PA21B_HORSE
ID PA21B_HORSE Reviewed; 132 AA.
AC P00594;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Contains:
DE RecName: Full=Phospholipase A2 isoform 2;
DE Flags: Precursor; Fragment;
GN Name=PLA2G1B;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE OF 1-7.
RC TISSUE=Pancreas;
RX PubMed=849461; DOI=10.1016/0005-2795(77)90062-9;
RA Evenberg A., Meyer H., Verheij H.M., de Haas G.H.;
RT "Isolation and properties of prophospholipase A2 and phospholipase A2 from
RT horse pancreas and horse pancreatic juice.";
RL Biochim. Biophys. Acta 491:265-274(1977).
RN [2]
RP PROTEIN SEQUENCE OF 8-132, AND ACTIVE SITE.
RC TISSUE=Pancreas;
RX PubMed=838712; DOI=10.1016/s0021-9258(17)40639-9;
RA Evenberg A., Meyer H., Gaastra W., Verheij H.M., de Haas G.H.;
RT "Amino acid sequence of phospholipase A2 from horse pancreas.";
RL J. Biol. Chem. 252:1189-1196(1977).
RN [3]
RP SEQUENCE REVISION TO 131-132.
RX PubMed=6349696; DOI=10.1016/0167-4838(83)90126-7;
RA Verheij H.M., Westerman J., Sternby B., de Haas G.H.;
RT "The complete primary structure of phospholipase A2 from human pancreas.";
RL Biochim. Biophys. Acta 747:93-99(1983).
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 PIR; A90615; PSHOA.
DR AlphaFoldDB; P00594; -.
DR SMR; P00594; -.
DR STRING; 9796.ENSECAP00000037604; -.
DR PaxDb; P00594; -.
DR InParanoid; P00594; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032052; F:bile acid binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
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 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; Zymogen.
FT PROPEP 1..7
FT /note="Removed by trypsin"
FT /evidence="ECO:0000269|PubMed:838712"
FT /id="PRO_0000022737"
FT CHAIN 8..132
FT /note="Phospholipase A2"
FT /evidence="ECO:0000269|PubMed:6349696,
FT ECO:0000269|PubMed:838712"
FT /id="PRO_0000022738"
FT CHAIN 10..132
FT /note="Phospholipase A2 isoform 2"
FT /id="PRO_0000045893"
FT ACT_SITE 55
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT ACT_SITE 106
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 18..84
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 34..131
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 36..52
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 51..112
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 58..105
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 68..98
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT DISULFID 91..103
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT NON_TER 1
SQ SEQUENCE 132 AA; 14694 MW; BC6B809A244052EA CRC64;
ENGISPRAVW QFRSMIQCTI PNSKPYLEFN DYGCYCGLGG SGTPVDELDA CCQVHDNCYT
QAKELSSCRF LVDNPYTESY KFSCSGTEVT CSDKNNACEA FICNCDRNAA ICFSKAPYNP
ENKNLDSKRK CA
