ID A0A0Q3M978_AMAAE Unreviewed; 908 AA.
AC A0A0Q3M978;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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};
GN ORFNames=AAES_227639 {ECO:0000313|EMBL:KQK78976.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK78976.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK78976.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK78976.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK78976.1}.
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DR EMBL; LMAW01002620; KQK78976.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3M978; -.
DR Proteomes; UP000051836; 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; 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; 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:UP000051836}.
FT DOMAIN 727..908
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 106..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 103699 MW; 16104FDCFF18F2C9 CRC64;
MRLSCLGHRT QAGSCSSALT SLSPISRILI QSQEKDSSDP DYIPINSRFR CVQEAEETLL
IDIAANTGCK VRIQGEEAAE RLFEIPDEER CLGFLAEVQS IQEAHLKASP MEPKDSSSWH
QVEKNLPGLS QASSSGALGF EDDFTALSIE EKRNGQNNQA GSRREPPPPP VPQNRQFLRE
REGSSRDQPK VTNTMRKMFL PSSQSGQREG LIKHLLAKRE KAYVNLHNFR FFVGTWNVNG
QSPDSSLEPW LVCDSEPPDV YCIGFQELDL STEAFFYFDS VKEQEWLTAV EKALHPHAKY
KKVQMVRLVG MMLLIFAKKD QLSNIREIVT ESVGTGVMGK MGNKGGVAVR FVFHXTTFCI
VNSHLAAHVE DFERRNQDYK DICARMSFVT PDESLPHVNI MKHDVVIWLG DLNYRLCLPD
ASEVKSLISK NELQKLLTYD QLNIXRTQKK AFADFTEGEI KFIPTYKYDS KTDRWDSSGK
CRVPAWCDRI LWRGGNITQL RYGSHMDLKT SDHKPVSALF RIGVKVVDEQ KYRKLFEDIV
RLMDRMENDF LPSLELSRRE FEFQNVKFRQ LQKQKFQITN NGQVTCHFSF IPKLNDNHYC
KPWLRAEPCE GYLEPDESTD ISLDVYVSKD SVTLLNSGED KIEDILVLHL DRGKDYFLTI
SGTYLPSCFG TSLEALCRMR RPIREVPVTK LIDLAQRTEG LVLYQSSGFA ITRSGEGAQE
KSVLQMGALD SEEASGTPLQ VPKEMWLLVD HLFKHACHQE DLFQTPGMQE ELEQIIDCLD
TSIPETIPGS NHSVAEALLI FLEALPEPVI CXELYQRCLD WSHSSRLCRQ VIFQLPRCHR
SVFRYLMSFL RELLRYSEDN KVSVTMIAAL FSSLLLRPPP NLVTKQSQQD RQRAINFLYS
FLLAGDEE
//
