IMPA3_XENTR
ID IMPA3_XENTR Reviewed; 356 AA.
AC Q28CL4; Q0VGW1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=TEgg066b01.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-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}.
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DR EMBL; CR926321; CAJ82287.1; -; mRNA.
DR EMBL; BC080464; AAH80464.1; -; mRNA.
DR RefSeq; NP_001016215.2; NM_001016215.3.
DR AlphaFoldDB; Q28CL4; -.
DR SMR; Q28CL4; -.
DR STRING; 8364.ENSXETP00000012482; -.
DR PaxDb; Q28CL4; -.
DR DNASU; 548969; -.
DR GeneID; 548969; -.
DR KEGG; xtr:548969; -.
DR CTD; 54928; -.
DR Xenbase; XB-GENE-5751033; bpnt2.
DR eggNOG; KOG3853; Eukaryota.
DR InParanoid; Q28CL4; -.
DR OrthoDB; 1096950at2759; -.
DR Reactome; R-XTR-156584; Cytosolic sulfonation of small molecules.
DR UniPathway; UPA00823; UER00788.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000005659; Expressed in skeletal muscle tissue and 14 other tissues.
DR ExpressionAtlas; Q28CL4; baseline.
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..356
FT /note="Inositol monophosphatase 3"
FT /id="PRO_0000289045"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 169..172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 344
FT /note="S -> A (in Ref. 2; AAH80464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 38720 MW; EC57250FF884BB63 CRC64;
MAPMGIRLSP LGIGVFCLLG LGVLYHVYSG FLTGKFSAFL LGDRAEDPGP GEDTVDLREL
LAVSVRAAEL GGLEVKKVRE SNSLNEKAKG KTMEGADDKM TSGDVLSNKK MYHLIKNAFP
ALKVNTEEKV EADDEDAVSW DRNIPDDIKE QIKTKHVASE SITMWIDPLD ATQEYTENLV
NYVTTMVCVA VNGKPVIGVI HKPFTGFTAW AMLDGGSSIK KRNSYNEKTP TFIVSRSHSG
EVKEVTRQTF GNKTEIISAG GAGYKVLSLL DVTDDKQETA DVYIHVTYIK KWDICAGNAI
LNALGGQMTT LKGEEIMYTG SELNKGGLLA SIGMDHGVLV EKLSEKLQVN AKKPAK
