IMPA3_DANRE
ID IMPA3_DANRE Reviewed; 341 AA.
AC Q2YDR3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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; ORFNames=zgc:123256;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2005) 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}.
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DR EMBL; BC110106; AAI10107.1; -; mRNA.
DR RefSeq; NP_001032657.1; NM_001037568.1.
DR AlphaFoldDB; Q2YDR3; -.
DR SMR; Q2YDR3; -.
DR STRING; 7955.ENSDARP00000075369; -.
DR PaxDb; Q2YDR3; -.
DR Ensembl; ENSDART00000080925; ENSDARP00000075369; ENSDARG00000058114.
DR GeneID; 641570; -.
DR KEGG; dre:641570; -.
DR CTD; 54928; -.
DR ZFIN; ZDB-GENE-051127-23; bpnt2.
DR eggNOG; KOG3853; Eukaryota.
DR GeneTree; ENSGT00940000164879; -.
DR HOGENOM; CLU_034742_0_0_1; -.
DR InParanoid; Q2YDR3; -.
DR OMA; GNSMSEY; -.
DR OrthoDB; 1096950at2759; -.
DR PhylomeDB; Q2YDR3; -.
DR TreeFam; TF314300; -.
DR Reactome; R-DRE-156584; Cytosolic sulfonation of small molecules.
DR UniPathway; UPA00823; UER00788.
DR PRO; PR:Q2YDR3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000058114; Expressed in intestine and 22 other tissues.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008254; F:3'-nucleotidase activity; IBA:GO_Central.
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..341
FT /note="Inositol monophosphatase 3"
FT /id="PRO_0000289043"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 159..162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 37432 MW; 998D9833143F1904 CRC64;
MAPMGIRLSP LGIAVFCLLG VGVIYHLYAG VLSSRLAFFR QKRTVDLREL LALSIDAAVQ
GGREVKRIRE DNTLEEKSKG KTKEGASEKY TLGDLNSHRK MYYLIKNTFP NIQVNSEEHA
NAEGEATVWT RMIPEDILAK VSGGKEIPAE KITVWIDPLD ATQEYTENLL KYVTTMVCVA
VDGEPVIGVI HKPFTGYTVW GFVGEGSNVA PRDSYNTNSP KVIVSRSHAG KVKSFVQTAF
GNNTEIIPAG GAGYKALALL NPTDDKQETA DIYIHVTYIK KWDICAGDAI LKSLGGQMTT
LKGEQIDYSG LEGNKGGLLA SMKVDHKALV KRLPLWEDNK Q
