ID PLA1A_RAT Reviewed; 456 AA.
AC P97535;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 24-JAN-2024, entry version 140.
DE RecName: Full=Phospholipase A1 member A {ECO:0000305};
DE EC=3.1.1.111 {ECO:0000269|PubMed:8999922};
DE AltName: Full=Phosphatidylserine-specific phospholipase A1;
DE Short=PS-PLA1;
DE Flags: Precursor;
GN Name=Pla1a {ECO:0000312|RGD:621261}; Synonyms=Pspla1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-53; 139-149; 175-194;
RP 279-302; 372-376 AND 401-410, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=Wistar; TISSUE=Platelet;
RX PubMed=8999922; DOI=10.1074/jbc.272.4.2192;
RA Sato T., Aoki J., Nagai Y., Dohmae N., Takio K., Doi T., Arai H., Inoue K.;
RT "Serine phospholipid-specific phospholipase A that is secreted from
RT activated platelets.";
RL J. Biol. Chem. 272:2192-2198(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP FUNCTION.
RX PubMed=11395520; DOI=10.1074/jbc.m104597200;
RA Hosono H., Aoki J., Nagai Y., Bandoh K., Ishida M., Taguchi R., Arai H.,
RA Inoue K.;
RT "Phosphatidylserine-specific phospholipase A1 stimulates histamine release
RT from rat peritoneal mast cells through production of 2-acyl-1-
RT lysophosphatidylserine.";
RL J. Biol. Chem. 276:29664-29670(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 (PubMed:8999922).
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 (PubMed:11395520). Has no activity toward other glycerophospholipids
CC including phosphatidylcholines, phosphatidylethanolamines, phosphatidic
CC acids or phosphatidylinositols, or glycerolipids such as triolein
CC (PubMed:8999922). {ECO:0000269|PubMed:11395520,
CC ECO:0000269|PubMed:8999922}.
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:0000269|PubMed:8999922};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42213;
CC Evidence={ECO:0000305|PubMed:8999922};
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:0000269|PubMed:8999922};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40492;
CC Evidence={ECO:0000305|PubMed:8999922};
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:0000269|PubMed:8999922};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41188;
CC Evidence={ECO:0000305|PubMed:8999922};
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:0000269|PubMed:8999922};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32980;
CC Evidence={ECO:0000305|PubMed:8999922};
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:0000269|PubMed:8999922};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000305|PubMed:8999922};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8999922}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; D88666; BAA13672.1; -; mRNA.
DR EMBL; BC078727; AAH78727.1; -; mRNA.
DR RefSeq; NP_620237.1; NM_138882.1.
DR AlphaFoldDB; P97535; -.
DR SMR; P97535; -.
DR STRING; 10116.ENSRNOP00000071860; -.
DR BindingDB; P97535; -.
DR ChEMBL; CHEMBL2307; -.
DR SwissLipids; SLP:000000649; -.
DR ESTHER; ratno-P97535; Phospholipase.
DR GlyCosmos; P97535; 1 site, No reported glycans.
DR GlyGen; P97535; 1 site.
DR PhosphoSitePlus; P97535; -.
DR PaxDb; 10116-ENSRNOP00000035788; -.
DR Ensembl; ENSRNOT00000077727.2; ENSRNOP00000071860.1; ENSRNOG00000057153.2.
DR Ensembl; ENSRNOT00055027609; ENSRNOP00055022152; ENSRNOG00055016283.
DR Ensembl; ENSRNOT00060013018; ENSRNOP00060009877; ENSRNOG00060007899.
DR Ensembl; ENSRNOT00065032226; ENSRNOP00065025734; ENSRNOG00065019164.
DR GeneID; 85311; -.
DR KEGG; rno:85311; -.
DR UCSC; RGD:621261; rat.
DR AGR; RGD:621261; -.
DR CTD; 51365; -.
DR RGD; 621261; Pla1a.
DR eggNOG; ENOG502QQQP; Eukaryota.
DR GeneTree; ENSGT00940000159279; -.
DR HOGENOM; CLU_027171_3_1_1; -.
DR InParanoid; P97535; -.
DR OMA; AHANPQC; -.
DR OrthoDB; 3428256at2759; -.
DR PhylomeDB; P97535; -.
DR TreeFam; TF324997; -.
DR BRENDA; 3.1.1.111; 5301.
DR Reactome; R-RNO-1482801; Acyl chain remodelling of PS.
DR PRO; PR:P97535; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000057153; Expressed in stomach and 18 other cell types or tissues.
DR Genevisible; P97535; RN.
DR GO; GO:0002080; C:acrosomal membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0008970; F:phospholipase A1 activity; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; LIPASE; 1.
DR PANTHER; PTHR11610:SF111; PHOSPHOLIPASE A1 MEMBER A; 1.
DR Pfam; PF00151; Lipase; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:8999922"
FT CHAIN 25..456
FT /note="Phospholipase A1 member A"
FT /id="PRO_0000273333"
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 30
FT /note="T -> P (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="C -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="C -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 50202 MW; 0FE091FE165C2879 CRC64;
MCPGLWGTCF WLWGSLLWLS IGRSGNVPPT TQPKCTDFQS ANLLRGTNLK VQFLLFTPSD
PGCGQLVEED SDIRNSEFNA SLGTKLIIHG FRALGTKPSW INKFIRALLR AADANVIAVD
WVYGSTGMYF SAVENVVKLS LEISRFLSKL LELGVSESSI HIIGVSLGAH VGGMVGHFYK
GQLGRITGLD PAGPEYTRAS LEERLDSGDA LFVEAIHTDT DNLGIRIPVG HVDYFVNGGQ
DQPGCPAFIH AGYSYLICDH MRAVHLYISA LENTCPLMAF PCASYKAFLA GDCLDCFNPF
LLSCPRIGLV ERGGVKIEPL PKEVRVYLQT TSSAPYCVHH SLVEFNLKEK RKKDTSIEVT
FLGNNVTSSV KITIPKDHLE GRGIIAHQNP HCQINQVKLK FHISSRVWRK DRTPIVGTFC
TAPLPVNDSK KTVCIPEPVR LQVSMAVLRD LKMACV
//
