PP4P2_MOUSE
ID PP4P2_MOUSE Reviewed; 257 AA.
AC Q9CZX7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase;
DE Short=Type 2 PtdIns-4,5-P2 4-Ptase;
DE EC=3.1.3.78 {ECO:0000250|UniProtKB:Q8N4L2};
DE AltName: Full=PtdIns-4,5-P2 4-Ptase II;
DE AltName: Full=Transmembrane protein 55A;
GN Name=Pip4p2; Synonyms=Tmem55a;
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=Epididymis;
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=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22 AND SER-33, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [6]
RP FUNCTION, AND 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). Negatively
CC regulates the phagocytosis of large particles by reducing phagosomal
CC phosphatidylinositol 4,5-bisphosphate accumulation during cup formation
CC (PubMed:29378918). {ECO:0000250|UniProtKB:Q8N4L2,
CC ECO:0000269|PubMed:29378918}.
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:Q8N4L2};
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:29378918}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8N4L2}; 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; AK012054; BAB27995.1; -; mRNA.
DR EMBL; AK033845; BAC28493.1; -; mRNA.
DR EMBL; AK049213; BAC33613.1; -; mRNA.
DR EMBL; BC021435; AAH21435.1; -; mRNA.
DR CCDS; CCDS17981.1; -.
DR RefSeq; NP_082540.1; NM_028264.4.
DR AlphaFoldDB; Q9CZX7; -.
DR BioGRID; 215414; 6.
DR IntAct; Q9CZX7; 5.
DR STRING; 10090.ENSMUSP00000029875; -.
DR iPTMnet; Q9CZX7; -.
DR PhosphoSitePlus; Q9CZX7; -.
DR SwissPalm; Q9CZX7; -.
DR EPD; Q9CZX7; -.
DR jPOST; Q9CZX7; -.
DR MaxQB; Q9CZX7; -.
DR PaxDb; Q9CZX7; -.
DR PeptideAtlas; Q9CZX7; -.
DR PRIDE; Q9CZX7; -.
DR ProteomicsDB; 289872; -.
DR Antibodypedia; 3026; 44 antibodies from 13 providers.
DR Ensembl; ENSMUST00000029875; ENSMUSP00000029875; ENSMUSG00000028221.
DR GeneID; 72519; -.
DR KEGG; mmu:72519; -.
DR UCSC; uc008sbg.1; mouse.
DR CTD; 55529; -.
DR MGI; MGI:1919769; Pip4p2.
DR VEuPathDB; HostDB:ENSMUSG00000028221; -.
DR eggNOG; KOG4684; Eukaryota.
DR GeneTree; ENSGT00390000003680; -.
DR HOGENOM; CLU_087485_0_0_1; -.
DR InParanoid; Q9CZX7; -.
DR OMA; CQNMIDI; -.
DR OrthoDB; 1346704at2759; -.
DR PhylomeDB; Q9CZX7; -.
DR TreeFam; TF316367; -.
DR BioGRID-ORCS; 72519; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Pip4p2; mouse.
DR PRO; PR:Q9CZX7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9CZX7; protein.
DR Bgee; ENSMUSG00000028221; Expressed in frontonasal prominence and 256 other tissues.
DR Genevisible; Q9CZX7; 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; ISO:MGI.
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:0050765; P:negative regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IMP: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..257
FT /note="Type 2 phosphatidylinositol 4,5-bisphosphate 4-
FT phosphatase"
FT /id="PRO_0000235229"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 107..113
FT /note="CX5R motif"
FT COMPBIAS 13..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 107
FT /evidence="ECO:0000250"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 257 AA; 28038 MW; 0330A735DBCEC243 CRC64;
MAADGVDERS PLLSASHSGN VTPTAPPYLQ ESSPRAELPP PYTAIASPGT SGIPVINCRV
CQSLINLDGK LHQHVVKCTV CNEATPIKTP PTGKKYVRCP CNCLLICKDT SRRIGCPRPN
CRRIINLGPV MLISEEQPAQ PALPIQPEGT RVVCGHCGNT FLWMELRFNT LAKCPHCKKI
SSVGSALPRR RCCAYVTIGM ICIFIAVGLT VGTQDFSRRF HATYVSWAIA YLLGLICLIR
ACYWGAIRVS YPEHGFA
