PA2GF_MOUSE
ID PA2GF_MOUSE Reviewed; 168 AA.
AC Q9QZT4; Q8CE14;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Group IIF secretory phospholipase A2 {ECO:0000303|PubMed:11877435};
DE Short=GIIF sPLA2;
DE Short=sPLA2-IIF;
DE EC=3.1.1.4 {ECO:0000269|PubMed:11877435};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 2F;
DE Flags: Precursor;
GN Name=Pla2g2f;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10531313; DOI=10.1074/jbc.274.44.31195;
RA Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., Lambeau G.;
RT "On the diversity of secreted phospholipases A2. Cloning, tissue
RT distribution, and functional expression of two novel mouse group II
RT enzymes.";
RL J. Biol. Chem. 274:31195-31202(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF GLY-49 AND CYS-157, AND INDUCTION BY LPS.
RX PubMed=11877435; DOI=10.1074/jbc.m112385200;
RA Murakami M., Yoshihara K., Shimbara S., Lambeau G., Gelb M.H., Singer A.G.,
RA Sawada M., Inagaki N., Nagai H., Ishihara M., Ishikawa Y., Ishii T.,
RA Kudo I.;
RT "Cellular arachidonate-releasing function and inflammation-associated
RT expression of group IIF secretory phospholipase A2.";
RL J. Biol. Chem. 277:19145-19155(2002).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids (PubMed:10531313). Hydrolyzes the
CC ester bond of the fatty acyl group attached at the sn-2 position of
CC phospholipids (phospholipase A2 activity), the catalytic efficiency
CC decreasing in the following order: phosphatidylglycerols >
CC phosphatidylethanolamines > phosphatidylcholines > phosphatidylserines
CC (PubMed:11877435, PubMed:10531313). May play a role in lipid mediator
CC production in inflammatory conditions, by providing arachidonic acid to
CC downstream cyclooxygenases and lipoxygenases (PubMed:10531313).
CC {ECO:0000269|PubMed:10531313, ECO:0000269|PubMed:11877435}.
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,
CC ECO:0000269|PubMed:11877435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:11877435};
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:Q9BZM2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000250|UniProtKB:Q9BZM2};
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:11877435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000305|PubMed:11877435};
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:0000269|PubMed:11877435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000305|PubMed:11877435};
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:Q9BZM2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:Q9BZM2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phospho-L-serine + H(+); Xref=Rhea:RHEA:41752, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75020,
CC ChEBI:CHEBI:75029; Evidence={ECO:0000250|UniProtKB:Q9BZM2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41753;
CC Evidence={ECO:0000250|UniProtKB:Q9BZM2};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9BZM2};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9BZM2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:10531313,
CC ECO:0000269|PubMed:11877435};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11877435}. Cell
CC membrane; Peripheral membrane protein {ECO:0000269|PubMed:11877435}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QZT4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QZT4-2; Sequence=VSP_037525;
CC -!- TISSUE SPECIFICITY: Strongly expressed in testis.
CC {ECO:0000269|PubMed:10531313}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed during embryogenesis.
CC {ECO:0000269|PubMed:10531313}.
CC -!- INDUCTION: Strongly up-regulated by lipopolysaccharide (LPS) in brain,
CC heart, liver, colon and testis. {ECO:0000269|PubMed:11877435}.
CC -!- MISCELLANEOUS: [Isoform 2]: No signal peptide could be predicted in
CC this isoform, challenging its subcellular location within the secretory
CC pathway and hence the formation of disulfide bonds, which are required
CC for its activity. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AF166099; AAF04500.2; -; mRNA.
DR EMBL; AK029254; BAC26357.1; -; mRNA.
DR EMBL; AL844178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125567; AAI25568.1; -; mRNA.
DR CCDS; CCDS18832.1; -. [Q9QZT4-2]
DR RefSeq; NP_036175.2; NM_012045.4. [Q9QZT4-2]
DR AlphaFoldDB; Q9QZT4; -.
DR SMR; Q9QZT4; -.
DR STRING; 10090.ENSMUSP00000030526; -.
DR BindingDB; Q9QZT4; -.
DR ChEMBL; CHEMBL5361; -.
DR GlyGen; Q9QZT4; 3 sites.
DR iPTMnet; Q9QZT4; -.
DR PhosphoSitePlus; Q9QZT4; -.
DR PaxDb; Q9QZT4; -.
DR PRIDE; Q9QZT4; -.
DR ProteomicsDB; 294321; -. [Q9QZT4-1]
DR ProteomicsDB; 294322; -. [Q9QZT4-2]
DR Antibodypedia; 68368; 5 antibodies from 3 providers.
DR DNASU; 26971; -.
DR Ensembl; ENSMUST00000030526; ENSMUSP00000030526; ENSMUSG00000028749. [Q9QZT4-2]
DR GeneID; 26971; -.
DR KEGG; mmu:26971; -.
DR UCSC; uc008vlf.2; mouse. [Q9QZT4-2]
DR CTD; 64600; -.
DR MGI; MGI:1349661; Pla2g2f.
DR VEuPathDB; HostDB:ENSMUSG00000028749; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000161819; -.
DR HOGENOM; CLU_090683_2_0_1; -.
DR InParanoid; Q9QZT4; -.
DR OMA; ETECDKQ; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; Q9QZT4; -.
DR TreeFam; TF319283; -.
DR BRENDA; 3.1.1.4; 3474.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR BioGRID-ORCS; 26971; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Pla2g2f; mouse.
DR PRO; PR:Q9QZT4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9QZT4; protein.
DR Bgee; ENSMUSG00000028749; Expressed in lip and 62 other tissues.
DR Genevisible; Q9QZT4; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:MGI.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IMP:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:MGI.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:MGI.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
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; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Immunity; Innate immunity; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..168
FT /note="Group IIF secretory phospholipase A2"
FT /id="PRO_0000022760"
FT REGION 139..168
FT /note="Required for localization on the plasma membrane"
FT /evidence="ECO:0000269|PubMed:11877435"
FT ACT_SITE 67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..138
FT /evidence="ECO:0000250"
FT DISULFID 48..64
FT /evidence="ECO:0000250"
FT DISULFID 63..120
FT /evidence="ECO:0000250"
FT DISULFID 69..145
FT /evidence="ECO:0000250"
FT DISULFID 70..113
FT /evidence="ECO:0000250"
FT DISULFID 79..106
FT /evidence="ECO:0000250"
FT DISULFID 98..111
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MADGAQANPKGFRKKALVKHSTGRKSPSLRASPSKTSRSSLGM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_037525"
FT MUTAGEN 49
FT /note="G->S: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:11877435"
FT MUTAGEN 157
FT /note="C->S: No effect on lipase activity toward 1-
FT palmitoyl-2-arachidonoyl-phosphatidylethanolamine (2-AA-
FT PE)."
FT /evidence="ECO:0000269|PubMed:11877435"
SQ SEQUENCE 168 AA; 18880 MW; 9E15FB6AC0F5450C CRC64;
MKKFFAIAVL AGSVVTTAHS SLLNLKSMVE AITHRNSILS FVGYGCYCGL GGRGHPMDEV
DWCCHAHDCC YEKLFEQGCR PYVDHYDHRI ENGTMIVCTE LNETECDKQT CECDKSLTLC
LKDHPYRNKY RGYFNVYCQG PTPNCSIYDP YPEEVTCGHG LPATPVST
