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Database: UniProt
Entry: A0A067R5J1_ZOONE
LinkDB: A0A067R5J1_ZOONE
Original site: A0A067R5J1_ZOONE 
ID   A0A067R5J1_ZOONE        Unreviewed;       344 AA.
AC   A0A067R5J1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   ORFNames=L798_08457 {ECO:0000313|EMBL:KDR17547.1};
OS   Zootermopsis nevadensis (Dampwood termite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Termopsidae; Zootermopsis.
OX   NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR17547.1, ECO:0000313|Proteomes:UP000027135};
RN   [1] {ECO:0000313|EMBL:KDR17547.1, ECO:0000313|Proteomes:UP000027135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KDR17547.1};
RX   PubMed=24845553; DOI=10.1038/ncomms4636;
RA   Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA   Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA   Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA   Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA   Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA   Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA   Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA   Liebig J.;
RT   "Molecular traces of alternative social organization in a termite genome.";
RL   Nat. Commun. 5:3636-3636(2014).
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}.
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DR   EMBL; KK852729; KDR17547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067R5J1; -.
DR   STRING; 136037.A0A067R5J1; -.
DR   EnsemblMetazoa; KDR17547; KDR17547; L798_08457.
DR   eggNOG; KOG3853; Eukaryota.
DR   InParanoid; A0A067R5J1; -.
DR   OMA; DELHKQP; -.
DR   OrthoDB; 3665671at2759; -.
DR   Proteomes; UP000027135; 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   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:UP000027135};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   344 AA;  37745 MW;  79D90DDE2F10BA7F CRC64;
     MRIANMNFGG TIRLNRIGIC IIIGACIILV LYINSSGMES PKTEPGKNNG FVSLKKLLVA
     AIEVAVKGGK EIVAVRNAPN IGEKSKGNTK GINDPVTKAD YNSHCVMYYS LIHSFPKVKI
     ISEENIKQSD CKNLSYLGDD SDGVHNLNPL NDELVQAEDI TVWIDPLDAT KEFTENKLQY
     VTTMVCVAVK GNPIIGVIHK PFEGEPHTFW AWEGKSASDN LKNNKADRHS TTSIIMSISH
     PGLVKNISEQ AFGKSITTVS AAGAGYKSLE VARRHVDAYL HVTEIKKWDI CAGNAIIKAL
     GGKMTTLSNE VLDYSSEDIV NKKGLLTTME NHELYLEKLK PFKL
//
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