PA21B_RAT
ID PA21B_RAT Reviewed; 146 AA.
AC P04055;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Phospholipase A2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:17158102};
DE AltName: Full=Group IB phospholipase A2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B;
DE Flags: Precursor;
GN Name=Pla2g1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
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=2909239; DOI=10.1016/0167-4781(89)90141-3;
RA Sakata T., Nakamura E., Tsuruta Y., Tamaki M., Teraoka H., Tojo H., Ono T.,
RA Okamoto M.;
RT "Presence of pancreatic-type phospholipase A2 mRNA in rat gastric mucosa
RT and lung.";
RL Biochim. Biophys. Acta 1007:124-126(1989).
RN [3]
RP PROTEIN SEQUENCE OF 23-54.
RX PubMed=6501264; DOI=10.1093/oxfordjournals.jbchem.a134896;
RA Ono T., Tojo H., Inoue K., Kagamiyama H., Yamano T., Okamoto M.;
RT "Rat pancreatic phospholipase A2: purification, characterization, and N-
RT terminal amino acid sequence.";
RL J. Biochem. 96:785-792(1984).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1420353; DOI=10.1016/0167-4781(92)90133-k;
RA Kanda A., Tamaki M., Nakamura E., Teraoka H., Yoshida N.;
RT "Characterization of recombinant human and rat pancreatic phospholipases A2
RT secreted from Saccharomyces cerevisiae: difference in proteolytic
RT processing.";
RL Biochim. Biophys. Acta 1171:1-10(1992).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14998370; DOI=10.1042/bj20040031;
RA Sun Y.X., Tsuboi K., Okamoto Y., Tonai T., Murakami M., Kudo I., Ueda N.;
RT "Biosynthesis of anandamide and N-palmitoylethanolamine by sequential
RT actions of phospholipase A2 and lysophospholipase D.";
RL Biochem. J. 380:749-756(2004).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17158102; DOI=10.1074/jbc.m606369200;
RA Jin X.H., Okamoto Y., Morishita J., Tsuboi K., Tonai T., Ueda N.;
RT "Discovery and characterization of a Ca2+-independent
RT phosphatidylethanolamine N-acyltransferase generating the anandamide
RT precursor and its congeners.";
RL J. Biol. Chem. 282:3614-3623(2007).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets dietary phospholipids in the intestinal tract (PubMed:1420353,
CC PubMed:17158102). Hydrolyzes the ester bond of the fatty acyl group
CC attached at sn-2 position of phospholipids (phospholipase A2 activity)
CC with preference for phosphatidylethanolamines and phosphatidylglycerols
CC over phosphatidylcholines (PubMed:1420353, PubMed:17158102). May play a
CC role in the biosynthesis of N-acyl ethanolamines that regulate energy
CC metabolism and inflammation in the intestinal tract (PubMed:14998370).
CC Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl
CC lysophosphatidylethanolamines, which are further cleaved by a
CC lysophospholipase D to release N-acyl ethanolamines (PubMed:14998370).
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:Q9Z0Y2, ECO:0000269|PubMed:1420353,
CC ECO:0000269|PubMed:14998370, ECO:0000269|PubMed:17158102}.
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:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC ProRule:PRU10036, ECO:0000269|PubMed:17158102};
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:0000269|PubMed:17158102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000305|PubMed:17158102};
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:0000269|PubMed:17158102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:17158102};
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:0000269|PubMed:17158102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:17158102};
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:0000269|PubMed:1420353};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000305|PubMed:1420353};
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:0000269|PubMed:14998370};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000305|PubMed:14998370};
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:0000269|PubMed:14998370};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000305|PubMed:14998370};
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:0000269|PubMed:14998370};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425;
CC Evidence={ECO:0000305|PubMed:14998370};
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; D00036; BAA00024.1; -; mRNA.
DR PIR; A92008; PSRT.
DR RefSeq; NP_113773.1; NM_031585.1.
DR RefSeq; XP_017453797.1; XM_017598308.1.
DR AlphaFoldDB; P04055; -.
DR SMR; P04055; -.
DR STRING; 10116.ENSRNOP00000001525; -.
DR BindingDB; P04055; -.
DR ChEMBL; CHEMBL5016; -.
DR DrugCentral; P04055; -.
DR SwissLipids; SLP:000001183; -.
DR PaxDb; P04055; -.
DR GeneID; 29526; -.
DR KEGG; rno:29526; -.
DR UCSC; RGD:61949; rat.
DR CTD; 5319; -.
DR RGD; 61949; Pla2g1b.
DR VEuPathDB; HostDB:ENSRNOG00000001153; -.
DR eggNOG; KOG4087; Eukaryota.
DR HOGENOM; CLU_090683_1_1_1; -.
DR InParanoid; P04055; -.
DR OMA; ELDTCCQ; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; P04055; -.
DR TreeFam; TF319283; -.
DR Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-RNO-1482801; Acyl chain remodelling of PS.
DR Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
DR Reactome; R-RNO-1482922; Acyl chain remodelling of PI.
DR Reactome; R-RNO-1482925; Acyl chain remodelling of PG.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR PRO; PR:P04055; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001153; Expressed in stomach and 18 other tissues.
DR Genevisible; P04055; RN.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0032052; F:bile acid binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:RGD.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IDA:BHF-UCL.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:RGD.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:RGD.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:BHF-UCL.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0002227; P:innate immune response in mucosa; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; ISO:RGD.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISO:RGD.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:1904635; P:positive regulation of podocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0046324; P:regulation of glucose import; ISS:BHF-UCL.
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 1: Evidence at protein level;
KW Autocatalytic cleavage; Calcium; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Lipid metabolism; Metal-binding; Phospholipid metabolism;
KW Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..15
FT PROPEP 16..22
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:6501264"
FT /id="PRO_0000022747"
FT CHAIN 23..146
FT /note="Phospholipase A2"
FT /id="PRO_0000022748"
FT ACT_SITE 70
FT ACT_SITE 121
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; 16424 MW; 7EC4F7A491B913D0 CRC64;
MKLLLLAALL TAGVTAHSIS TRAVWQFRNM IKCTIPGSDP LREYNNYGCY CGLGGSGTPV
DDLDRCCQTH DHCYNQAKKL ESCKFLIDNP YTNTYSYKCS GNVITCSDKN NDCESFICNC
DRQAAICFSK VPYNKEYKDL DTKKHC
