ID   L5JZA8_PTEAL            Unreviewed;       527 AA.
AC   L5JZA8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Inositol polyphosphate 1-phosphatase {ECO:0000313|EMBL:ELK04789.1};
GN   ORFNames=PAL_GLEAN10026067 {ECO:0000313|EMBL:ELK04789.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK04789.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759}.
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DR   EMBL; KB031068; ELK04789.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5JZA8; -.
DR   STRING; 9402.L5JZA8; -.
DR   eggNOG; KOG3099; Eukaryota.
DR   InParanoid; L5JZA8; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd01640; IPPase; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   Gene3D; 4.10.460.10; Inositol Polyphosphate 1-phosphatase, domain 1; 1.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   InterPro; IPR044897; INPP1_dom_1.
DR   PANTHER; PTHR43028; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1.
DR   PANTHER; PTHR43028:SF3; INOSITOL POLYPHOSPHATE 1-PHOSPHATASE; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552}.
FT   REGION          58..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  57715 MW;  D821737F97FAB6F9 CRC64;
     MEEDFKSEFV SSYKNKTSGL GDPGALFFLA LPFESSNSTC DVADASLLQA WDTLARPGSL
     EASPHGSAPR SLEGPRGGGL ANAEVGARAE RGSPQPSFAF AFASVDSRGW VPIPFTAATE
     KQGSEMSDIL RELLRVSEKA ASIARACRQQ EALFQLLIEE KKEGEKNKKF AVDFKTLADV
     LVQEVIKQNM ENKFPGLAKK IFGEESNEFT NELGEKVILR LCPTEEETVE LLSKVLNGNK
     VASEALAKVV HQDVAFTDPT LDSIDITIPQ DILGIWVDPI DSTYQYIKGS ADVKSNQGIF
     PSGLQCVTIL IGVYDIQTGV PLMGVINQPF VSQDLNTLRW KGQCYWGLSY METNIYSHQP
     SVSKRNGSEP WSQLTKNTSS EVEFSHQFSA VISTSEKENI KAALSRVCGD RIFRAAGAGY
     KSLCVVQGLV DVYIFSEDTT FRWDSCAAHA ILRAMGGGMV DLKECLERNP ETGLDLPQLV
     YHVENEGASG VDRWANKGGL IAYRSSKQLE TFLSLLIQNL APTDAHR
//