PPAC1_DROME
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 03-AUG-2022, entry version 140.
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; P82890; -.
DR PRIDE; P82890; -.
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 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 OMA; TGSWHVG; -.
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 tissues.
DR Genevisible; P82890; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0005634; C:nucleus; ISS:FlyBase.
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 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 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
