ID   IMPA3_XENLA             Reviewed;         351 AA.
AC   Q6NTW5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Inositol monophosphatase 3;
DE            Short=IMP 3;
DE            Short=IMPase 3;
DE            EC=3.1.3.25;
DE   AltName: Full=3'(2'), 5'-bisphosphate nucleotidase 2;
DE   AltName: Full=Inositol monophosphatase domain-containing protein 1;
DE   AltName: Full=Inositol-1(or 4)-monophosphatase 3;
DE   AltName: Full=Myo-inositol monophosphatase A3;
GN   Name=bpnt2; Synonyms=impa3, impad1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC         Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC068839; AAH68839.1; -; mRNA.
DR   RefSeq; NP_001084511.1; NM_001091042.1.
DR   AlphaFoldDB; Q6NTW5; -.
DR   SMR; Q6NTW5; -.
DR   GeneID; 414458; -.
DR   KEGG; xla:414458; -.
DR   CTD; 414458; -.
DR   Xenbase; XB-GENE-5751113; bpnt2.S.
DR   OMA; GNSMSEY; -.
DR   OrthoDB; 1096950at2759; -.
DR   UniPathway; UPA00823; UER00788.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 414458; Expressed in liver and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Membrane; Metal-binding; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..351
FT                   /note="Inositol monophosphatase 3"
FT                   /id="PRO_0000289044"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         164..167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  38118 MW;  2599E44B71C40E6C CRC64;
     MAPMGIRLSP LGIGVFCLLA LGVLYHVYSG FLTGRFAAFL LGDRAGDTVD LRELLAVSVR
     AAELGGVEVK KVRESNSLNE KAKGKTREGE DEKMTSGDVL SNKKMYHLIK NAFPAVLVNT
     EEQVDPDEED AVSWDHDIPD EIKDKIKTSK PVSSESITIW IDPLDATHEY AENLVKYVTT
     MVCVAVNGKP VIGVIHKPFT GYTAWAMVDE GANIKKRSSY NEKTPTFIVS RSHSGEVKEV
     TRQTFGNKTE IISAGGAGYK VLSLLDVTAD EQEKADVYIH VTYIKKWDIC AGNAILNALG
     GHMTTLKGEE ISYTGSEQNE GGLLASIGMD HSALVGKLAE KISVNAKKPA K