ID A0A4W6DHP1_LATCA Unreviewed; 905 AA. AC A0A4W6DHP1; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 29-MAY-2024, entry version 21. DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044}; DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044}; GN Name=INPP5B {ECO:0000313|Ensembl:ENSLCAP00010024461.1}; OS Lates calcarifer (Barramundi) (Holocentrus calcarifer). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Carangaria; Carangaria incertae sedis; Centropomidae; Lates. OX NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010024461.1, ECO:0000313|Proteomes:UP000314980}; RN [1] {ECO:0000313|Proteomes:UP000314980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Sai Rama Sridatta P.; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLCAP00010024461.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A4W6DHP1; -. DR STRING; 8187.ENSLCAP00010024461; -. DR Ensembl; ENSLCAT00010024994.1; ENSLCAP00010024461.1; ENSLCAG00010011442.1. DR GeneTree; ENSGT00940000156762; -. DR InParanoid; A0A4W6DHP1; -. DR Proteomes; UP000314980; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:TreeGrafter. 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; IPR013783; Ig-like_fold. DR InterPro; IPR031896; INPP5B_PH_dom. DR InterPro; IPR046985; IP5. DR InterPro; IPR000300; IPPc. DR InterPro; IPR048869; OCRL-1_2_ASH. DR InterPro; IPR037793; OCRL1/INPP5B_INPP5c. 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:SF163; TYPE II INOSITOL 1,4,5-TRISPHOSPHATE 5-PHOSPHATASE; 1. DR Pfam; PF16776; INPP5B_PH; 1. DR Pfam; PF21310; OCRL-like_ASH; 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:UP000314980}. FT DOMAIN 720..905 FT /note="Rho-GAP" FT /evidence="ECO:0000259|PROSITE:PS50238" FT REGION 167..225 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 167..186 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 187..206 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 905 AA; 103171 MW; E1D61B0C7B4D4434 CRC64; MDQSVAIQET LEREENCIIA VQCDVFFDGI TESRLLGLVE STTEHAIFIY THRRMAITAD DVSLEDIIPI SLDFAVVEVS SPEELAVVGA DTRLRVSYQE DALELRLPFG SHSRLFLSEV NRAWSDVCKS PTQAPKFEWI SKYHKSNRGQ GVVKQALAPL GTKLTKLSQH RKTEKLSDKK GSLEREKGSN NGTQKSKVYS SPESQGFSGR EDRDDLVRSS SHTPSNKAQI LAMPQFGLRD NLIKCELLKN EDLYTYLGNF SCFLGTYNVN GQTPKESLRP WLSCTSDPPD MYCVGFQELD LSKEAFFFND TPKELEWTKA VSEALHPDAK YALVKLVRLV GIMLIFYVKK EHAEFISDVE AETVGTGIMG RMGNKGAVAI RFRFHNSDIC VVNSHLAAHI EEYERRNQDY KDICSRLQFR QLDPTQPPLT IMKHDVVLWI GDLNYRISEL DVDNVKELIS KKDFETLHSY DQLKRQIDEE AVFVGFVEGE IDFQPTYKYD TGSDKWDTSE KCRVPAWCDR ILWRGKNIEQ KHYQSHMTLK TSDHKPVSSL LVIGIKRVNA EAYKKTFEDI VRNIDKMENE CIPSVTLSKR EFHFNNVKFM QHQAETLSLF NDGQVPCQFE FIQKPNEPTY CKPWLTANPP KGFIAQGGSV DIELEVFVNR LTAPELNSGK QQIEDILVLH LERGKDYFIS VTGNYLPSCY GTSIYSLCHL REPVQDMPQE TLRELAEMSG DENAVNAEKP LDIPKELWMM VDHLFRYAIK QEDIFQQPGL RSEFAEIRDC LDTGMPDSLP GSNHSVAEAL LLFLDALPEP VVPYPFYQQC LESCSSASQC EKVISMLPQC HQNVFNYLSA FLRELLKNSA SNRLDVNILA TIFASLLLRS PTKQDLAEKR KTQEFFQHFL TQGSS //