PPAC_DICDI
ID PPAC_DICDI Reviewed; 179 AA.
AC Q55GW2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Low molecular weight phosphotyrosine protein phosphatase;
DE Short=LMW-PTP;
DE Short=LMW-PTPase;
DE EC=3.1.3.48;
DE AltName: Full=Low molecular weight cytosolic acid phosphatase;
DE EC=3.1.3.2;
GN Name=acp1; ORFNames=DDB_G0267484;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC phosphatase family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73195.1; -; Genomic_DNA.
DR RefSeq; XP_647072.1; XM_641980.1.
DR AlphaFoldDB; Q55GW2; -.
DR SMR; Q55GW2; -.
DR STRING; 44689.DDB0266663; -.
DR PaxDb; Q55GW2; -.
DR EnsemblProtists; EAL73195; EAL73195; DDB_G0267484.
DR GeneID; 8615876; -.
DR KEGG; ddi:DDB_G0267484; -.
DR dictyBase; DDB_G0267484; acp1.
DR eggNOG; KOG3217; Eukaryota.
DR HOGENOM; CLU_071415_2_2_1; -.
DR InParanoid; Q55GW2; -.
DR OMA; TGSWHVG; -.
DR PhylomeDB; Q55GW2; -.
DR PRO; PR:Q55GW2; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; ISS:dictyBase.
DR GO; GO:0016791; F:phosphatase activity; ISS:dictyBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR InterPro; IPR023485; Ptyr_pPase.
DR InterPro; IPR036196; Ptyr_pPase_sf.
DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR Pfam; PF01451; LMWPc; 1.
DR PRINTS; PR00719; LMWPTPASE.
DR SMART; SM00226; LMWPc; 1.
DR SUPFAM; SSF52788; SSF52788; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..179
FT /note="Low molecular weight phosphotyrosine protein
FT phosphatase"
FT /id="PRO_0000331562"
FT ACT_SITE 15
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT ACT_SITE 21
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11064"
SQ SEQUENCE 179 AA; 20470 MW; E14FE7B06D8D697B CRC64;
MSADSKNQKK VLFVCLGNIC RSTMAEIVLR GLVHSRGILD DFQIDSAGTS SYHIGDTPDP
RTVQSCNQNM GRAISEESLK HFKSIPLHRA RQFTDEDFSK FDYIFAMDES NLSNIKKVLK
HSTTKDNHIA TIKRLGEYHT HKKINVEDPY YGDMSNFNIC FNHVHDCLVN FLKEIESLN
