PA2G3_BOVIN
ID PA2G3_BOVIN Reviewed; 501 AA.
AC Q1JPB9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Group 3 secretory phospholipase A2;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q9NZ20};
DE AltName: Full=Group III secretory phospholipase A2;
DE Short=GIII sPLA2;
DE Short=sPLA2-III;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 3;
DE Flags: Precursor;
GN Name=PLA2G3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids. Hydrolyzes the ester bond of the
CC fatty acyl group attached at sn-2 position of phospholipids without
CC apparent head group selectivity (By similarity). Contributes to
CC phospholipid remodeling of low-density lipoprotein (LDL) and high-
CC density lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids
CC releasing unsaturated fatty acids that regulate macrophage
CC differentiation toward foam cells (By similarity). May act in an
CC autocrine and paracrine manner. Secreted by immature mast cells, acts
CC on nearby fibroblasts upstream to PTDGS to synthesize prostaglandin D2
CC (PGD2), which in turn promotes mast cell maturation and degranulation
CC via PTGDR (By similarity). Secreted by epididymal epithelium, acts on
CC immature sperm cells within the duct, modulating the degree of
CC unsaturation of the fatty acyl components of phosphatidylcholines
CC required for acrosome assembly and sperm cell motility. Facilitates the
CC replacement of fatty acyl chains in phosphatidylcholines in sperm
CC membranes from omega-6 and omega-9 to omega-3 polyunsaturated fatty
CC acids (PUFAs). Coupled to lipoxygenase pathway, may process omega-6
CC PUFAs to generate oxygenated lipid mediators in the male reproductive
CC tract (By similarity). At pericentrosomal preciliary compartment,
CC negatively regulates ciliogenesis likely by regulating endocytotic
CC recycling of ciliary membrane protein (By similarity). Coupled to
CC cyclooxygenase pathway provides arachidonate to generate prostaglandin
CC E2 (PGE2), a potent immunomodulatory lipid in inflammation and
CC tumorigenesis (By similarity). At colonic epithelial barrier,
CC preferentially hydrolyzes phospholipids having arachidonate and
CC docosahexaenoate at sn-2 position, contributing to the generation of
CC oxygenated metabolites involved in colonic stem cell homeostasis (By
CC similarity). Releases C16:0 and C18:0 lysophosphatidylcholine
CC subclasses from neuron plasma membranes and promotes neurite outgrowth
CC and neuron survival (By similarity). {ECO:0000250|UniProtKB:Q8BZT7,
CC ECO:0000250|UniProtKB:Q9NZ20}.
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:Q9NZ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ20};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ20};
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:Q9NZ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ20};
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:Q9NZ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ20};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ20};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P00630};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P00630};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9NZ20}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9NZ20}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q9NZ20}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9NZ20}. Note=Localized at pericentrosomal
CC preciliary compartment. {ECO:0000250|UniProtKB:Q9NZ20}.
CC -!- DOMAIN: The phospholipase A2-like domain represents the fully processed
CC form after N- and C-termini are cleaved off. It is the secreted mature
CC form found in biological fluids. {ECO:0000250|UniProtKB:Q9NZ20}.
CC -!- PTM: N-glycosylation does not affect the catalytic activity, but is
CC required for proper secretion. A nonglycosylated form was observed in
CC several cell types. {ECO:0000250|UniProtKB:Q9NZ20}.
CC -!- PTM: In several cell types, the N- and C-termini are cleaved off.
CC {ECO:0000250|UniProtKB:Q9NZ20}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; BT025434; ABF57390.1; -; mRNA.
DR AlphaFoldDB; Q1JPB9; -.
DR SMR; Q1JPB9; -.
DR Allergome; 9634; Bos d PLA2.
DR PRIDE; Q1JPB9; -.
DR InParanoid; Q1JPB9; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISS:UniProtKB.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISS:UniProtKB.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; ISS:UniProtKB.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:2001135; P:regulation of endocytic recycling; ISS:UniProtKB.
DR Gene3D; 1.20.90.10; -; 2.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR Pfam; PF05826; Phospholip_A2_2; 1.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 2.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Disulfide bond; Endosome; Glycoprotein; Hydrolase;
KW Lipid metabolism; Mast cell degranulation; Membrane; Metal-binding;
KW Phospholipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..501
FT /note="Group 3 secretory phospholipase A2"
FT /id="PRO_0000289139"
FT REGION 119..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..291
FT /note="Phospholipase A2-like"
FT REGION 284..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 214
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 159..181
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 180..220
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 187..213
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 211..244
FT /evidence="ECO:0000250|UniProtKB:P00630"
SQ SEQUENCE 501 AA; 55376 MW; BDA39AB12205D036 CRC64;
MGVLVVLLGV LSFLGRTLGG SPALHWDSTS CHLARPIPGR PLRSLSFLGK DAQGLALFHA
HWDGHGRLQV CSRQDEPELT AAYGALCAGE ITRGSFIHTP GPELQRALAT LQSQWEACRG
PAESPAGTRE KRAAGQNGVP GIGRQWVKRG WTVPGTLWCG VGDSAGNSSE LGVFQGPDLC
CREHDRCPHN VSPFQYNYGI RNYRFHTISH CNCDARFQQC LQDQRDSVSD IMGVAFFNVL
AIPCFVLEEQ EACVEWYWWG GCRRYGSVPF ARLQPRTFYN ASWSSPATSL TPSPQNPALS
RPQPMQHPQQ WPSEWKESKS PSKTNATALQ APVASPGSDR ASTVQLEVTH PGFQGTTGGR
KPPGAHRACR SFRHLDQCEH QIGPQETKFQ LFNSAHEPLF HCNCTRRLAR FLRLHGPPVG
ASMLWELPGM TCFKLAPPLD CAEGKGCPRD PRAFKVSARH LLRLQQRRLQ LQGTGTDNGQ
VWPSEDQGAP ISFYNRCLQL T
