ID   EPP_DROME               Reviewed;         751 AA.
AC   Q9VCE9; Q86PB2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Ecdysteroid-phosphate phosphatase {ECO:0000303|PubMed:17348005};
DE            EC=3.1.3.- {ECO:0000269|PubMed:17348005};
DE   AltName: Full=Protein UBASH3A homolog {ECO:0000305};
DE   AltName: Full=Ubiquitin-associated and SH3 domain-containing protein {ECO:0000305};
GN   Name=Epp {ECO:0000303|PubMed:17348005,
GN   ECO:0000312|FlyBase:FBgn0039137};
GN   ORFNames=CG13604 {ECO:0000312|FlyBase:FBgn0039137};
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Head;
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).
RN   [4] {ECO:0000312|EMBL:AAO24996.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAO24996.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAO24996.1};
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=17348005; DOI=10.1002/prot.21357;
RA   Davies L., Anderson I.P., Turner P.C., Shirras A.D., Rees H.H.,
RA   Rigden D.J.;
RT   "An unsuspected ecdysteroid/steroid phosphatase activity in the key T-cell
RT   regulator, Sts-1: surprising relationship to insect ecdysteroid phosphate
RT   phosphatase.";
RL   Proteins 67:720-731(2007).
CC   -!- FUNCTION: Steroid phosphatase that dephosphorylates ecdysteroids such
CC       as ecdysone 22-phosphate (E22P), 3-epi-ecdysone 22-phosphate (E22P) and
CC       3-epi-ecdysone 2-phosphate (E2P) (PubMed:17348005). Likely catalyzes
CC       the conversion of inactive phosphorylated ecdysteroids into their
CC       active forms (By similarity). Shows high activity towards ecdysone 22-
CC       phosphate (E22P), but is also significantly active against 3-epi-
CC       ecdysone 22-phosphate (E22P) and 3-epi-ecdysone 2-phosphate (E2P)
CC       (PubMed:17348005). Also displays acid phosphatase activity towards 4-
CC       nitrophenyl phosphate (pNNP) in vitro (PubMed:17348005). Has no
CC       activity towards 3-epi-ecdysone 3-phosphate (E3P) (PubMed:17348005).
CC       {ECO:0000250|UniProtKB:Q7YTB0, ECO:0000269|PubMed:17348005}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ecdysone 22-phosphate + H2O = ecdysone + phosphate;
CC         Xref=Rhea:RHEA:63576, ChEBI:CHEBI:15377, ChEBI:CHEBI:16688,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:147380;
CC         Evidence={ECO:0000269|PubMed:17348005};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=20-hydroxyecdysone 22-phosphate + H2O = 20-hydroxyecdysone +
CC         phosphate; Xref=Rhea:RHEA:63580, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16587, ChEBI:CHEBI:43474, ChEBI:CHEBI:147382;
CC         Evidence={ECO:0000250|UniProtKB:Q7YTB0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxyecdysone 22-phosphate + H2O = 2-deoxyecdysone +
CC         phosphate; Xref=Rhea:RHEA:63584, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:19566, ChEBI:CHEBI:43474, ChEBI:CHEBI:147386;
CC         Evidence={ECO:0000250|UniProtKB:Q7YTB0};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Active at pH 4 and 7.4 with ecdysone 22-phosphate (E22P),
CC         3-epi-ecdysone 22-phosphate (E22P) or 3-epi-ecdysone 2-phosphate
CC         (E2P) as substrate. {ECO:0000269|PubMed:17348005};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17348005}.
CC       Nucleus {ECO:0000269|PubMed:17348005}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A {ECO:0000312|FlyBase:FBgn0039137}; Synonyms=long
CC       {ECO:0000303|PubMed:17348005};
CC         IsoId=Q9VCE9-1; Sequence=Displayed;
CC       Name=B {ECO:0000312|FlyBase:FBgn0039137}; Synonyms=C
CC       {ECO:0000312|FlyBase:FBgn0039137};
CC         IsoId=Q9VCE9-2; Sequence=VSP_061772;
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DR   EMBL; AE014297; AAF56217.1; -; Genomic_DNA.
DR   EMBL; AE014297; ABW08745.1; -; Genomic_DNA.
DR   EMBL; AE014297; ABW08746.1; -; Genomic_DNA.
DR   EMBL; AY051411; AAK92835.1; -; mRNA.
DR   EMBL; BT003239; AAO24996.1; -; mRNA.
DR   RefSeq; NP_001097896.1; NM_001104426.1. [Q9VCE9-2]
DR   RefSeq; NP_001097897.1; NM_001104427.1. [Q9VCE9-2]
DR   RefSeq; NP_651202.1; NM_142945.3. [Q9VCE9-1]
DR   AlphaFoldDB; Q9VCE9; -.
DR   SMR; Q9VCE9; -.
DR   BioGRID; 67775; 4.
DR   DIP; DIP-21366N; -.
DR   IntAct; Q9VCE9; 1.
DR   STRING; 7227.FBpp0303396; -.
DR   PaxDb; 7227-FBpp0083896; -.
DR   DNASU; 42840; -.
DR   EnsemblMetazoa; FBtr0084509; FBpp0083896; FBgn0039137. [Q9VCE9-1]
DR   EnsemblMetazoa; FBtr0113275; FBpp0112187; FBgn0039137. [Q9VCE9-2]
DR   EnsemblMetazoa; FBtr0113276; FBpp0112188; FBgn0039137. [Q9VCE9-2]
DR   GeneID; 42840; -.
DR   KEGG; dme:Dmel_CG13604; -.
DR   UCSC; CG13604-RA; d. melanogaster. [Q9VCE9-1]
DR   AGR; FB:FBgn0039137; -.
DR   CTD; 42840; -.
DR   FlyBase; FBgn0039137; Epp.
DR   VEuPathDB; VectorBase:FBgn0039137; -.
DR   eggNOG; KOG3734; Eukaryota.
DR   GeneTree; ENSGT00940000167071; -.
DR   InParanoid; Q9VCE9; -.
DR   OMA; NMPKEIP; -.
DR   OrthoDB; 5484137at2759; -.
DR   PhylomeDB; Q9VCE9; -.
DR   BioGRID-ORCS; 42840; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 42840; -.
DR   PRO; PR:Q9VCE9; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0039137; Expressed in eye disc (Drosophila) and 36 other cell types or tissues.
DR   ExpressionAtlas; Q9VCE9; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003993; F:acid phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0102531; F:ecdysteroid-phosphate phosphatase activity; IDA:FlyBase.
DR   GO; GO:0016791; F:phosphatase activity; ISS:FlyBase.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; ISS:FlyBase.
DR   GO; GO:0045455; P:ecdysteroid metabolic process; IDA:FlyBase.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   CDD; cd11791; SH3_UBASH3; 1.
DR   CDD; cd14301; UBA_UBS3B; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR16469; UBIQUITIN-ASSOCIATED AND SH3 DOMAIN-CONTAINING BA-RELATED; 1.
DR   PANTHER; PTHR16469:SF27; UBIQUITIN-ASSOCIATED AND SH3 DOMAIN-CONTAINING PROTEIN B; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   Genevisible; Q9VCE9; DM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Nucleus; Protein phosphatase;
KW   Reference proteome; SH3 domain.
FT   CHAIN           1..751
FT                   /note="Ecdysteroid-phosphate phosphatase"
FT                   /id="PRO_0000210995"
FT   DOMAIN          16..60
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          271..336
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          367..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..751
FT                   /note="Phosphatase-like"
FT   COMPBIAS        367..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        498
FT                   /evidence="ECO:0000250|UniProtKB:Q7YTB0"
FT   ACT_SITE        499
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7YTB0"
FT   ACT_SITE        681
FT                   /evidence="ECO:0000250|UniProtKB:Q7YTB0"
FT   VAR_SEQ         1..439
FT                   /note="Missing (in isoform B)"
FT                   /id="VSP_061772"
SQ   SEQUENCE   751 AA;  84466 MW;  FF893BB3FEDFDB2D CRC64;
     MATLPPRKSQ TPTRICISKQ HLTPLQTLLQ MGFPRHRAEK ALASTGNRGV QIASDWLLAH
     VNDGTLDECA PREYIIYACP TGPFLQQLEE FWAKSRQMCG WNGAHNYVPH ITLVSFFKAP
     DECSLQLSKA LKQVVDMTGA LLDRPLKLEP YMSQNFMGFF VAEEDANYLK RLALQYVKEV
     SNSIISDTYE QLDAIVACFP WCGAVSSGTR CIPRSSRSIS LEPHVKSLHL TLAYQFPQAQ
     FNALKALVET LDASCASNWE LRLYSRDPRL ATKQVQKVVY PHNPHETDEL ELRIGDYIYL
     NTEVVDSSSD GWAEGISWLT GSTGHLPVNY TERTAESDAW TLHRVVQLSK SVASSLTSAE
     DLDIVDGRSI STEPDDRQNT AHPDIIEGSS FEESEQSVEK YLRQTLKPCL ELPSVQLLNS
     HNLTHQHNPN TPTIEITTNM SSSSTSMSKQ PVDEILVEPP AAQPPRPDDT LSVHSDHSLH
     PGSLDASHAK NRKIYIMRHG ERVDFTFGTW IPYCFDEFGN YMRKDLNMPK TLPRRKNSPE
     GWQNDSPLTN VGVYQANLIG QALLEAQVQI DHVYCSPSYR CIQTCTSALE GLKLTGKQKI
     KLEPGLFEWM AWYPSGVPDW LTKNELTEAK FDVDLDYEPV QPASELTARL KESTEQFYER
     NHDVILQLLE QTTGNILVVA HATTLDTCSR QLTGGVPRST NELRQVIHKI PYCSLATVEQ
     VDGVWKLVEP ECLPVTHSKN PRFEWNALSA T
//