PLA1A_MOUSE
ID PLA1A_MOUSE Reviewed; 456 AA.
AC Q8VI78; E9QN71; Q99J51;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Phospholipase A1 member A {ECO:0000305};
DE EC=3.1.1.111 {ECO:0000250|UniProtKB:P97535};
DE AltName: Full=Phosphatidylserine-specific phospholipase A1;
DE Short=PS-PLA1;
DE Flags: Precursor;
GN Name=Pla1a {ECO:0000312|MGI:MGI:1934677}; Synonyms=Pspla1;
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].
RA Nagai Y., Aoki J., Amano K., Okamoto M., Taya C., Matsuda Y., Yonekawa H.,
RA Inoue K.;
RT "Molecular cloning and chromosomal mapping of PS-PLA1.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION.
RX PubMed=11210182; DOI=10.1007/s003350010256;
RA Wen X.-Y., Stewart A.K., Skaug J., Wei E., Tsui L.-C.;
RT "Murine phosphatidylserine-specific phospholipase A1 (Ps-pla1) maps to
RT chromosome 16 but is distinct from the lpd (lipid defect) locus.";
RL Mamm. Genome 12:129-132(2001).
CC -!- FUNCTION: Hydrolyzes the ester bond of the acyl group attached at the
CC sn-1 position of phosphatidylserines (phospholipase A1 activity) and 1-
CC acyl-2-lysophosphatidylserines (lysophospholipase activity) in the
CC pathway of phosphatidylserines acyl chain remodeling (By similarity).
CC Cleaves phosphatidylserines exposed on the outer leaflet of the plasma
CC membrane of apoptotic cells producing 2-acyl-1-lysophosphatidylserines,
CC which in turn enhance mast cell activation and histamine production.
CC Has no activity toward other glycerophospholipids including
CC phosphatidylcholines, phosphatidylethanolamines, phosphatidic acids or
CC phosphatidylinositols, or glycerolipids such as triolein (By
CC similarity). {ECO:0000250|UniProtKB:P97535,
CC ECO:0000250|UniProtKB:Q53H76}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-
CC sn-glycero-3-phospho-L-serine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:42212, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57262, ChEBI:CHEBI:65214;
CC EC=3.1.1.111; Evidence={ECO:0000250|UniProtKB:P97535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42213;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + H(+); Xref=Rhea:RHEA:40491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74905,
CC ChEBI:CHEBI:77342; Evidence={ECO:0000250|UniProtKB:P97535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40492;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phospho-L-serine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phospho-L-serine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41187, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:75032, ChEBI:CHEBI:77830;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41188;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + H2O = a fatty acid +
CC H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:32979,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:64379, ChEBI:CHEBI:64765; EC=3.1.1.111;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32980;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P97535}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AF063498; AAL55475.1; -; mRNA.
DR EMBL; AC154809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAAA01219438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT571259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003470; AAH03470.1; -; mRNA.
DR EMBL; BC030670; AAH30670.1; -; mRNA.
DR CCDS; CCDS28166.1; -.
DR RefSeq; NP_598863.3; NM_134102.4.
DR RefSeq; XP_006522834.1; XM_006522771.1.
DR RefSeq; XP_006522835.1; XM_006522772.1.
DR AlphaFoldDB; Q8VI78; -.
DR SMR; Q8VI78; -.
DR STRING; 10090.ENSMUSP00000002926; -.
DR ESTHER; mouse-psplip; Phospholipase.
DR GlyGen; Q8VI78; 1 site.
DR PhosphoSitePlus; Q8VI78; -.
DR MaxQB; Q8VI78; -.
DR PaxDb; Q8VI78; -.
DR PeptideAtlas; Q8VI78; -.
DR PRIDE; Q8VI78; -.
DR ProteomicsDB; 289610; -.
DR Antibodypedia; 32751; 234 antibodies from 28 providers.
DR DNASU; 85031; -.
DR Ensembl; ENSMUST00000002926; ENSMUSP00000002926; ENSMUSG00000002847.
DR GeneID; 85031; -.
DR KEGG; mmu:85031; -.
DR UCSC; uc007zew.1; mouse.
DR CTD; 51365; -.
DR MGI; MGI:1934677; Pla1a.
DR VEuPathDB; HostDB:ENSMUSG00000002847; -.
DR eggNOG; ENOG502QQQP; Eukaryota.
DR GeneTree; ENSGT00940000159279; -.
DR HOGENOM; CLU_027171_3_1_1; -.
DR InParanoid; Q8VI78; -.
DR OMA; HTDADNF; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; Q8VI78; -.
DR TreeFam; TF324997; -.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR BioGRID-ORCS; 85031; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Pla1a; mouse.
DR PRO; PR:Q8VI78; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8VI78; protein.
DR Bgee; ENSMUSG00000002847; Expressed in left lobe of liver and 95 other tissues.
DR Genevisible; Q8VI78; MM.
DR GO; GO:0002080; C:acrosomal membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR016272; Lipase_LIPH.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..456
FT /note="Phospholipase A1 member A"
FT /id="PRO_0000273331"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 245..258
FT /evidence="ECO:0000250"
FT DISULFID 282..293
FT /evidence="ECO:0000250"
FT DISULFID 296..304
FT /evidence="ECO:0000250"
FT CONFLICT 83
FT /note="G -> R (in Ref. 3; AAH03470/AAH30670)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="V -> R (in Ref. 1; AAL55475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 49984 MW; 2A476BEE006514A3 CRC64;
MRPGLWETCF WLWGPLLWLS IGSSGNVPPT TQPKCTDFQS ANLLRGTNLK VQFLLFTPSD
PSCGQLVEEG SDIRSSEFNA SLGTKVIIHG FRALGTKPSW IDKFISAVLR AADANVIAVD
WVYGSTGVYY SAVENVVKLS LEISRFLSKL LELGVSESSI HIIGVSLGAH VGGMVGHFYK
GQLGQITGLD PAGPEYTRAS LEERLDAGDA LFVEAIHTDT DNLGIRIPVG HVDYFVNGGQ
DQPGCPAFFH AGYNYLICDH MRAVHLYISA LENTCPLMAF PCASYKAFLA GDCLDCFNPF
LLSCPRIGLV ERGGVMIEPL PKEVKVYLLT TSSAPYCVHH SLVEFYLKEK RKKDTSIEVT
FLSNNVTSSV KITIPKQQLE GRGVMAHPNP QCQINQVKLK FQVSSRVWRK DRTPVVGTFC
TAPLPVNDSK KTVCIPEPVR LQAGVPAFQD LKIACV
