ID   A0A3B3TC58_9TELE        Unreviewed;       582 AA.
AC   A0A3B3TC58;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Inositol polyphosphate-5-phosphatase Jb {ECO:0000313|Ensembl:ENSPKIP00000040857.1};
GN   Name=INPP5J {ECO:0000313|Ensembl:ENSPKIP00000040857.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000040857.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000040857.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC       type II family. {ECO:0000256|ARBA:ARBA00005910}.
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DR   AlphaFoldDB; A0A3B3TC58; -.
DR   STRING; 1676925.ENSPKIP00000040857; -.
DR   Ensembl; ENSPKIT00000021883.1; ENSPKIP00000040857.1; ENSPKIG00000017651.1.
DR   GeneTree; ENSGT00940000156855; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR   CDD; cd09094; INPP5c_INPP5J-like; 1.
DR   Gene3D; 2.60.40.2840; -; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR046985; IP5.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR041611; SKICH.
DR   PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR   PANTHER; PTHR11200:SF127; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 5-PHOSPHATASE A; 1.
DR   Pfam; PF17751; SKICH; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
PE   3: Inferred from homology;
FT   DOMAIN          161..478
FT                   /note="Inositol polyphosphate-related phosphatase"
FT                   /evidence="ECO:0000259|SMART:SM00128"
FT   REGION          1..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   582 AA;  64935 MW;  1FEA4CC0EDFA1F53 CRC64;
     MDVGQPTRRD TEPSGQAGSA PPRTPTTPIA QGGPPTSLTP RAPRRARQSD QPAECQLTPE
     LSRSQPGDAG RMEPDTPRAP QVQSRVQVTT PQSGKPVPQG SGSLGPLGPE GPQQNSSGSR
     SPTSTRAAPV PQPPPSLPED TQFTAHQQRA GTTDIQVQAV EDFVHLVTWN VGSAVPPDDL
     TSLLELNIGD GNTDMYIILQ EVNSMINKRL KDVLFTDQWS EVFMDTLSPF GYVLVTSQRM
     QGVLLLVFAK YYHLPFLRGV QTESTRTGLG GYWQGNKGGV SARMTVFGHP ICFLNCHLPA
     HMENSEQRME DFESILQQQQ FEGQAATGVL DHSVVFWFGD LNFRIEDYDI QVVKSAIDSN
     NLSLLWEKDQ LQLNMAKDSE KVLDGFLEGP LKFPPTYKFD VGTNTYDTGK KRKPAWTDRI
     LWRLRPASQL VAARRGLASG LTSGTRVTQY SYRSHMEYVI SDHKPVSAIF TLQFQFPYKV
     DIPWVTLMVE DEWTKPSDAT AKFKLVPTFS RSSWDWIGLY KVGFKHHKDY VGYVWAKQEE
     TDFLTQEYQV TFAEEDLPKG SGDYILGYYS NNMSTIVGVT EP
//