PLA1A_BOVIN
ID PLA1A_BOVIN Reviewed; 456 AA.
AC Q5E9H0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Phospholipase A1 member A;
DE EC=3.1.1.111 {ECO:0000250|UniProtKB:P97535};
DE Flags: Precursor;
GN Name=PLA1A;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; BT020950; AAX08967.1; -; mRNA.
DR EMBL; BC112606; AAI12607.1; -; mRNA.
DR RefSeq; NP_001015610.1; NM_001015610.1.
DR AlphaFoldDB; Q5E9H0; -.
DR SMR; Q5E9H0; -.
DR STRING; 9913.ENSBTAP00000012361; -.
DR ESTHER; bovin-q5e9h0; Phospholipase.
DR PaxDb; Q5E9H0; -.
DR PRIDE; Q5E9H0; -.
DR GeneID; 515900; -.
DR KEGG; bta:515900; -.
DR CTD; 51365; -.
DR eggNOG; ENOG502QQQP; Eukaryota.
DR HOGENOM; CLU_027171_3_1_1; -.
DR InParanoid; Q5E9H0; -.
DR OrthoDB; 534956at2759; -.
DR TreeFam; TF324997; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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.
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 /evidence="ECO:0000255"
FT /id="PRO_0000273329"
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 34
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"
SQ SEQUENCE 456 AA; 50121 MW; CE1E056D7673DBF0 CRC64;
MPPDFWERCF WLWGLLLWLS VGSTGDAPPT PQTNCTDFQN ANLLRGTNLK VQFLLFTPLD
PSCGQLVEES SDIQNSGFNA TLGTKLVIHG FRALGTKPSW IDRFIDALLR AADANVIAVD
WVYGSTAAYF SAVENVIKLG LEISRFLRKL LALGVSESSI HIIGISLGAH VGGMVGHFYN
GQLGQITGLD PAGPEYTRAS LEERLDPGDA LFVEAIHTDT DNLGIRIPVG HVDYFINGGQ
DQPGCPTSIY AGYSYLICDH MRAVHLYISA LENSCPLVAF PCTNYKDFLA GQCLDCFNPF
LLSCPRIGLV EQGGVKIEPL PKEVKVYLLT TSMAPYCVHH SLVEFHLQEP RNKDTCITVT
FLSSSVTSSV KITIPRHQRV GKGVLAHPSP QCQINQVKLK LQASHRVWKK DQTTIIGRFC
TAPLPVNDNK KMVCLPEPVN LQASETVSHD LKITCI
