PLA1A_DANRE
ID PLA1A_DANRE Reviewed; 456 AA.
AC Q6NYZ4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Phospholipase A1 member A;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN Name=pla1a; ORFNames=zgc:77160;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes the ester bond at the sn-1 position of
CC glycerophospholipids and produces 2-acyl lysophospholipids. Hydrolyzes
CC phosphatidylserine (PS) in the form of liposomes and 1-acyl-2
CC lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine
CC (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA) or
CC phosphatidylinositol (PI). {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 -!- 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; BC066406; AAH66406.1; -; mRNA.
DR RefSeq; NP_996939.1; NM_207056.1.
DR AlphaFoldDB; Q6NYZ4; -.
DR SMR; Q6NYZ4; -.
DR ESTHER; danre-q6nyz4; Phospholipase.
DR PaxDb; Q6NYZ4; -.
DR GeneID; 334017; -.
DR KEGG; dre:334017; -.
DR CTD; 51365; -.
DR ZFIN; ZDB-GENE-030131-5949; pla1a.
DR InParanoid; Q6NYZ4; -.
DR OrthoDB; 534956at2759; -.
DR Reactome; R-DRE-1482801; Acyl chain remodelling of PS.
DR PRO; PR:Q6NYZ4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; -; 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; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..456
FT /note="Phospholipase A1 member A"
FT /id="PRO_0000273334"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 248..262
FT /evidence="ECO:0000250"
FT DISULFID 286..297
FT /evidence="ECO:0000250"
FT DISULFID 300..308
FT /evidence="ECO:0000250"
SQ SEQUENCE 456 AA; 50476 MW; E660CEC641AF7A65 CRC64;
MAWKWIKAFV YLSVCVTSAL GDDEEASASK CADFNNTTWL EYRQATKLQV QYLLLTRKNA
NCASLFTQDC LNHTQKHTAY FNSSLPTKVI VHGYRALGSK PSWVSGLAQA LLREEDVNVL
VVDWVYGASF AYNLVVENYK EVAVQISVLI NQLTKYGSTL ESFHFIGVSL GAHVSGFVGT
LFHGKLGRIT GLDPAGPMFK SADPFDRLDS SDALFVEAIH TDSDYFGISI PVGHVDFFLN
GGMDQAGCAR SRFASMYGYV ICDHMRALHV YMSALNGSCP LIGFPCSGYE EFLAGKCITC
DDPFNGTCPQ IGLLKNSGIT ATPLPNQEKV YLLTTASGPF CAHHILVELN VSRLDKTAEV
QLILKSIGHP ETELNLKLYT DETRYKTVAA HPEQLCKIDS MQLINTGGRF YRQGDIHFEY
ICISEIPQTR GMDPLCVKNI HIGRGVPWSH DFVQVC
