Legends: 1, N-linked (GlcNAc...). {ECO:0000255}; 2, CONFLICT A -> T (in Ref. 1; AAC63334). {ECO:0000305}; 3, CONFLICT I -> V (in Ref. 1; AAC63334). {ECO:0000305}; 4, TOPO_DOM Cytoplasmic. {ECO:0000255}; 5, TRANSMEM Helical. {ECO:0000255}; 6, TOPO_DOM Lumenal. {ECO:0000255}; 7, VAR_SEQ GLPFAILTSRHTPFQRGIFCNDESIKYPYKEDTIPYALLGG IMIPFSIVV -> SMPMAVLNLGQIYPFQRGFFCNDNSIQY PYHDSTVASTILTIVGLGLPISS (in isoform 2). {ECO:0000303|PubMed:10405762}.
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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 06-JUL-2016, entry version 84.
DE RecName: Full=Phospholipid phosphatase 1 {ECO:0000250|UniProtKB:O14494};
DE EC=3.1.3.4;
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};
GN Synonyms=LPP1, PAP2A, PPAP2A;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC Hystricognathi; Caviidae; 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).
CC -!- FUNCTION: Broad-specificity phosphohydrolase that dephosphorylates
CC exogenous bioactive glycerolipids and sphingolipids. Catalyzes the
CC conversion of phosphatidic acid (PA) to diacylglycerol (DG). In
CC addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-
CC phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P) (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC 1,2-diacyl-sn-glycerol + phosphate.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
DR EMBL; AF088283; AAC63333.1; -; mRNA.
DR EMBL; AF088284; AAC63334.1; -; mRNA.
DR RefSeq; NP_001166474.1; NM_001173003.1.
DR ProteinModelPortal; O88956; -.
DR STRING; 10141.ENSCPOP00000008809; -.
DR GeneID; 100135603; -.
DR CTD; 8611; -.
DR eggNOG; KOG3030; Eukaryota.
DR eggNOG; COG0671; LUCA.
DR HOGENOM; HOG000041307; -.
DR HOVERGEN; HBG002048; -.
DR InParanoid; O88956; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.144.10; -; 1.
DR InterPro; IPR028670; LPP1.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR10165:SF26; PTHR10165:SF26; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
KW Hydrolase; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 285 Phospholipid phosphatase 1.
FT /FTId=PRO_0000220904.
FT TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 7 27 Helical. {ECO:0000255}.
FT TOPO_DOM 28 53 Lumenal. {ECO:0000255}.
FT TRANSMEM 54 74 Helical. {ECO:0000255}.
FT TOPO_DOM 75 94 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 95 115 Helical. {ECO:0000255}.
FT TOPO_DOM 116 165 Lumenal. {ECO:0000255}.
FT TRANSMEM 166 186 Helical. {ECO:0000255}.
FT TOPO_DOM 187 199 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 200 220 Helical. {ECO:0000255}.
FT TOPO_DOM 221 229 Lumenal. {ECO:0000255}.
FT TRANSMEM 230 250 Helical. {ECO:0000255}.
FT TOPO_DOM 251 285 Cytoplasmic. {ECO:0000255}.
FT CARBOHYD 142 142 N-linked (GlcNAc...). {ECO:0000255}.
FT VAR_SEQ 21 70 GLPFAILTSRHTPFQRGIFCNDESIKYPYKEDTIPYALLGG
FT IMIPFSIVV -> SMPMAVLNLGQIYPFQRGFFCNDNSIQY
FT PYHDSTVASTILTIVGLGLPISS (in isoform 2).
FT {ECO:0000303|PubMed:10405762}.
FT /FTId=VSP_009650.
FT CONFLICT 5 5 A -> T (in Ref. 1; AAC63334).
FT {ECO:0000305}.
FT CONFLICT 218 218 I -> V (in Ref. 1; AAC63334).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 105 247 ipfam:PAP2 [T]
FT MYHIT 102 243 ismart:acidPPc [T]
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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