ID H2PWQ4_PONAB Unreviewed; 867 AA.
AC H2PWQ4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN Name=OCRL {ECO:0000313|Ensembl:ENSPPYP00000023176.3};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000023176.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000023176.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000023176.3}
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; H2PWQ4; -.
DR Ensembl; ENSPPYT00000024147.3; ENSPPYP00000023176.3; ENSPPYG00000020704.3.
DR eggNOG; KOG0565; Eukaryota.
DR GeneTree; ENSGT00940000157996; -.
DR HOGENOM; CLU_006779_3_1_1; -.
DR InParanoid; H2PWQ4; -.
DR TreeFam; TF317034; -.
DR Proteomes; UP000001595; Chromosome X.
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; cd13382; PH_OCRL1; 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; IPR046985; IP5.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR048869; OCRL-1_2_ASH.
DR InterPro; IPR037793; OCRL1/INPP5B_INPP5c.
DR InterPro; IPR037787; OCRL1_PH.
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; 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 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:UP000001595}.
FT DOMAIN 721..867
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 162..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 99572 MW; BF41AD8C5591F3AA CRC64;
MEPPLPVGAQ PLATVEGMEM KGPLREPCAL TLAQRNGQYE LIIQLHEKEQ HVQDIIPINS
HFRCVQEAEE TLLIDIASNS GCKIRVQGDW IRERRFEIPD EEHCLKFLSA VLAAQKAQSQ
LLVPEQKDSS SWYQKLDTKD KPSVFSGLLG FEDNFSSMNL DKKINSQNQP TGIHREPPPP
PSSVNKMLPR EKEASNKEQP KVTNTMRKLF VPNTQSGQRE GLIKHILAKR EKEYVNIQTF
RFFVGTWNVN GQSPDSGLEP WLNCDPNPPD IYCIGFQELD LSTEAFFYFE SVKEQEWSMA
VERGLHSKAK YKKVQLVRLV GMMLLIFARK DQCRYIRDIA TETVGTGIMG KMGNKGGVAV
RFVFHNTTFC IVNSHLAAHV EDFERRNQDY KDICARMSFV VPNQTLPQLN IMKHDVVIWL
GDLNYRLCMP DANEVKSLIN KKDLQRLLKF DQLNIQRTQK KAFVDFNEGE IKFIPTYKYD
SKTDRWDSSG KCRVPAWCDR ILWRGTNVNQ LNYRSHMELK TSDHKPVSAL FHIGVKVVDE
RRYRKVFEDS VRIMDRMEND FLPSLELSRR EFVFENVKFR QLQKEKFQIS NNGQVPCHFS
FIPKLNDSQY CKPWLRAEPF EGYLEPNETV DISLDVYVSK DSVTILNSGE DKIEDILVLH
LDRGKDYFLT ISGNYLPSCF GTSLEALCRM KRPIREVPVT KLIDLEEDSF LEKEKSLLQM
VPLDEGASER PLQVPKEIWL LVDHLFKYAC HQDDLFQTPG MQEELQQIID CLDTSIPETI
PGSNHSVAEA LLIFLEALPE PVICYELYQR CLDSAHDPRI CRQASVLQLL TRLGSKGLIL
TVHVGGSTVE HGVLRHVHGP STLVKAI
//
