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PA21B_CAVPO
ID   PA21B_CAVPO             Reviewed;         146 AA.
AC   P43434;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 129.
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   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8344290; DOI=10.1111/j.1432-1033.1993.tb18010.x;
RA   Ying Z., Tojo H., Nonaka Y., Okamoto M.;
RT   "Cloning and expression of phospholipase A2 from guinea pig gastric mucosa,
RT   its induction by carbachol and secretion in vivo.";
RL   Eur. J. Biochem. 215:91-97(1993).
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; D00740; BAA00640.1; -; mRNA.
DR   PIR; S34049; S34049.
DR   RefSeq; XP_003477984.1; XM_003477936.2.
DR   AlphaFoldDB; P43434; -.
DR   SMR; P43434; -.
DR   STRING; 10141.ENSCPOP00000011120; -.
DR   Ensembl; ENSCPOT00000047764; ENSCPOP00000032707; ENSCPOG00000012358.
DR   GeneID; 100732984; -.
DR   KEGG; cpoc:100732984; -.
DR   CTD; 5319; -.
DR   eggNOG; KOG4087; Eukaryota.
DR   GeneTree; ENSGT00940000154885; -.
DR   HOGENOM; CLU_090683_1_1_1; -.
DR   InParanoid; P43434; -.
DR   OMA; ELDTCCQ; -.
DR   OrthoDB; 1422829at2759; -.
DR   TreeFam; TF319283; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
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                   /evidence="ECO:0000250"
FT   PROPEP          16..22
FT                   /note="Activation peptide"
FT                   /id="PRO_0000022735"
FT   CHAIN           23..146
FT                   /note="Phospholipase A2"
FT                   /evidence="ECO:0000269|PubMed:8344290"
FT                   /id="PRO_0000022736"
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"
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;  16187 MW;  760DE6CD11E20E07 CRC64;
     MKLLVLAALL SVSAAAHIIT PRALWQFRDM IKCAIPGSRP YSEYNNYGCF CGLGGSGTPV
     DELDRCCEIH DACYTQAKHL ESCKSVIDNP YTNSYSFSCS GTNIICSSKN KECEEFICNC
     DRAAAICFSK APYNENNKNI NKKERC
 
 
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