ID A4IIM0_XENTR Unreviewed; 275 AA.
AC A4IIM0;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6 {ECO:0000256|ARBA:ARBA00040581};
DE EC=3.6.1.68 {ECO:0000256|ARBA:ARBA00038898};
DE AltName: Full=Phospholipid phosphatase 6 {ECO:0000256|ARBA:ARBA00042093};
GN Name=plpp6 {ECO:0000313|RefSeq:NP_001096415.1,
GN ECO:0000313|Xenbase:XB-GENE-5871301};
GN Synonyms=LOC100125020 {ECO:0000313|EMBL:AAI36075.1}, ppapdc2
GN {ECO:0000313|RefSeq:NP_001096415.1,
GN ECO:0000313|Xenbase:XB-GENE-5871301};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI36075.1};
RN [1] {ECO:0000313|RefSeq:NP_001096415.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI36075.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000313|EMBL:AAI36075.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001096415.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (2E)-geranyl phosphate + H(+)
CC + phosphate; Xref=Rhea:RHEA:47944, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:88107; EC=3.6.1.68;
CC Evidence={ECO:0000256|ARBA:ARBA00035809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47945;
CC Evidence={ECO:0000256|ARBA:ARBA00035809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl phosphate + H2O = (2E)-geraniol + phosphate;
CC Xref=Rhea:RHEA:68020, ChEBI:CHEBI:15377, ChEBI:CHEBI:17447,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:88107;
CC Evidence={ECO:0000256|ARBA:ARBA00036169};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68021;
CC Evidence={ECO:0000256|ARBA:ARBA00036169};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesyl
CC phosphate + H(+) + phosphate; Xref=Rhea:RHEA:48128,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:88226, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000256|ARBA:ARBA00037020};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48129;
CC Evidence={ECO:0000256|ARBA:ARBA00037020};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl phosphate + H2O = (2E,6E)-farnesol +
CC phosphate; Xref=Rhea:RHEA:48132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16619, ChEBI:CHEBI:43474, ChEBI:CHEBI:88226;
CC Evidence={ECO:0000256|ARBA:ARBA00036036};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48133;
CC Evidence={ECO:0000256|ARBA:ARBA00036036};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (2E,6E,10E)-
CC geranylgeranyl phosphate + H(+) + phosphate; Xref=Rhea:RHEA:68008,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58756, ChEBI:CHEBI:144936;
CC Evidence={ECO:0000256|ARBA:ARBA00035926};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68009;
CC Evidence={ECO:0000256|ARBA:ARBA00035926};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl phosphate + H2O = (2E,6E,10E)-
CC geranylgeraniol + phosphate; Xref=Rhea:RHEA:68016, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46762, ChEBI:CHEBI:144936;
CC Evidence={ECO:0000256|ARBA:ARBA00036255};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68017;
CC Evidence={ECO:0000256|ARBA:ARBA00036255};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-
CC dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859,
CC ChEBI:CHEBI:82929; Evidence={ECO:0000256|ARBA:ARBA00001611};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC Evidence={ECO:0000256|ARBA:ARBA00001611};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + presqualene diphosphate = H(+) + phosphate + presqualene
CC monophosphate; Xref=Rhea:RHEA:67968, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57310,
CC ChEBI:CHEBI:176803; Evidence={ECO:0000256|ARBA:ARBA00036000};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67969;
CC Evidence={ECO:0000256|ARBA:ARBA00036000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + presqualene monophosphate = phosphate + presqualene
CC alcohol; Xref=Rhea:RHEA:68024, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:176803, ChEBI:CHEBI:176962;
CC Evidence={ECO:0000256|ARBA:ARBA00035802};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68025;
CC Evidence={ECO:0000256|ARBA:ARBA00035802};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Nucleus envelope
CC {ECO:0000256|ARBA:ARBA00004259}. Nucleus inner membrane
CC {ECO:0000256|ARBA:ARBA00004540}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; BC136074; AAI36075.1; -; mRNA.
DR RefSeq; NP_001096415.1; NM_001102945.1.
DR DNASU; 100125020; -.
DR GeneID; 100125020; -.
DR KEGG; xtr:100125020; -.
DR AGR; Xenbase:XB-GENE-5871301; -.
DR CTD; 403313; -.
DR Xenbase; XB-GENE-5871301; plpp6.
DR OMA; MYKSDSA; -.
DR OrthoDB; 1221241at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd03391; PAP2_containing_2_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR14969:SF18; POLYISOPRENOID DIPHOSPHATE_PHOSPHATE PHOSPHOHYDROLASE PLPP6; 1.
DR PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 149..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 149..263
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 30..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 275 AA; 30692 MW; 1FC70523977F3BDA CRC64;
MPSPRVSRAA NNAANPMNKI EFMSLLTNRT NSSDPVSVRH RASDSPVHRK DSFNSTSSTS
SQQQQQQQQL PEEDCMKLNP SFLGIALSSL LAVDLWLSKT IGVCAREGSS WGSARPLMKL
VEISGHGIPW IAGTLYCLYK SDSNAGREVI LNLLFALLLD LVLVGIVKGI VKRRRPIHNR
MDMFATFSVD KYSFPSGHAT RAAMVSRFML NHLVLAVPVR ILVMLWAIVV SLSRVMLGRH
NVTDVLFGFF MGHMQYSLIE YLWLSPSTLP ALFRM
//
