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Database: UniProt
Entry: A0A0B2VKK8_TOXCA
LinkDB: A0A0B2VKK8_TOXCA
Original site: A0A0B2VKK8_TOXCA 
ID   A0A0B2VKK8_TOXCA        Unreviewed;       531 AA.
AC   A0A0B2VKK8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=inositol-phosphate phosphatase {ECO:0000256|ARBA:ARBA00013106};
DE            EC=3.1.3.25 {ECO:0000256|ARBA:ARBA00013106};
DE   AltName: Full=Inositol-1(or 4)-monophosphatase 3 {ECO:0000256|ARBA:ARBA00042949};
DE   AltName: Full=Myo-inositol monophosphatase A3 {ECO:0000256|ARBA:ARBA00042119};
GN   Name=impad1 {ECO:0000313|EMBL:KHN81909.1};
GN   ORFNames=Tcan_03560 {ECO:0000313|EMBL:KHN81909.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN81909.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN81909.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN81909.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) 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         Evidence={ECO:0000256|ARBA:ARBA00001033};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005152}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759}.
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:KHN81909.1}.
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DR   EMBL; JPKZ01001443; KHN81909.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2VKK8; -.
DR   STRING; 6265.A0A0B2VKK8; -.
DR   OMA; FPSRKYL; -.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   PANTHER; PTHR43028; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1.
DR   PANTHER; PTHR43028:SF4; INOSITOL MONOPHOSPHATASE 3; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          432..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   531 AA;  59047 MW;  0A50D67C20DD856C CRC64;
     MHIRVNLKNL TIFCILCAFS FIGYVILSSG ERFPDVGVEL RDVISYAVLA VEIGGRAITR
     VHEERSLGIV KKGKTAEGRD EFLTKADLAS NSLILDTFKR FPGIYVVTEE KDSHLRDEDL
     QNYRADNYEV WLGVKETIDK LPSKKVKLSK LTVWVDPLDA TQEFSEGLLE YVTVMVCIAL
     DGRPIFGAVY RPFLSETLFG LVGYGVINGN GKRWNSTVLQ NVPKKILISR SHAGTVEELV
     NKTFGDEFTV EAAGGSGYKT LRLINGTAQI YLHRTAISKW DTCAGDALIT AIGGAMIDLN
     GNPIDYRSAS NTRIDGGLFV ALKNPFTLLK SCLLLTSDQI GETRTMRELE VKLNKVALEK
     LRIASEYIRL SYELEKMLDN YRFNLSKTKS IIGISNASAA VIDYREMDPT VRIDVDDKGN
     FSVADSSLTT QSKSSEVTTR KRAGSKDNSE IKGEQEEKPN RMPVFRPFGV LEPSSAKAAR
     NDIARCIRLI CHIASIKSEL LRVMEQYKAL KTELNYVCLP TEMKGSCQVS G
//
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