PP4P1_RAT
ID PP4P1_RAT Reviewed; 284 AA.
AC Q5PPM8;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase;
DE Short=Type 1 PtdIns-4,5-P2 4-Ptase;
DE EC=3.1.3.78 {ECO:0000250|UniProtKB:Q86T03};
DE AltName: Full=PtdIns-4,5-P2 4-Ptase I;
DE AltName: Full=Transmembrane protein 55B;
GN Name=Pip4p1 {ECO:0000250|UniProtKB:Q86T03}; Synonyms=Tmem55b;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, 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: Catalyzes the hydrolysis of phosphatidylinositol-4,5-
CC bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate
CC (PtdIns-4-P) (By similarity). Does not hydrolyze phosphatidylinositol
CC 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol
CC 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-
CC monophosphate, phosphatidylinositol 4-monophosphate and
CC phosphatidylinositol 3-monophosphate (By similarity). Regulates
CC lysosomal positioning by recruiting JIP4 to lysosomal membranes, thus
CC inducing retrograde transport of lysosomes along microtubules (By
CC similarity). Contributes to assembly of the V-ATPase complex in lipid
CC rafts of the lysosomal membrane and to subsequent amino acid-dependent
CC activation of mTORC1 (By similarity). May play a role in the regulation
CC of cellular cholesterol metabolism (By similarity).
CC {ECO:0000250|UniProtKB:Q86T03}.
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-5-phosphate) + phosphate; Xref=Rhea:RHEA:25674,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795,
CC ChEBI:CHEBI:58456; EC=3.1.3.78;
CC Evidence={ECO:0000250|UniProtKB:Q86T03};
CC -!- SUBUNIT: Interacts (via transmembrane domain) with ATP6V0D1 (By
CC similarity). Interacts with LAMTOR1, RRAGA and RRAGC (By similarity).
CC {ECO:0000250|UniProtKB:Q3TWL2}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q3TWL2}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q3TWL2}; Multi-
CC pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000250|UniProtKB:Q3TWL2}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TWL2}; Multi-pass
CC membrane protein {ECO:0000255}.
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DR EMBL; BC087604; AAH87604.1; -; mRNA.
DR RefSeq; NP_001014255.1; NM_001014233.2.
DR AlphaFoldDB; Q5PPM8; -.
DR SMR; Q5PPM8; -.
DR STRING; 10116.ENSRNOP00000013225; -.
DR iPTMnet; Q5PPM8; -.
DR PhosphoSitePlus; Q5PPM8; -.
DR SwissPalm; Q5PPM8; -.
DR PaxDb; Q5PPM8; -.
DR PRIDE; Q5PPM8; -.
DR Ensembl; ENSRNOT00000013225; ENSRNOP00000013225; ENSRNOG00000009948.
DR GeneID; 364298; -.
DR KEGG; rno:364298; -.
DR UCSC; RGD:1307475; rat.
DR CTD; 90809; -.
DR RGD; 1307475; Pip4p1.
DR eggNOG; KOG4684; Eukaryota.
DR GeneTree; ENSGT00390000003680; -.
DR HOGENOM; CLU_087485_0_0_1; -.
DR InParanoid; Q5PPM8; -.
DR OMA; APYGVPN; -.
DR OrthoDB; 1346704at2759; -.
DR PhylomeDB; Q5PPM8; -.
DR TreeFam; TF316367; -.
DR Reactome; R-RNO-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-RNO-8847453; Synthesis of PIPs in the nucleus.
DR PRO; PR:Q5PPM8; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000009948; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q5PPM8; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0034597; F:phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISO:RGD.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; ISS:UniProtKB.
DR GO; GO:0070070; P:proton-transporting V-type ATPase complex assembly; ISS:UniProtKB.
DR GO; GO:0006991; P:response to sterol depletion; ISS:UniProtKB.
DR InterPro; IPR019178; PtdIns-P2-Ptase.
DR PANTHER; PTHR21014; PTHR21014; 1.
DR Pfam; PF09788; Tmemb_55A; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Endosome; Hydrolase; Lipid metabolism;
KW Lysosome; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..284
FT /note="Type 1 phosphatidylinositol 4,5-bisphosphate 4-
FT phosphatase"
FT /id="PRO_0000072580"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 140..146
FT /note="CX5R motif"
FT COMPBIAS 46..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /evidence="ECO:0000250"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 284 AA; 29993 MW; 6F9A2E2645A5908B CRC64;
MAADGERSPL LSEAGDGGAG GNGLAGPGGS ATGPGGGLTP SAPPYGAGKH APPQAFPPFP
EGHPAVLPGE DPPPYSPLTS PDSGSAPMIT CRVCQSPINV EGKMHQHVVK CGVCNEATPI
KNAPPGKKYV RCPCNCLLIC KVTSQRIACP RPYCKRIINL GPVHPGPLSP EPQPMGVRVI
CGHCKNTFLW TEFTDRTLAR CPHCRKVSSI GRRYPRKRCI CCFLLGLLLA VTATGLAFGT
WKPAQQYGGI YAAWAFVILL AVLCLGRALY WGCMKVSHPV QNFS
