PA21B_CANLF
ID PA21B_CANLF Reviewed; 146 AA.
AC P06596;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Phospholipase A2;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055};
DE AltName: Full=Group IB phospholipase A2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B;
DE Flags: Precursor;
GN Name=PLA2G1B;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3754861; DOI=10.1093/oxfordjournals.jbchem.a135532;
RA Ohara O., Tamaki M., Nakamura E., Tsuruta Y., Fujii Y., Shin M.,
RA Teraoka H., Okamoto M.;
RT "Dog and rat pancreatic phospholipases A2: complete amino acid sequences
RT deduced from complementary DNAs.";
RL J. Biochem. 99:733-739(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2142076; DOI=10.1111/j.1432-1033.1990.tb15576.x;
RA Kerfelec B., Laforge K.S., Vasiloudes P., Puigserver A., Scheele G.A.;
RT "Isolation and sequence of the canine pancreatic phospholipase A2 gene.";
RL Eur. J. Biochem. 190:299-304(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3562437; DOI=10.1097/00006676-198609000-00007;
RA Kerfelec B., Laforge K.S., Puigserver A., Scheele G.A.;
RT "Primary structures of canine pancreatic lipase and phospholipase A2
RT messenger RNAs.";
RL Pancreas 1:430-437(1986).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets dietary phospholipids in the intestinal tract. Hydrolyzes the
CC ester bond of the fatty acyl group attached at sn-2 position of
CC phospholipids (phospholipase A2 activity) with preference for
CC phosphatidylethanolamines and phosphatidylglycerols over
CC phosphatidylcholines. May play a role in the biosynthesis of N-acyl
CC ethanolamines that regulate energy metabolism and inflammation in the
CC intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl
CC lysophosphatidylethanolamines, which are further cleaved by a
CC lysophospholipase D to release N-acyl ethanolamines (By similarity).
CC May act in an autocrine and paracrine manner (By similarity). Has anti-
CC helminth activity in a process regulated by gut microbiota. Upon
CC helminth infection of intestinal epithelia, directly affects
CC phosphatidylethanolamine contents in the membrane of helminth larvae,
CC likely controlling an array of phospholipid-mediated cellular processes
CC such as membrane fusion and cell division while providing for better
CC immune recognition, ultimately reducing larvae integrity and
CC infectivity (By similarity). {ECO:0000250|UniProtKB:P04054,
CC ECO:0000250|UniProtKB:P04055, ECO:0000250|UniProtKB:Q9Z0Y2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055,
CC ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC ProRule:PRU10036};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489;
CC Evidence={ECO:0000250|UniProtKB:P04054};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:P04054};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:P04054};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000250|UniProtKB:P04054};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000250|UniProtKB:P04054};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = (9Z,12Z)-octadecadienoate + H(+) +
CC N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425;
CC Evidence={ECO:0000250|UniProtKB:P04055};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P00593};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593};
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000250|UniProtKB:P00592}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}.
CC Note=Secreted from pancreatic acinar cells in its inactive form.
CC {ECO:0000250|UniProtKB:P04054}.
CC -!- PTM: Activated by trypsin cleavage in the duodenum. Can also be
CC activated by thrombin or autocatalytically.
CC {ECO:0000250|UniProtKB:P04054}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; D00035; BAA00023.1; -; mRNA.
DR EMBL; M35301; AAA30883.1; -; mRNA.
DR PIR; S11316; PSDG.
DR RefSeq; NP_001003320.1; NM_001003320.1.
DR AlphaFoldDB; P06596; -.
DR SMR; P06596; -.
DR STRING; 9615.ENSCAFP00000015064; -.
DR PaxDb; P06596; -.
DR Ensembl; ENSCAFT00030043741; ENSCAFP00030038174; ENSCAFG00030023773.
DR Ensembl; ENSCAFT00040036824; ENSCAFP00040032073; ENSCAFG00040019883.
DR Ensembl; ENSCAFT00845052590; ENSCAFP00845041272; ENSCAFG00845029696.
DR GeneID; 404011; -.
DR KEGG; cfa:404011; -.
DR CTD; 5319; -.
DR VEuPathDB; HostDB:ENSCAFG00845029696; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000154885; -.
DR InParanoid; P06596; -.
DR OMA; ELDTCCQ; -.
DR OrthoDB; 1422829at2759; -.
DR TreeFam; TF319283; -.
DR Reactome; R-CFA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-CFA-1482801; Acyl chain remodelling of PS.
DR Reactome; R-CFA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-CFA-1482922; Acyl chain remodelling of PI.
DR Reactome; R-CFA-1482925; Acyl chain remodelling of PG.
DR Reactome; R-CFA-1483166; Synthesis of PA.
DR Proteomes; UP000002254; Chromosome 26.
DR Bgee; ENSCAFG00000010263; Expressed in pancreas and 37 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0032052; F:bile acid binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0019731; P:antibacterial humoral response; IEA:Ensembl.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0002227; P:innate immune response in mucosa; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:Ensembl.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:Ensembl.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IBA:GO_Central.
DR GO; GO:1904635; P:positive regulation of podocyte apoptotic process; ISS:UniProtKB.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 2: Evidence at transcript level;
KW Autocatalytic cleavage; Calcium; Disulfide bond; Hydrolase;
KW Lipid metabolism; Metal-binding; Phospholipid metabolism;
KW Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..15
FT PROPEP 16..22
FT /id="PRO_0000022733"
FT CHAIN 23..146
FT /note="Phospholipase A2"
FT /id="PRO_0000022734"
FT ACT_SITE 70
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT ACT_SITE 121
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 33..99
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 49..146
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 51..67
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 66..127
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 73..120
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 83..113
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 106..118
FT /evidence="ECO:0000250|UniProtKB:P00593"
SQ SEQUENCE 146 AA; 16236 MW; F6258ED9527F3692 CRC64;
MKFLVLAALL TVAAAEGGIS PRAVWQFRNM IKCTIPESDP LKDYNDYGCY CGLGGSGTPV
DELDKCCQTH DHCYSEAKKL DSCKFLLDNP YTKIYSYSCS GSEITCSSKN KDCQAFICNC
DRSAAICFSK APYNKEHKNL DTKKYC
