PP4P2_HUMAN
ID PP4P2_HUMAN Reviewed; 257 AA.
AC Q8N4L2; B2R9H4; Q68CU2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
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:0000269|PubMed:16365287};
DE AltName: Full=PtdIns-4,5-P2 4-Ptase II;
DE AltName: Full=Transmembrane protein 55A;
GN Name=PIP4P2 {ECO:0000312|HGNC:HGNC:25452};
GN Synonyms=TMEM55A {ECO:0000312|HGNC:HGNC:25452};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=16365287; DOI=10.1073/pnas.0509740102;
RA Ungewickell A., Hugge C., Kisseleva M., Chang S.-C., Zou J., Feng Y.,
RA Galyov E.E., Wilson M., Majerus P.W.;
RT "The identification and characterization of two phosphatidylinositol-4,5-
RT bisphosphate 4-phosphatases.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18854-18859(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylinositol-4,5-
CC bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate
CC (PtdIns-4-P) (PubMed:16365287). 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 (PubMed:16365287). Negatively
CC regulates the phagocytosis of large particles by reducing phagosomal
CC phosphatidylinositol 4,5-bisphosphate accumulation during cup formation
CC (By similarity). {ECO:0000250|UniProtKB:Q9CZX7,
CC ECO:0000269|PubMed:16365287}.
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:0000269|PubMed:16365287};
CC -!- INTERACTION:
CC Q8N4L2; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2820617, EBI-18159983;
CC Q8N4L2; P01375: TNF; NbExp=3; IntAct=EBI-2820617, EBI-359977;
CC Q8N4L2; Q5T4F4: ZFYVE27; NbExp=3; IntAct=EBI-2820617, EBI-3892947;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:16365287}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:16365287}; Multi-
CC pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000250|UniProtKB:Q9CZX7}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9CZX7}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16365287}.
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; AK313783; BAG36521.1; -; mRNA.
DR EMBL; CH471060; EAW91672.1; -; Genomic_DNA.
DR EMBL; BC033892; AAH33892.1; -; mRNA.
DR EMBL; CR749733; CAH18492.1; -; mRNA.
DR CCDS; CCDS6252.1; -.
DR RefSeq; NP_061180.1; NM_018710.2.
DR AlphaFoldDB; Q8N4L2; -.
DR BioGRID; 120700; 40.
DR IntAct; Q8N4L2; 27.
DR MINT; Q8N4L2; -.
DR STRING; 9606.ENSP00000285419; -.
DR SwissLipids; SLP:000000851; -.
DR DEPOD; PIP4P2; -.
DR iPTMnet; Q8N4L2; -.
DR PhosphoSitePlus; Q8N4L2; -.
DR SwissPalm; Q8N4L2; -.
DR BioMuta; PIP4P2; -.
DR DMDM; 74728868; -.
DR EPD; Q8N4L2; -.
DR jPOST; Q8N4L2; -.
DR MassIVE; Q8N4L2; -.
DR MaxQB; Q8N4L2; -.
DR PaxDb; Q8N4L2; -.
DR PeptideAtlas; Q8N4L2; -.
DR PRIDE; Q8N4L2; -.
DR ProteomicsDB; 71939; -.
DR Antibodypedia; 3026; 44 antibodies from 13 providers.
DR DNASU; 55529; -.
DR Ensembl; ENST00000285419.8; ENSP00000285419.3; ENSG00000155099.8.
DR GeneID; 55529; -.
DR KEGG; hsa:55529; -.
DR MANE-Select; ENST00000285419.8; ENSP00000285419.3; NM_018710.3; NP_061180.1.
DR UCSC; uc003yes.5; human.
DR CTD; 55529; -.
DR DisGeNET; 55529; -.
DR GeneCards; PIP4P2; -.
DR HGNC; HGNC:25452; PIP4P2.
DR HPA; ENSG00000155099; Low tissue specificity.
DR MIM; 609864; gene.
DR neXtProt; NX_Q8N4L2; -.
DR OpenTargets; ENSG00000155099; -.
DR PharmGKB; PA142670771; -.
DR VEuPathDB; HostDB:ENSG00000155099; -.
DR eggNOG; KOG4684; Eukaryota.
DR GeneTree; ENSGT00390000003680; -.
DR InParanoid; Q8N4L2; -.
DR OMA; CQNMIDI; -.
DR OrthoDB; 1346704at2759; -.
DR PhylomeDB; Q8N4L2; -.
DR TreeFam; TF316367; -.
DR BioCyc; MetaCyc:HS14553-MON; -.
DR BRENDA; 3.1.3.78; 2681.
DR PathwayCommons; Q8N4L2; -.
DR SignaLink; Q8N4L2; -.
DR BioGRID-ORCS; 55529; 12 hits in 1080 CRISPR screens.
DR ChiTaRS; TMEM55A; human.
DR GenomeRNAi; 55529; -.
DR Pharos; Q8N4L2; Tbio.
DR PRO; PR:Q8N4L2; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8N4L2; protein.
DR Bgee; ENSG00000155099; Expressed in pigmented layer of retina and 178 other tissues.
DR ExpressionAtlas; Q8N4L2; baseline and differential.
DR Genevisible; Q8N4L2; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IDA:FlyBase.
DR GO; GO:0005765; C:lysosomal membrane; IDA:FlyBase.
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; IDA:FlyBase.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:FlyBase.
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_0000235228"
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:23186163"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZX7"
SQ SEQUENCE 257 AA; 28081 MW; 2E059F7D07BA9227 CRC64;
MAADGVDERS PLLSASHSGN VTPTAPPYLQ ESSPRAELPP PYTAIASPDA SGIPVINCRV
CQSLINLDGK LHQHVVKCTV CNEATPIKNP PTGKKYVRCP CNCLLICKDT SRRIGCPRPN
CRRIINLGPV MLISEEQPAQ PALPIQPEGT RVVCGHCGNT FLWMELRFNT LAKCPHCKKI
SSVGSALPRR RCCAYITIGM ICIFIGVGLT VGTPDFARRF RATYVSWAIA YLLGLICLIR
ACYWGAIRVS YPEHSFA
