ID   PP4P2_XENLA             Reviewed;         256 AA.
AC   Q5EAU3;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Type II 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 {ECO:0000250|UniProtKB:Q8N4L2};
GN   Synonyms=tmem55a {ECO:0000250|UniProtKB:Q8N4L2};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylinositol-4,5-
CC       bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate
CC       (PtdIns-4-P). {ECO:0000250|UniProtKB:Q8N4L2}.
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:0000250|UniProtKB:Q8N4L2}; Multi-pass membrane protein
CC       {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8N4L2}; Multi-
CC       pass membrane protein {ECO:0000255}.
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; BC090241; AAH90241.1; -; mRNA.
DR   RefSeq; NP_001089295.1; NM_001095826.1.
DR   AlphaFoldDB; Q5EAU3; -.
DR   DNASU; 734343; -.
DR   GeneID; 734343; -.
DR   KEGG; xla:734343; -.
DR   CTD; 734343; -.
DR   Xenbase; XB-GENE-951977; pip4p2.L.
DR   OrthoDB; 1346704at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 734343; Expressed in egg cell and 8 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034597; F:phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity; IEA:InterPro.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
DR   InterPro; IPR019178; PtdIns-P2-Ptase.
DR   PANTHER; PTHR21014; PTHR21014; 1.
DR   Pfam; PF09788; Tmemb_55A; 1.
PE   2: Evidence at transcript level;
KW   Endosome; Hydrolase; Lipid metabolism; Lysosome; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..256
FT                   /note="Type II phosphatidylinositol 4,5-bisphosphate 4-
FT                   phosphatase"
FT                   /id="PRO_0000235231"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           106..112
FT                   /note="CX5R motif"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   256 AA;  27999 MW;  0C28B2A77F19EB3F CRC64;
     MAADGIDERS PLISPSSGNV TPTAPPYIQE NNLQAELPPP YTAIASPDAG GVPVINCRVC
     QSLINLDGKL HQHVVKCTVC NEATPIKTPP LGKKYVRCPC NCLLICKDIS RRIGCPRPNC
     RRIINLGPVM LIPEEQPAQP ALPVQPDGTR VVCGHCGNTF LWMELRFNTL AKCPHCKKIS
     SVGSALPRRR CCTYITMGMI CIFIGVGLTV GTQDFARRFH ATYVSWAVAY LVGLVCLVRA
     CYWGAIKFSY PEHSFA