ID   A0A3Q1EX59_9TELE        Unreviewed;       921 AA.
AC   A0A3Q1EX59;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE            EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000009806.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000009806.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane
CC       {ECO:0000256|ARBA:ARBA00004580}. Early endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004146}. Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004608}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
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; A0A3Q1EX59; -.
DR   Ensembl; ENSAPOT00000000935.1; ENSAPOP00000009806.1; ENSAPOG00000012272.1.
DR   GeneTree; ENSGT00940000157996; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052745; F:inositol phosphate phosphatase activity; IEA:InterPro.
DR   GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd09093; INPP5c_INPP5B; 1.
DR   CDD; cd04380; RhoGAP_OCRL1; 1.
DR   Gene3D; 2.30.29.110; -; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR046985; IP5.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR048869; OCRL-1_2_ASH.
DR   InterPro; IPR037793; OCRL1/INPP5B_INPP5c.
DR   InterPro; IPR031995; OCRL_clath-bd.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR047078; RhoGAP_OCRL1.
DR   PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR   PANTHER; PTHR11200:SF176; INOSITOL POLYPHOSPHATE 5-PHOSPHATASE OCRL; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF21310; OCRL-like_ASH; 1.
DR   Pfam; PF16726; OCRL_clath_bd; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT   DOMAIN          730..921
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          111..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   921 AA;  105391 MW;  478A6AB116101D46 CRC64;
     RMEPSLGICG QELRSGQKEP RLLSLIERSG EFILGVLATP DAVVSRPVAQ LSIPINGNFE
     ILREAEEALL IDFSVDSCVR IRIKGEKVPE LLLELQDDDR TQTFFAQVKS AQQQVKSKPT
     KPKAMEPLAP SAQRGPVPIP PQRLFSISSV LNNLNPVSKD PVQSLASDFG FEENFNHALK
     VEEKKNHQNL PPLPPHRAVS LQPKDNSLIT NTNFRSGFDR LDRPPSWCDS PTTNSMRQAM
     FSSQAGQREY LIKHRLGKKE NEYVDIRPFK FFTGTWNVNG QPPDSSLESW LGCDPEPPDI
     YALGFQELDL STEAFFYMDS SKEQLWVEAV ERSLHSKAKY KKVRIIRLVG MMLVVFVKKI
     HKSHIKEVAA EHVGTGIMGK MGNKGGVAVR FVFHNTSFCI VNSHLAAHVE DFERRNQDYK
     DICARMTFHL LDHPPLSIVK HDVVIWLGDL NYRLFINEAS EVKQLIAQNE LKKLQEYDQL
     NIQRQTKRAF TDFMEGDINF IPTYKYDPKT DRWDSSGKCR VPAWCDRILW RGNNVQQLKY
     RSHMELKTSD HKPVSSLFDI GVKVVDEQRH KKVFEEIVRA MDRMENDFLP SVSLSRREFT
     FENVKFRQLQ KERFLIKNDG QVPCHFAFIP KLSDSQYCKP WLRAEPSDGF LEPNETLEIY
     LEVYVSKDSV TLLNSGEDSI EDILVLHLDR GKDYFITISG KYMPSCFGTS LETLCRMKKP
     IREIPITKLI DLEKSKVSFL MVDGASTEDK PLKIPKEVWI LVNHLFTKSC DQEDLFQTPG
     LQEELQSIID CLDTSIPESI PGCNHSVAEA LLIFLEALPE PVVCYELYQR CLDSSHDSRL
     CKQLISQLPR AHRNVFRYLM AFLKELLKHS HNNNLTASLI ATLFASLLIR PPPNLVSRQT
     SHDRQKAIDF VLGFLMAGDE D
//