ID PLA1A_PONAB Reviewed; 456 AA.
AC Q5RBQ5; Q5REF0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Phospholipase A1 member A;
DE EC=3.1.1.111 {ECO:0000250|UniProtKB:P97535};
DE Flags: Precursor;
GN Name=PLA1A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes the ester bond of the acyl group attached at the
CC sn-1 position of phosphatidylserines (phospholipase A1 activity) and 1-
CC acyl-2-lysophosphatidylserines (lysophospholipase activity) in the
CC pathway of phosphatidylserines acyl chain remodeling (By similarity).
CC Cleaves phosphatidylserines exposed on the outer leaflet of the plasma
CC membrane of apoptotic cells producing 2-acyl-1-lysophosphatidylserines,
CC which in turn enhance mast cell activation and histamine production.
CC Has no activity toward other glycerophospholipids including
CC phosphatidylcholines, phosphatidylethanolamines, phosphatidic acids or
CC phosphatidylinositols, or glycerolipids such as triolein (By
CC similarity). {ECO:0000250|UniProtKB:P97535,
CC ECO:0000250|UniProtKB:Q53H76}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-
CC sn-glycero-3-phospho-L-serine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:42212, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57262, ChEBI:CHEBI:65214;
CC EC=3.1.1.111; Evidence={ECO:0000250|UniProtKB:P97535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42213;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + H(+); Xref=Rhea:RHEA:40491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74905,
CC ChEBI:CHEBI:77342; Evidence={ECO:0000250|UniProtKB:P97535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40492;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phospho-L-serine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phospho-L-serine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41187, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:75032, ChEBI:CHEBI:77830;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41188;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + H2O = a fatty acid +
CC H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:32979,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:64379, ChEBI:CHEBI:64765; EC=3.1.1.111;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32980;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P97535}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RBQ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RBQ5-2; Sequence=VSP_022510;
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; CR857579; CAH89857.1; -; mRNA.
DR EMBL; CR858583; CAH90805.1; -; mRNA.
DR RefSeq; NP_001124864.1; NM_001131392.1. [Q5RBQ5-1]
DR RefSeq; NP_001128786.1; NM_001135314.1. [Q5RBQ5-2]
DR AlphaFoldDB; Q5RBQ5; -.
DR SMR; Q5RBQ5; -.
DR STRING; 9601.ENSPPYP00000015111; -.
DR ESTHER; ponpy-q5ref0; Phospholipase.
DR GlyCosmos; Q5RBQ5; 1 site, No reported glycans.
DR Ensembl; ENSPPYT00000015714.3; ENSPPYP00000015111.3; ENSPPYG00000013512.3. [Q5RBQ5-1]
DR GeneID; 100171726; -.
DR GeneID; 100189689; -.
DR KEGG; pon:100171726; -.
DR CTD; 51365; -.
DR eggNOG; ENOG502QQQP; Eukaryota.
DR GeneTree; ENSGT00940000159279; -.
DR InParanoid; Q5RBQ5; -.
DR OMA; AHANPQC; -.
DR OrthoDB; 3428256at2759; -.
DR Proteomes; UP000001595; Chromosome 3.
DR GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR016272; Lipase_LIPH.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; LIPASE; 1.
DR PANTHER; PTHR11610:SF111; PHOSPHOLIPASE A1 MEMBER A; 1.
DR Pfam; PF00151; Lipase; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..456
FT /note="Phospholipase A1 member A"
FT /id="PRO_0000273332"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 245..258
FT /evidence="ECO:0000250"
FT DISULFID 282..293
FT /evidence="ECO:0000250"
FT DISULFID 296..304
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_022510"
SQ SEQUENCE 456 AA; 49710 MW; 701E778E40AFF55F CRC64;
MPPGPWESCF WVGGLLLWLS VGSSGDAPPT PQPNCADFQS ANLFEGTDLK VQFLLFVPSN
PSCGQLVEGS SDLQNSGFNA TLGTKLIIHG FRVLGTKPSW IDKFIRTLLL ATNANVIAVD
WIYGSTGVYF SAVKNVIKLS LEISLFLNKL LVLGVSESSI HIIGVSLGAH VGGMVGQLFG
GQLGQITGLD PAGPEYTRAS VEERLDAGDA LFVEAIHTDT DNLGIRIPVG HVDYFVNGGQ
DQPGCPTFFY AGYSYLICDH MRAVHLYISA LENSCPLMAF PCASYKAFLA GRCLDCFNPF
LLSCPRIGLV EQGGVKIEPL PKEVKVYLLT TSSAPYCMHH SLVEFHLKEL RNKDTNIEVT
FLSSNVTSSS KITIPKQQRY GKGIIAHATP QCQINQVKFK FQSSNRVWKK DRTTIIGKFC
TALLPVNDRE KMVCLPEPVN LQASVTVSRD LNLACV
//
