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PLPP1_CAVPO
ID   PLPP1_CAVPO             Reviewed;         285 AA.
AC   O88956; O88957;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Phospholipid phosphatase 1 {ECO:0000305};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:O14494};
DE            EC=3.1.3.106 {ECO:0000250|UniProtKB:Q61469};
DE            EC=3.1.3.4 {ECO:0000269|PubMed:18215144};
DE            EC=3.1.3.81 {ECO:0000250|UniProtKB:Q61469};
DE   AltName: Full=Lipid phosphate phosphohydrolase 1;
DE   AltName: Full=PAP2-alpha;
DE   AltName: Full=Phosphatidate phosphohydrolase type 2a;
DE   AltName: Full=Phosphatidic acid phosphatase 2a;
DE            Short=PAP-2a;
DE            Short=PAP2a;
GN   Name=PLPP1 {ECO:0000250|UniProtKB:O14494}; Synonyms=LPP1, PAP2A, PPAP2A;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Airway smooth muscle;
RX   PubMed=10405762; DOI=10.1016/s0898-6568(99)00028-5;
RA   Tate R.J., Tolan D., Pyne S.;
RT   "Molecular cloning of magnesium-independent type 2 phosphatidic acid
RT   phosphatases from airway smooth muscle.";
RL   Cell. Signal. 11:515-522(1999).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND MUTAGENESIS OF ARG-127
RP   AND HIS-223.
RX   PubMed=18215144; DOI=10.1042/bj20071607;
RA   Long J.S., Pyne N.J., Pyne S.;
RT   "Lipid phosphate phosphatases form homo- and hetero-oligomers: catalytic
RT   competency, subcellular distribution and function.";
RL   Biochem. J. 411:371-377(2008).
CC   -!- FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma
CC       membrane that catalyzes the dephosphorylation of a variety of
CC       glycerolipid and sphingolipid phosphate esters including
CC       phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol
CC       pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-
CC       phosphate/C1P (PubMed:18215144). Also acts on N-oleoyl ethanolamine
CC       phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential
CC       physiological compound (By similarity). Through its extracellular
CC       phosphatase activity allows both the hydrolysis and the cellular uptake
CC       of these bioactive lipid mediators from the milieu, regulating signal
CC       transduction in different cellular processes (By similarity). It is for
CC       instance essential for the extracellular hydrolysis of S1P and
CC       subsequent conversion into intracellular S1P (By similarity). Involved
CC       in the regulation of inflammation, platelets activation, cell
CC       proliferation and migration among other processes (By similarity). May
CC       also have an intracellular activity to regulate phospholipid-mediated
CC       signaling pathways (By similarity). {ECO:0000250|UniProtKB:O08564,
CC       ECO:0000250|UniProtKB:O14494, ECO:0000269|PubMed:18215144}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC         glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC         Evidence={ECO:0000269|PubMed:18215144};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC         Evidence={ECO:0000305|PubMed:18215144};
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:0000250|UniProtKB:O14494};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC         Evidence={ECO:0000250|UniProtKB:O14494};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-
CC         di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333,
CC         ChEBI:CHEBI:74546; Evidence={ECO:0000250|UniProtKB:O14494};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC         Evidence={ECO:0000250|UniProtKB:O14494};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol +
CC         phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589;
CC         Evidence={ECO:0000250|UniProtKB:O14494};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737;
CC         Evidence={ECO:0000250|UniProtKB:O14494};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-
CC         octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937,
CC         ChEBI:CHEBI:84973; Evidence={ECO:0000250|UniProtKB:O14494};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885;
CC         Evidence={ECO:0000250|UniProtKB:O14494};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol +
CC         phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683;
CC         EC=3.1.3.106; Evidence={ECO:0000250|UniProtKB:Q61469};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156;
CC         Evidence={ECO:0000250|UniProtKB:Q61469};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-
CC         octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544,
CC         ChEBI:CHEBI:75757; Evidence={ECO:0000250|UniProtKB:Q61469};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC         Evidence={ECO:0000250|UniProtKB:Q61469};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.1.3.81;
CC         Evidence={ECO:0000250|UniProtKB:Q61469};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450;
CC         Evidence={ECO:0000250|UniProtKB:Q61469};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine;
CC         Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:60119;
CC         Evidence={ECO:0000250|UniProtKB:O14494};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC         Evidence={ECO:0000250|UniProtKB:O14494};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-
CC         enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674;
CC         Evidence={ECO:0000250|UniProtKB:O14494};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744;
CC         Evidence={ECO:0000250|UniProtKB:O14494};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-
CC         octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815,
CC         ChEBI:CHEBI:85376; Evidence={ECO:0000250|UniProtKB:O14494};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041;
CC         Evidence={ECO:0000250|UniProtKB:O14494};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-
CC         octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466,
CC         ChEBI:CHEBI:145465; Evidence={ECO:0000250|UniProtKB:O14494};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161;
CC         Evidence={ECO:0000250|UniProtKB:O14494};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC         H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate;
CC         Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:64839, ChEBI:CHEBI:75466;
CC         Evidence={ECO:0000250|UniProtKB:O08564};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256;
CC         Evidence={ECO:0000250|UniProtKB:O08564};
CC   -!- ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase.
CC       Insensitive to N-ethylmaleimide. {ECO:0000250|UniProtKB:O14494}.
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000269|PubMed:18215144}.
CC   -!- SUBUNIT: Forms functional homodimers and homooligomers that are not
CC       required for substrate recognition and catalytic activity
CC       (PubMed:18215144). Can also form heterooligomers with PLPP2 and PLPP3
CC       (PubMed:18215144). {ECO:0000269|PubMed:18215144}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14494};
CC       Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein
CC       {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O14494}; Multi-pass
CC       membrane protein {ECO:0000255}. Membrane, caveola
CC       {ECO:0000250|UniProtKB:Q61469}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=PAP2a1;
CC         IsoId=O88956-1; Sequence=Displayed;
CC       Name=2; Synonyms=PAP2a2;
CC         IsoId=O88956-2; Sequence=VSP_009650;
CC   -!- PTM: N-glycosylated. N-linked sugars are of the complex type. N-
CC       glycosylation is not required for the phosphatase activity.
CC       {ECO:0000250|UniProtKB:Q61469}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
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DR   EMBL; AF088283; AAC63333.1; -; mRNA.
DR   EMBL; AF088284; AAC63334.1; -; mRNA.
DR   RefSeq; NP_001166474.1; NM_001173003.1.
DR   AlphaFoldDB; O88956; -.
DR   STRING; 10141.ENSCPOP00000008809; -.
DR   GeneID; 100135603; -.
DR   KEGG; cpoc:100135603; -.
DR   CTD; 8611; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   InParanoid; O88956; -.
DR   OrthoDB; 1354951at2759; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR   GO; GO:0106235; F:ceramide-1-phosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR   GO; GO:0006670; P:sphingosine metabolic process; ISS:UniProtKB.
DR   InterPro; IPR028670; LPP1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR043216; PA_PP_rel.
DR   PANTHER; PTHR10165; PTHR10165; 1.
DR   PANTHER; PTHR10165:SF26; PTHR10165:SF26; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Hydrolase;
KW   Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..285
FT                   /note="Phospholipid phosphatase 1"
FT                   /id="PRO_0000220904"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q61469"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..53
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q61469"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q61469"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..165
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q61469"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..199
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q61469"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        221..229
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q61469"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..285
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q61469"
FT   REGION          120..128
FT                   /note="Phosphatase sequence motif I"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   REGION          168..171
FT                   /note="Phosphatase sequence motif II"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   REGION          216..227
FT                   /note="Phosphatase sequence motif III"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   REGION          260..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           5..7
FT                   /note="PDZ-binding; involved in localization to the apical
FT                   cell membrane"
FT                   /evidence="ECO:0000250|UniProtKB:O14494"
FT   COMPBIAS        270..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        171
FT                   /note="Proton donors"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   ACT_SITE        223
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   SITE            227
FT                   /note="Stabilizes the active site histidine for
FT                   nucleophilic attack"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         21..70
FT                   /note="GLPFAILTSRHTPFQRGIFCNDESIKYPYKEDTIPYALLGGIMIPFSIVV
FT                   -> SMPMAVLNLGQIYPFQRGFFCNDNSIQYPYHDSTVASTILTIVGLGLPISS (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10405762"
FT                   /id="VSP_009650"
FT   MUTAGEN         127
FT                   /note="R->K: Loss of lipid phosphatase activity."
FT                   /evidence="ECO:0000269|PubMed:18215144"
FT   MUTAGEN         223
FT                   /note="H->L: Decreased lipid phosphatase activity."
FT                   /evidence="ECO:0000269|PubMed:18215144"
FT   CONFLICT        5
FT                   /note="A -> T (in Ref. 1; AAC63334)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="I -> V (in Ref. 1; AAC63334)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   285 AA;  32133 MW;  E6F48E188DED6CF5 CRC64;
     MFDKARLPYV ALDVLCVVLA GLPFAILTSR HTPFQRGIFC NDESIKYPYK EDTIPYALLG
     GIMIPFSIVV MIIGETLSVY CNLLHSNSFI RNNYIATIYK SIGTFLFGAA ASQSLTDIAK
     YSIGRLRPHF LSVCDPDWSK VNCSDGYIEY YVCRGNAEKV KEGRLSFYSG HSSFSMYCMV
     FVALYLQARM KGDWARLLRP TLQFGLVAAS IYVGLSRISD YKHHWSDVLT GLIQGAIVAI
     LVAVYVSDFF KARNSPFQER KEEDSHTTLH ETPTAGNHYR SNHQP
 
 
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