INP5E_DROME
ID INP5E_DROME Reviewed; 747 AA.
AC Q9VTW2;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Inositol polyphosphate 5-phosphatase E {ECO:0000303|PubMed:26723017};
DE EC=3.1.3.36 {ECO:0000305|PubMed:26723017};
DE AltName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase {ECO:0000305|PubMed:26723017};
DE AltName: Full=Phosphatidylinositol polyphosphate 5-phosphatase type IV {ECO:0000305};
GN Name=INPP5E {ECO:0000303|PubMed:26723017, ECO:0000312|FlyBase:FBgn0036273};
GN ORFNames=CG10426 {ECO:0000312|FlyBase:FBgn0036273};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM49972.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM49972.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26723017; DOI=10.1016/j.celrep.2015.12.009;
RA Park J., Lee N., Kavoussi A., Seo J.T., Kim C.H., Moon S.J.;
RT "Ciliary phosphoinositide regulates ciliary protein trafficking in
RT Drosophila.";
RL Cell Rep. 13:2808-2816(2015).
CC -!- FUNCTION: Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns
CC 3,4,5-P3) to PtdIns-P2, and phosphatidylinositol 4,5-bisphosphate
CC (PtdIns 4,5-P2) to phosphatidylinositol 4-phosphate (PI-4-P). By
CC controlling the phosphoinositide composition of the cilia membrane of
CC auditory receptor neurons, regulates the cilia localization of ktub and
CC consequently the transient receptor potential channels iav and nompC.
CC {ECO:0000269|PubMed:26723017}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000305|PubMed:26723017};
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:26723017}. Note=Localized to the transition zone,
CC which marks the boundary between the plasma membrane and the ciliary
CC membrane. {ECO:0000269|PubMed:26723017}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile, however flies display a
CC decrease in extracellular sound-evoked potentials. This hearing defect
CC is likely due to the increased levels of phosphatidylinositol 4,5-
CC bisphosphate (PtdIns 4,5-P2) in the ciliary base that results in the
CC abnormal localization of membrane proteins such as ktub, iav and nompC.
CC Expression of ktub in the cilia is decreased and displays abnormal
CC accumulation inside chordotonal cilia, iav is enriched in the ciliary
CC base, and nompC which is typically found in the distal cilia, is
CC slightly mislocalized towards the proximal cilia and its expression is
CC decreased. However there is no effect on the localization of eys.
CC {ECO:0000269|PubMed:26723017}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type IV family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014296; AAF49933.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94446.1; -; Genomic_DNA.
DR EMBL; AY118603; AAM49972.1; -; mRNA.
DR RefSeq; NP_001261753.1; NM_001274824.1.
DR RefSeq; NP_648566.1; NM_140309.2.
DR AlphaFoldDB; Q9VTW2; -.
DR SMR; Q9VTW2; -.
DR IntAct; Q9VTW2; 2.
DR STRING; 7227.FBpp0075739; -.
DR PaxDb; Q9VTW2; -.
DR PRIDE; Q9VTW2; -.
DR DNASU; 39404; -.
DR EnsemblMetazoa; FBtr0076007; FBpp0075739; FBgn0036273.
DR EnsemblMetazoa; FBtr0333356; FBpp0305548; FBgn0036273.
DR GeneID; 39404; -.
DR KEGG; dme:Dmel_CG10426; -.
DR UCSC; CG10426-RA; d. melanogaster.
DR CTD; 56623; -.
DR FlyBase; FBgn0036273; INPP5E.
DR VEuPathDB; VectorBase:FBgn0036273; -.
DR eggNOG; KOG0565; Eukaryota.
DR GeneTree; ENSGT00940000158199; -.
DR HOGENOM; CLU_011711_5_4_1; -.
DR InParanoid; Q9VTW2; -.
DR OMA; DIYLEGM; -.
DR OrthoDB; 1399831at2759; -.
DR PhylomeDB; Q9VTW2; -.
DR BioGRID-ORCS; 39404; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39404; -.
DR PRO; PR:Q9VTW2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036273; Expressed in testis and 16 other tissues.
DR GO; GO:0097546; C:ciliary base; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0016020; C:membrane; ISS:FlyBase.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; ISS:FlyBase.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:FlyBase.
DR GO; GO:0061512; P:protein localization to cilium; IMP:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Cell projection; Hydrolase; Lipid metabolism; Reference proteome.
FT CHAIN 1..747
FT /note="Inositol polyphosphate 5-phosphatase E"
FT /id="PRO_0000442517"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 82590 MW; 4A9B7BE5373C8B1E CRC64;
MQHSSAGSEE RITSSTSSPR SGHKTASSLF GLLSKRPSKV EPHPVTPESP RLQQRPVSAC
GQYDVSFAKC NADTSANHVN NNGSTLKSQT LPLEKSHSGL ISFHRRAKPS SSKGKNHSHR
HSTDAGSQSD GGADVVMRRK SPKHRSPNHN RFSHQFSLCC KAEKKPMTPP VTVRYNSIPD
SNSVLRRDNL SLSWSMVDNN SGSLHSSEGS SHRPRPSSEC ASAPESPVAS KTFFAHCSPA
AASASVARSE SLQNRSPIRP MAVSACRSRL RLKLYPPGQE LPPLQAATEP GDIKRATTPQ
HMSSPNIATQ PDGIEHIEEQ PGVRFMSHEN MTLQRQGSGS NLARQTLMAA HALNLIPADN
ARERSYLDGR LGSTSLLGPS ELSRVLPQKE ITVFVGTWNM NGHSPPKQLN DFVLPANVEH
VPDIVVMGTQ ESTPDRFEWE VTIQETLGPS HVLFHATTLG TLHLAVYMRR DLIWYCSVPE
DASMSVRTGS AFRTKGAVAI SFCLFGTSML FVTSHLTAHQ QKVKERVSDV KRIINALDLP
RNLPNQRHKN KDVTQNFDNV FWCGDLNFRL GEPREKLLEW IQNTKFPLPS HLPHGYMHTD
QLTSVLADGA AFRGFMEANI TFPPTYKYDP GSQNFDTSSK QRAPAYTDRI LYKYRQMQGL
VIRRQTLVPG VSTPTQPHVQ CLLYDSVPSI TTSDHKPVWA LFRTLIRAGT DAIPLAAGLF
SRDIYLEGMR RRLNNQYSGA SAVCVLQ
