PP4P1_XENLA
ID PP4P1_XENLA Reviewed; 281 AA.
AC Q5XKA6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 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=Liver;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) 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: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 -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q86T03}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q86T03}; Multi-
CC pass membrane protein {ECO:0000255}.
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DR EMBL; BC083005; AAH83005.1; -; mRNA.
DR RefSeq; NP_001088129.1; NM_001094660.1.
DR AlphaFoldDB; Q5XKA6; -.
DR SMR; Q5XKA6; -.
DR GeneID; 494834; -.
DR KEGG; xla:494834; -.
DR CTD; 494834; -.
DR Xenbase; XB-GENE-6255074; pip4p1.L.
DR OMA; APYGVPN; -.
DR OrthoDB; 1346704at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 494834; Expressed in brain and 19 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; IEA:InterPro.
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..281
FT /note="Type 1 phosphatidylinositol 4,5-bisphosphate 4-
FT phosphatase"
FT /id="PRO_0000235235"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..143
FT /note="CX5R motif"
FT COMPBIAS 31..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /evidence="ECO:0000250"
SQ SEQUENCE 281 AA; 29750 MW; 569CA51619E4AEBF CRC64;
MADGERSPLL SDLGDGGGMG AAMGPGAPSP GSALPTAPPY GGPGPASNKP QGFPEFPAAH
GSVITGEDPP PYSPLTSPES GSAPMITCRV CQSLINVEGK MHQHVVKCGV CNEATPIKNA
PQGKKYVRCP CNCLLICKVT SQRIACPRPY CKRIINLGPV HAGPLSPEPQ PVGVRVICGH
CKNNFLWTEF SDRTLARCPH CRKVSSIGMR YPRKRCFCCF LLGVLLALAA AGLVGGTWTL
AYKYGGIYAS WAILLLLALA CIGRGIYWAC MRVSHPVQSF S