PP4P1_MOUSE
ID PP4P1_MOUSE Reviewed; 284 AA.
AC Q3TWL2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATP6V0D1; LAMTOR1;
RP RRAGA AND RRAGC.
RX PubMed=29644770; DOI=10.1111/gtc.12583;
RA Hashimoto Y., Shirane M., Nakayama K.I.;
RT "TMEM55B contributes to lysosomal homeostasis and amino acid-induced mTORC1
RT activation.";
RL Genes Cells 23:418-434(2018).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=29378918; DOI=10.1242/jcs.213272;
RA Morioka S., Nigorikawa K., Okada E., Tanaka Y., Kasuu Y., Yamada M.,
RA Kofuji S., Takasuga S., Nakanishi H., Sasaki T., Hazeki K.;
RT "TMEM55a localizes to macrophage phagosomes to downregulate phagocytosis.";
RL J. Cell Sci. 131:0-0(2018).
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 (PubMed:29644770). May play a role in the
CC regulation of cellular cholesterol metabolism (By similarity).
CC {ECO:0000250|UniProtKB:Q86T03, ECO:0000269|PubMed:29644770}.
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
CC (PubMed:29644770). Interacts with LAMTOR1, RRAGA and RRAGC
CC (PubMed:29644770). {ECO:0000269|PubMed:29644770}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:29378918}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:29644770}; Multi-
CC pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000269|PubMed:29378918}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000269|PubMed:29378918}; Multi-pass membrane protein
CC {ECO:0000255}.
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DR EMBL; AK144251; BAE25798.1; -; mRNA.
DR EMBL; AK159641; BAE35254.1; -; mRNA.
DR EMBL; BC106163; AAI06164.1; -; mRNA.
DR CCDS; CCDS27028.1; -.
DR RefSeq; NP_001028443.1; NM_001033271.5.
DR RefSeq; NP_001297434.1; NM_001310505.1.
DR RefSeq; NP_001297435.1; NM_001310506.1.
DR RefSeq; NP_001297436.1; NM_001310507.1.
DR AlphaFoldDB; Q3TWL2; -.
DR SMR; Q3TWL2; -.
DR BioGRID; 230098; 1.
DR STRING; 10090.ENSMUSP00000124782; -.
DR iPTMnet; Q3TWL2; -.
DR PhosphoSitePlus; Q3TWL2; -.
DR SwissPalm; Q3TWL2; -.
DR EPD; Q3TWL2; -.
DR jPOST; Q3TWL2; -.
DR MaxQB; Q3TWL2; -.
DR PaxDb; Q3TWL2; -.
DR PeptideAtlas; Q3TWL2; -.
DR PRIDE; Q3TWL2; -.
DR Antibodypedia; 64010; 55 antibodies from 17 providers.
DR Ensembl; ENSMUST00000160835; ENSMUSP00000124782; ENSMUSG00000035953.
DR GeneID; 219024; -.
DR KEGG; mmu:219024; -.
DR UCSC; uc007tma.1; mouse.
DR CTD; 90809; -.
DR MGI; MGI:2448501; Pip4p1.
DR VEuPathDB; HostDB:ENSMUSG00000035953; -.
DR eggNOG; KOG4684; Eukaryota.
DR GeneTree; ENSGT00390000003680; -.
DR InParanoid; Q3TWL2; -.
DR OMA; APYGVPN; -.
DR OrthoDB; 1346704at2759; -.
DR PhylomeDB; Q3TWL2; -.
DR TreeFam; TF316367; -.
DR Reactome; R-MMU-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-MMU-8847453; Synthesis of PIPs in the nucleus.
DR BioGRID-ORCS; 219024; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q3TWL2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3TWL2; protein.
DR Bgee; ENSMUSG00000035953; Expressed in retinal neural layer and 221 other tissues.
DR ExpressionAtlas; Q3TWL2; baseline and differential.
DR Genevisible; Q3TWL2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0034597; F:phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity; ISO:MGI.
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:MGI.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:UniProtKB.
DR GO; GO:0070070; P:proton-transporting V-type ATPase complex assembly; IMP: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_0000235234"
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:19144319"
SQ SEQUENCE 284 AA; 30047 MW; 6F85B05FBA3B908B 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
WKHAQQYGGI YAAWAFVILL AVLCLGRALY WACMKVSHPV QNFS
