN13591.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAO41564.1; -; Genomic_DNA.
DR   RefSeq; NP_001027186.1; NM_001032015.2.
DR   RefSeq; NP_001027187.1; NM_001032016.2.
DR   PDB; 7CUY; X-ray; 2.08 A; A/B=1-155.
DR   PDBsum; 7CUY; -.
DR   AlphaFoldDB; P82890; -.
DR   SMR; P82890; -.
DR   STRING; 7227.FBpp0099893; -.
DR   PaxDb; 7227-FBpp0099893; -.
DR   DNASU; 3772179; -.
DR   EnsemblMetazoa; FBtr0091747; FBpp0099893; FBgn0040077.
DR   EnsemblMetazoa; FBtr0091748; FBpp0099895; FBgn0040077.
DR   GeneID; 3772179; -.
DR   KEGG; dme:Dmel_CG33748; -.
DR   UCSC; CG33748-RA; d. melanogaster.
DR   AGR; FB:FBgn0040077; -.
DR   CTD; 3772179; -.
DR   FlyBase; FBgn0040077; primo-1.
DR   VEuPathDB; VectorBase:FBgn0040077; -.
DR   eggNOG; KOG3217; Eukaryota.
DR   GeneTree; ENSGT00940000167505; -.
DR   HOGENOM; CLU_071415_2_0_1; -.
DR   InParanoid; P82890; -.
DR   OMA; VCHGNIC; -.
DR   PhylomeDB; P82890; -.
DR   BioGRID-ORCS; 3772179; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 3772179; -.
DR   PRO; PR:P82890; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0040077; Expressed in Malpighian tubule and 14 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0005634; C:nucleus; 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:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:FlyBase.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:FlyBase.
DR   CDD; cd16343; LMWPTP; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
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   PANTHER; PTHR11717:SF7; LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11717; LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE; 1.
DR   Pfam; PF01451; LMWPc; 1.
DR   PRINTS; PR00719; LMWPTPASE.
DR   PRINTS; PR00720; MAMMALPTPASE.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; Phosphotyrosine protein phosphatases I; 1.
DR   Genevisible; P82890; DM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydrolase; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..155
FT                   /note="Low molecular weight phosphotyrosine protein
FT                   phosphatase 1"
FT                   /id="PRO_0000046562"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        15
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        124
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   STRAND          3..14
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   HELIX           15..29
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   STRAND          34..43
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   TURN            45..48
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   HELIX           53..61
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   HELIX           77..80
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   STRAND          82..88
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   HELIX           89..98
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   STRAND          106..109
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:7CUY"
FT   HELIX           132..151
FT                   /evidence="ECO:0007829|PDB:7CUY"
SQ   SEQUENCE   155 AA;  17556 MW;  26C05D1EC3B1A07C CRC64;
     MVRKVLMICL GNICRSPIAE VVMVDTLEKA NVKDVEVDSA AIGGWHVGNR ADPRAISTLQ
     KHGLKCTHIV RQIRKQDFSE FDYIFGMDED NMSELRRLAP KGSKAELLML GDFGLEKKNR
     IIEDPYYERG AEGFETAYQQ CVVACAAFMK ERLQK
//