ID A0A091DGM4_FUKDA Unreviewed; 887 AA.
AC A0A091DGM4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN ORFNames=H920_16661 {ECO:0000313|EMBL:KFO21956.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO21956.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO21956.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO21956.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KN124226; KFO21956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DGM4; -.
DR STRING; 885580.ENSFDAP00000021487; -.
DR eggNOG; KOG0565; Eukaryota.
DR OrthoDB; 21647at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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:UP000028990}.
FT DOMAIN 702..884
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 143..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 102974 MW; 3AD220B0B8A083B4 CRC64;
MKGPLREPCA LTLAQRNGQY ELIIQLQKKE RHSQDIIPIN SHFRCVQEAE ETLLIDIASN
SGCKIRVQGD WSRERRFEIP DEEHCLKFLS EVLAAQEAQS QHLVPEQKDS SSWYQKLDTK
DKPSVFSGLL GFEDNFSSMN LDKKINSQNQ PTGIHREPPP PPPSVNRMLP REKETSNKEQ
PKVTNTMRKL FVPNTQSGTR EGLIKHILAK REKEYVNIQN FKFFVGTWNV NGQSPDSGLE
PWLNCDPNPP DIYCIGFQEL DLSTEAFFYF ESVKEQEWSM AVEKGLHSKA KYKKVQLVRL
VGMMLLIFAR KDQYRYIRDV ATETVGTGIM GKMGNKGGVA VRFVFHNTTF CIVNSHLAAH
VEDFERRNQD YKDICARMSF VVPRQPLPQL NIMKHDVVIW LGDLNYRLCM PDANEVKSLI
NKNDLQRLLK FDQLNIQRTQ KRAFVDFNEG EIKFIPTYKY DSKTDRWDSS GKCRVPAWCD
RILWRGTNVD QLHYRSHMEL KTSDHKPVSS LFHIGVKVVD ERRYRKVFED IVRIMDRMEN
DFLPSLELSR REFVFENVKF RQLQKEKFQI SNNGQVPCHF SFIPKLNDSQ YCKPWLRAEP
FEGYLEPNET VDISLDVYVS KDSVTILNSG EDKIEDILVL HLDRGKDYFL TISGNYLPSC
FGTSLEALCR MKRPIREVPV TKLIDLEEDS FLEKENSLLQ MVPLDEGASE RPLQVPKEIW
LLVDHLFRYA CHQEDLFQTP GMQEELQQII DCLDTSIPET IPGSNHSVAE ALLIFLEALP
EPVICYELYQ RCLDSAHDPW ICRQVISQLP RCHRNVFRYL MAFLRELLKF SEYNNVSANM
IATLFTSLLL RPPPNLMARQ TSSDRQRAIQ FLLGFLLGSD EDKSFPL
//
