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Database: UniProt
Entry: A0A212EJG4_DANPL
LinkDB: A0A212EJG4_DANPL
Original site: A0A212EJG4_DANPL 
ID   A0A212EJG4_DANPL        Unreviewed;       697 AA.
AC   A0A212EJG4;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
GN   ORFNames=KGM_216123 {ECO:0000313|EMBL:OWR41626.1};
OS   Danaus plexippus plexippus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX   NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR41626.1, ECO:0000313|Proteomes:UP000007151};
RN   [1] {ECO:0000313|EMBL:OWR41626.1, ECO:0000313|Proteomes:UP000007151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-2 {ECO:0000313|EMBL:OWR41626.1};
RX   PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA   Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT   "The monarch butterfly genome yields insights into long-distance
RT   migration.";
RL   Cell 147:1171-1185(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-
CC         phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934;
CC         Evidence={ECO:0000256|ARBA:ARBA00023732};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC         phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC         Evidence={ECO:0000256|ARBA:ARBA00001291};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWR41626.1}.
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DR   EMBL; AGBW02014472; OWR41626.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212EJG4; -.
DR   STRING; 278856.A0A212EJG4; -.
DR   KEGG; dpl:KGM_216123; -.
DR   eggNOG; KOG1089; Eukaryota.
DR   InParanoid; A0A212EJG4; -.
DR   Proteomes; UP000007151; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; IEA:UniProt.
DR   CDD; cd15738; FYVE_MTMR_unchar; 1.
DR   CDD; cd14532; PTP-MTMR6-like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR030564; Myotubularin_fam.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   Pfam; PF21098; PH-GRAM_MTMR6-like; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007151};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          83..455
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   DOMAIN          632..683
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   ACT_SITE        293
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         231..232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         293..299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   697 AA;  78651 MW;  5F1AA4DEB48AB74F CRC64;
     MRKETWILLM HISTVERLPI TTTGSPLLVR TKTFQSVFFV IPRERDCHEM HQTLLRLSQP
     VNLEELYCFH YKSTPDDLPK SAGWNFFDIQ TEFQRMNVPN EQWTLCNANR DYELCDTYPS
     EIYVPARASS AVLLGSASFR SRGRLPVLAY LHHNKAAIAR CSQPLSGFSA RCMEDEQMLD
     LIRRANPNCG YMYVVDTRPR INAMVNRAAG KGYENEAFYE NIKFQFMGIG NIHVMRKSLQ
     KLVETCEQNS PTMSSFLNGL ESSGWLKHIK SILDTSWWIA SAISGGVSVC VHCSDGWDRT
     AQVCSLAALC IEPHYRTING YQALIEKDWL SFGHKFTARC GHVACDSRER SPVFTQLLDC
     TWQLLRQAPE AFQFNERFLL TLHDHAHACQ YGTFIGNCQK DRRDLRLSER TFSLWGYMAS
     HLNEYKNPLY NPKAYPDILK PDLSAQSIRF WRGMYCRHES GVHPRESLAD LLPAAVHHAT
     ALTHHIDYLA KRISTFKNLL SGRKERKDDT VVNYQNGSSD TVDIETKMEA AEIDNKQSAM
     MSCTPIRAHD VTSKSKHRQH ARTLHYESGG NLSELECANH DHPLKEGAPK IIPLITEKAD
     AMIPATLSLL EAEISTVALD WKTIKNVTEC GCSTPLDHFS RKHHCWGCGR VVCTRCVAAR
     AALPALHAAR AAPLCAACAP STPSTPVTPP DLLTSAT
//
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