PP4P2_BOVIN
ID PP4P2_BOVIN Reviewed; 257 AA.
AC Q3SZ48;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 {ECO:0000250|UniProtKB:Q8N4L2};
GN Synonyms=TMEM55A {ECO:0000250|UniProtKB:Q8N4L2};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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) (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 (By similarity). {ECO:0000250|UniProtKB:Q8N4L2,
CC ECO:0000250|UniProtKB:Q9CZX7}.
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}. 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}.
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DR EMBL; BC103147; AAI03148.1; -; mRNA.
DR RefSeq; NP_001035684.1; NM_001040594.2.
DR AlphaFoldDB; Q3SZ48; -.
DR STRING; 9913.ENSBTAP00000028656; -.
DR PaxDb; Q3SZ48; -.
DR PRIDE; Q3SZ48; -.
DR Ensembl; ENSBTAT00000028656; ENSBTAP00000028656; ENSBTAG00000039968.
DR GeneID; 616641; -.
DR KEGG; bta:616641; -.
DR CTD; 55529; -.
DR VEuPathDB; HostDB:ENSBTAG00000039968; -.
DR VGNC; VGNC:32910; PIP4P2.
DR eggNOG; KOG4684; Eukaryota.
DR GeneTree; ENSGT00390000003680; -.
DR HOGENOM; CLU_087485_0_0_1; -.
DR InParanoid; Q3SZ48; -.
DR OMA; CQNMIDI; -.
DR OrthoDB; 1346704at2759; -.
DR TreeFam; TF316367; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000039968; Expressed in occipital lobe and 100 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB.
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 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_0000235227"
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..34
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:0000250|UniProtKB:Q8N4L2"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZX7"
SQ SEQUENCE 257 AA; 28040 MW; F7936385A5CAC6FC CRC64;
MAADGVDERS PLLSASHSGS VTPTAPPYLQ DSSPRAELPP PYTAIVSPDA SGIPVINCRV
CQSLINLDGK LHQHVVKCTV CNEATPIKNP PAGKKYVRCP CNCLLICKDT SRRIGCPRPN
CRRIINLGPV MLVSEEQPAQ PALPVQPEGT RVVCGHCGNT FLWMELRFNT LAKCPHCKKI
SSVGSALPRR RCCAYITIGM MCIFIGIGLT VGTQDFARRF HATYVSWAIA YLLGLVCLIR
ACYWGAIRVS YPEHSFA
