ID   TP4AA_DICDI             Reviewed;         166 AA.
AC   Q54DU9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Probable protein tyrosine phosphatase type IVA A;
DE            EC=3.1.3.48;
DE   Flags: Precursor;
GN   ORFNames=DDB_G0292024;
OS   Dictyostelium discoideum (Social amoeba).
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   -!- 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000187; EAL61368.1; -; Genomic_DNA.
DR   RefSeq; XP_629773.1; XM_629771.1.
DR   AlphaFoldDB; Q54DU9; -.
DR   SMR; Q54DU9; -.
DR   STRING; 44689.Q54DU9; -.
DR   PaxDb; 44689-DDB0238561; -.
DR   EnsemblProtists; EAL61368; EAL61368; DDB_G0292024.
DR   GeneID; 8628449; -.
DR   KEGG; ddi:DDB_G0292024; -.
DR   dictyBase; DDB_G0292024; -.
DR   eggNOG; KOG2836; Eukaryota.
DR   HOGENOM; CLU_099263_2_0_1; -.
DR   InParanoid; Q54DU9; -.
DR   OMA; GQKNSCC; -.
DR   PhylomeDB; Q54DU9; -.
DR   Reactome; R-DDI-8873719; RAB geranylgeranylation.
DR   PRO; PR:Q54DU9; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14500; PTP-IVa; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR022778; CDKN3.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR23339:SF123; PROTEIN TYROSINE PHOSPHATASE TYPE IVA A-RELATED; 1.
DR   PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF05706; CDKN3; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Lipoprotein; Membrane; Methylation; Prenylation;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..163
FT                   /note="Probable protein tyrosine phosphatase type IVA A"
FT                   /id="PRO_0000329025"
FT   PROPEP          164..166
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396656"
FT   DOMAIN          10..164
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        75
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        107
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   BINDING         108..113
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         163
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           163
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..107
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   166 AA;  18422 MW;  B9A1CE094E6AB73D CRC64;
     MTGIRSALPN PASLVESSTH RFLIFDAPND DNLPLYINEL KKYNVSHLVR ACDPTYSTEP
     LQAIGIQVHD MPFADGGSPP DAVVNNWIKI LGESYKKDSK ETIGIHCVAG LGRAPVLVAI
     ALIEGGMNPL QAVEYIRERR RGSINIKQIQ YLKNYKSKKK SSCRIM
//