INP5E_PANTR
ID INP5E_PANTR Reviewed; 644 AA.
AC A0FI79;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phosphatidylinositol polyphosphate 5-phosphatase type IV {ECO:0000305};
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:0000250|UniProtKB:Q9NRR6};
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hampshire D.J., Woods C.G., Riley J.H., Inglehearn C.F.;
RT "The complete CDS of the chimpanzee INPP5E homolog.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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). Plays an essential role in the primary cilium by
CC controlling ciliary growth and phosphoinositide 3-kinase (PI3K)
CC signaling and stability (By similarity). {ECO:0000250|UniProtKB:Q9JII1,
CC ECO:0000250|UniProtKB:Q9NRR6}.
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:0000250|UniProtKB:Q9NRR6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22765;
CC Evidence={ECO:0000250|UniProtKB:Q9NRR6};
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:0000250|UniProtKB:Q9WVR1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9WVR1}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9WVR1}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:Q9WVR1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9WVR1}. Nucleus {ECO:0000250|UniProtKB:Q9JII1}.
CC Note=Peripheral membrane protein associated with Golgi stacks.
CC {ECO:0000250|UniProtKB:Q9JII1}.
CC -!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase family.
CC {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; DQ997811; ABJ97675.1; -; mRNA.
DR RefSeq; NP_001070981.1; NM_001077513.1.
DR AlphaFoldDB; A0FI79; -.
DR SMR; A0FI79; -.
DR GeneID; 748603; -.
DR KEGG; ptr:748603; -.
DR CTD; 56623; -.
DR InParanoid; A0FI79; -.
DR OrthoDB; 885595at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:InterPro.
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; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
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 2: Evidence at transcript 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..641
FT /note="Phosphatidylinositol polyphosphate 5-phosphatase
FT type IV"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR6"
FT /id="PRO_0000285674"
FT PROPEP 642..644
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR6"
FT /id="PRO_0000431690"
FT REPEAT 10..13
FT /note="1"
FT REPEAT 15..18
FT /note="2"
FT REPEAT 28..31
FT /note="3"
FT REPEAT 39..42
FT /note="4"
FT REPEAT 55..58
FT /note="5"
FT REPEAT 69..71
FT /note="6"
FT REPEAT 72..74
FT /note="7"
FT REPEAT 75..78
FT /note="8"
FT REPEAT 121..124
FT /note="9"
FT REPEAT 169..172
FT /note="10"
FT REPEAT 183..185
FT /note="11"
FT REPEAT 190..193
FT /note="12"
FT REPEAT 236..239
FT /note="13"
FT REGION 1..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 10..242
FT /note="13 X 4 AA repeats of P-X-X-P"
FT COMPBIAS 80..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR6"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVR1"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JII1"
FT MOD_RES 641
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR6"
FT LIPID 641
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRR6"
SQ SEQUENCE 644 AA; 70221 MW; 550C54D617898C9A CRC64;
MPSKAENLRP SEPAPQPPEG RTLQGQLPGA PLAQRAGSPP DVPGSESPAL ACSTPATPSG
EDPPARAAPI APRPPARPRL ERALSLDDKG WRRRRFRGSQ EDLEARNGTS PSRGSVQSEG
PGAPAHSCSP PCLSTSLQEI PKSRGVLSSE RGSPSSGGNP LSGVASSSPN LPHRDAAVAG
SSPRLPSLLP PRPPPALSLD IASDSLRTAN KVDSDLADYK LRAQPLLVRA HSSLGPGRPR
SPLACDDCSL RSAKSSFSLL APIRSKDVRS RSYLEGSLLA SGALLGADEL ARYFPDRNVA
LFVATWNMQG QKELPPSLDE FLLPAEADYA QDLYVIGVQE GCSDRREWET RLQETLGPHY
VLLSSAAHGV LYMSLFIRRD LIWFCSEVEC STVTTRIVSQ IKTKGALGIS FTFFGTSFLF
ITSHFTSGDG KVAERLLDYT RTVQALALPR NVPDTNPYRS SAADVTTRFD EVFWFGDFNF
RLSGGRTVVD ALLCQGLVVD VPALLQHDQL IREMRKGSIF KGFQEPDIHF LPSYKFDIGK
DTYDSTSKQR TPSYTDRVLY RSRHKGDICP VSYSSCPGIK TSDHRPVYGL FRVKVRPGRD
NIPLAAGKFD RELYLLGIKR RISKEIQRQQ ALQSQNSSTI CSVS
