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Database: UniProt
Entry: A0A3P9P6X7_POERE
LinkDB: A0A3P9P6X7_POERE
Original site: A0A3P9P6X7_POERE 
ID   A0A3P9P6X7_POERE        Unreviewed;       874 AA.
AC   A0A3P9P6X7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE            EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000017549.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000017549.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000017549.1};
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}.
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DR   AlphaFoldDB; A0A3P9P6X7; -.
DR   STRING; 8081.ENSPREP00000017549; -.
DR   Ensembl; ENSPRET00000017735.1; ENSPREP00000017549.1; ENSPREG00000011774.1.
DR   GeneTree; ENSGT00940000157996; -.
DR   OMA; NVNNKPC; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000011774; Expressed in caudal fin and 1 other cell type or tissue.
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:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR   GO; GO:0003341; P:cilium movement; IEA:Ensembl.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR   GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR   GO; GO:0032402; P:melanosome transport; IEA:Ensembl.
DR   GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR   GO; GO:0048884; P:neuromast development; IEA:Ensembl.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:Ensembl.
DR   GO; GO:0035776; P:pronephric proximal tubule development; IEA:Ensembl.
DR   GO; GO:0001919; P:regulation of receptor recycling; IEA:Ensembl.
DR   GO; GO:0048259; P:regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR   GO; GO:0097205; P:renal filtration; IEA:Ensembl.
DR   GO; GO:0071871; P:response to epinephrine; IEA:Ensembl.
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:UP000242638}.
FT   DOMAIN          685..874
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..171
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   874 AA;  100090 MW;  6944AB0C8FA48D35 CRC64;
     RMESTLGISN EESAHTVKGQ ELRSGQKEPR LLSLIERNGE FILGVLATPD AVVSRPVAQL
     SIPVNQKFEI IREAEEALLI NFSDDSSFTI RIRGEKPPEL MLELQDDERT QTFLTQVKSA
     QEQGEGLKNP VKVEEKKNQQ NRIVASREPP PVPTLPPRKA SFPPTNPLPP SYRPTDYTDR
     PTSWCDSPTT NSMRQAMLSS EAGQREYLIK HRLGKKEKEY VDIQPFSFFI GTWNVNGQSP
     DSSLEPWLCC DPDPPDIYAV GFQELDLSTE AFFYLDSSKE QVWVEAVERS LNRKGDYKRI
     RVIRLVGMML VVFVKKKHKK HIKELAAEHV GTGIMGKMGN KGGVAIRFVF HNTSFCIVNC
     HLAAHAEDFE RRNQDYRDIC ARMTFHLLDY PPLSIVKHDV VIWLGDLNYR LFLYEAAEVK
     RLIAENALKK LQENDQLNIQ RQTKKAFVDF IEGDINFVPT YKYDTKTDRW DSSGKCRIPA
     WCDRILWRGS NVQQLKYRSH MEMKTSDHKP VSSLFKIGVK VVDEQRQKRV FEDIVRAMDR
     MENDCLPSVS LSRIDFTFKD VKFRQLQKER FLIKNDGQVP CHFAFIPKPN DPNYCKPWLR
     AEPSDGFLEP SETLEIYLEV YVSKDSVTLL NSGQDSIYDI LVLHLDRGKD YFITISGNYL
     SSCFGTSLET LCRIRKPVRE VANLIDLSMV NLMFADGGSS DDVPLKIPKE VWILVNHLFT
     KSCDQEDLFQ TPGLQEELQS IIDCLDTSIP ESLPGCNHSV AEALLIFLEA LPEPVVCYEL
     YQRCLDSSHD SRLCKQLVSQ LSRPHRNVFR YLMSFLKELL KHSNNNNLTA NLIATLFASL
     LIRPPPNMVS RQSGQDRQKA INFILGFLMS ADDD
//
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