INP5E_RAT
ID INP5E_RAT Reviewed; 648 AA.
AC Q9WVR1; A0A0G2K6T4;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phosphatidylinositol polyphosphate 5-phosphatase type IV;
DE AltName: Full=5-phosphatase that induces arborization {ECO:0000303|PubMed:10405344};
DE Short=Pharbin {ECO:0000303|PubMed:10405344};
DE AltName: Full=72 kDa inositol polyphosphate 5-phosphatase;
DE AltName: Full=Inositol polyphosphate-5-phosphatase E;
DE AltName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase;
DE EC=3.1.3.36 {ECO:0000269|PubMed:10405344};
DE AltName: Full=Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase;
DE EC=3.1.3.86 {ECO:0000250|UniProtKB:Q9NRR6};
DE Flags: Precursor;
GN Name=Inpp5e;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Brain;
RX PubMed=10405344; DOI=10.1006/bbrc.1999.0998;
RA Asano T., Mochizuki Y., Matsumoto K., Takenawa T., Endo T.;
RT "Pharbin, a novel inositol polyphosphate 5-phosphatase, induces dendritic
RT appearances in fibroblasts.";
RL Biochem. Biophys. Res. Commun. 261:188-195(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically
CC hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate
CC (PtdIns(3,4,5)P3), phosphatidylinositol 4,5-bisphosphate PtdIns (4,5)P2
CC and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Specific for
CC lipid substrates, inactive towards water soluble inositol phosphates
CC (By similarity) (PubMed:10405344). Plays an essential role in the
CC primary cilium by controlling ciliary growth and phosphoinositide 3-
CC kinase (PI3K) signaling and stability (By similarity).
CC {ECO:0000250|UniProtKB:Q9JII1, ECO:0000250|UniProtKB:Q9NRR6,
CC ECO:0000269|PubMed:10405344}.
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:0000269|PubMed:10405344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22765;
CC Evidence={ECO:0000305|PubMed:10405344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:57836; EC=3.1.3.86;
CC Evidence={ECO:0000250|UniProtKB:Q9NRR6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25529;
CC Evidence={ECO:0000250|UniProtKB:Q9NRR6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3-phosphate) + phosphate; Xref=Rhea:RHEA:32955,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57923,
CC ChEBI:CHEBI:58088; Evidence={ECO:0000250|UniProtKB:Q9JII1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32956;
CC Evidence={ECO:0000250|UniProtKB:Q9JII1};
CC -!- SUBUNIT: Interacts (when prenylated) with PDE6D; this is important for
CC normal location in cilia. {ECO:0000250|UniProtKB:Q9NRR6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q9JII1}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:Q9JII1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9JII1}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9JII1}. Cell membrane
CC {ECO:0000269|PubMed:10405344}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10405344}; Cytoplasmic side
CC {ECO:0000269|PubMed:10405344}. Cell projection, ruffle
CC {ECO:0000269|PubMed:10405344}. Cytoplasm {ECO:0000269|PubMed:10405344}.
CC Nucleus {ECO:0000250|UniProtKB:Q9JII1}. Note=Peripheral membrane
CC protein associated with Golgi stacks. {ECO:0000250|UniProtKB:Q9JII1}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type IV family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA82150.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA82150.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB026288; BAA82150.1; ALT_SEQ; mRNA.
DR EMBL; AC129824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474001; EDL93496.1; -; Genomic_DNA.
DR EMBL; CH474001; EDL93498.1; -; Genomic_DNA.
DR RefSeq; NP_446084.1; NM_053632.1.
DR RefSeq; XP_006233729.1; XM_006233667.3.
DR AlphaFoldDB; Q9WVR1; -.
DR SMR; Q9WVR1; -.
DR STRING; 10116.ENSRNOP00000025763; -.
DR iPTMnet; Q9WVR1; -.
DR PhosphoSitePlus; Q9WVR1; -.
DR PaxDb; Q9WVR1; -.
DR PRIDE; Q9WVR1; -.
DR Ensembl; ENSRNOT00000079882; ENSRNOP00000073935; ENSRNOG00000019039.
DR GeneID; 114089; -.
DR KEGG; rno:114089; -.
DR UCSC; RGD:620478; rat.
DR CTD; 56623; -.
DR RGD; 620478; Inpp5e.
DR eggNOG; KOG0565; Eukaryota.
DR GeneTree; ENSGT00940000158199; -.
DR InParanoid; Q9WVR1; -.
DR OMA; HADYKLR; -.
DR OrthoDB; 885595at2759; -.
DR Reactome; R-RNO-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-RNO-5624958; ARL13B-mediated ciliary trafficking of INPP5E.
DR PRO; PR:Q9WVR1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000019039; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q9WVR1; baseline and differential.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0001726; C:ruffle; IDA:RGD.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IDA:RGD.
DR GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IDA:RGD.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:RHEA.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; ISO:RGD.
DR GO; GO:0106019; F:phosphatidylinositol-4,5-bisphosphate phosphatase activity; IDA:RGD.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; ISO:RGD.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IDA:RGD.
DR GO; GO:1903565; P:negative regulation of protein localization to cilium; ISO:RGD.
DR GO; GO:0017148; P:negative regulation of translation; IDA:RGD.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISO:RGD.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:RGD.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR042478; INPP5E.
DR InterPro; IPR000300; IPPc.
DR PANTHER; PTHR46625; PTHR46625; 1.
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 membrane; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Hydrolase; Lipid metabolism; Lipoprotein; Membrane;
KW Methylation; Nucleus; Phosphoprotein; Prenylation; Reference proteome;
KW Repeat.
FT CHAIN 1..645
FT /note="Phosphatidylinositol polyphosphate 5-phosphatase
FT type IV"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR6"
FT /id="PRO_0000209749"
FT PROPEP 646..648
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR6"
FT /id="PRO_0000431691"
FT REPEAT 59..62
FT /note="1"
FT REPEAT 76..79
FT /note="2"
FT REPEAT 147..150
FT /note="3"
FT REPEAT 240..243
FT /note="4"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..243
FT /note="4 X 4 AA repeats of P-X-X-P"
FT REGION 99..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR6"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JII1"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JII1"
FT MOD_RES 645
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR6"
FT LIPID 645
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR6"
SQ SEQUENCE 648 AA; 72040 MW; 4EA46F84628783EE CRC64;
MPSKSACLRH TEAPGQLEGR MLQGQLSNPE KKLIPTSASL PAADSQSSQT NSMPPLSMPA
KPSNQNLQAK ANLITPQPPI RPKLERTLSL DDKGWRRRRF RGSQEDLTVQ NGASPCRGSL
QDSVAQSPAY SRPLPCLSTS LQEIPKPRRA TGSEGGSPSL WSDCLSGMIS TSLDLLHREA
ASGGPHSRLA SLRATHTPPA MDLNIASSSL RTANKVDPEH TDYKLRMQNR LVRAHSNLGP
SRPRSPLAGD DHSIHSARSS FSLLAPIRTK DIRSRSYLEG SLLASGALLG ADELARYFPD
RNMALFVATW NMQGQKELPA SLDEFLLPTE ADYTQDLYVI GVQEGCSDRR EWETRLQETL
GPQYVLLSSA AHGVLYMSLF IRRDLIWFCS EVEYSTVTTR IVSQIKTKGA LGVSFTFFGT
SFLFITSHFT SGDGKVAERL LDYNRTIQAL ALPRNVPDTN PYRSSAGDVT TRFDEVFWFG
DFNFRLSGGR VAVEAFLKQD PEVDVLALLQ HDQLTREMKK GSIFKGFEEA EIHFLPSYKF
DIGKDTYDST SKQRTPSYTD RVLYKSRHKG DICPMKYSSC PGIKTSDHRP VYGLFRVKVR
PGRDNIPLAA GKFDRELYLI GIKRRISKEI QRQEALKSQS SSAVCTVS
