ID   M7BVE1_CHEMY            Unreviewed;       959 AA.
AC   M7BVE1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE            EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN   ORFNames=UY3_10772 {ECO:0000313|EMBL:EMP32097.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP32097.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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; KB542241; EMP32097.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7BVE1; -.
DR   STRING; 8469.M7BVE1; -.
DR   eggNOG; KOG0565; Eukaryota.
DR   Proteomes; UP000031443; 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; 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   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:UP000031443}.
FT   DOMAIN          742..954
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          186..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   959 AA;  109709 MW;  0EC364F81944D7CD CRC64;
     MAGGCRLMAP WLGRPALSPG AAPVPRASEE KYSHEVSNTF ALESFSFCAV MRLLSVSRLV
     IRSREKDPPD QDNIPINSRF RCVQEAEETL LIDIATNTGC KIRIQGDCTP ERLFEIPDEE
     RCLRFLTKVL NVQEAQLKAP LPEHREPASW YQVEKNLPAP PQSSVSGVLG FEDHFNAISL
     EKKRNLQNQQ MGSRREPPPP PLPPQNRQFH REREGVARDQ PKVTNTMRKL FVPNTHSGQR
     EGLIKHILAK REKEYVNIQS FRFFVGTWNV NGQSPDSGLE PWLVCDSEPP DVYCVGFQEL
     DLSTEAFFYL DSAKEHEWLA AVEKALHPKA KYKKVQVVRL VGMMLVVFAR KDQLSYITDI
     MAETVGTGIM GKMGNKGGVA VRFVFHNTTF CIVNSHLAAH VEDFERRNQD YKDICARLSF
     LPPDQGLPQL SIMKHDVVIW LGDLNYRLCL PDASEVKTLI SKLELQKLLT YDQLNIQRTH
     KKAFADFTEG EIKFIPTYKF DSKTDRWDSS GKCRVPAWCD RILWRGGNIN QLRYRSHMDL
     KTSDHKPVSS LFLIGVKIVD EQRYRRLFED IVRMMDRMEN DFLPSLELSR REFVFEKVKF
     RQLQKEKFQI TNNGQVTCHF FFIPKLNDSQ YCKPWLRAEP CEGYLEPNET VDISLDVYVS
     KDSVTLLNSG EDRIEDILVL HLDRGKDYFL TISGSYLPSC FGTSLEALCR MRRPIREVPV
     TKLVDLGEDS FLEKEKSLLQ MGPLDSEDAS ERPLKVPKEI WLLVDHLFKC ACHQEDLFQT
     PGMQEELQQI IDCLDTSIPE TIRILPSAEG GARLPAPPME ILLLPSLGQA PSGSNHSVAE
     ALLIFLEALP EPVICYELYQ RCLDCSHDSR LCRQVISHLP RCHHNVFHYL MAFLRELLKY
     SEDNNVSANM IATLFTSLLL RPPPNLMLKQ SPQDRQRAIS FLLGFLLGGD EESPPCPRC
//