PA2A2_HELSU
ID PA2A2_HELSU Reviewed; 142 AA.
AC P80003; P80006;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Acidic phospholipase A2 PA4;
DE Short=PLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Contains:
DE RecName: Full=Acidic phospholipase A2 PA2;
OS Heloderma suspectum (Gila monster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Anguimorpha; Neoanguimorpha; Helodermatidae; Heloderma.
OX NCBI_TaxID=8554;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=2013276; DOI=10.1111/j.1432-1033.1991.tb15847.x;
RA Vandermeers A., Vandermeers-Piret M.-C., Vigneron L., Rathe J.,
RA Stievenart M., Christophe J.;
RT "Differences in primary structure among five phospholipases A2 from
RT Heloderma suspectum.";
RL Eur. J. Biochem. 196:537-544(1991).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC subfamily. {ECO:0000305}.
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DR PIR; S25093; S25093.
DR AlphaFoldDB; P80003; -.
DR SMR; P80003; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.90.10; -; 1.
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; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Secreted.
FT CHAIN 1..142
FT /note="Acidic phospholipase A2 PA4"
FT /id="PRO_0000045885"
FT CHAIN 1..141
FT /note="Acidic phospholipase A2 PA2"
FT /id="PRO_0000045886"
FT ACT_SITE 36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 11..33
FT /evidence="ECO:0000250"
FT DISULFID 32..72
FT /evidence="ECO:0000250"
FT DISULFID 39..65
FT /evidence="ECO:0000250"
SQ SEQUENCE 142 AA; 15640 MW; 9B79D5F5CD775E3B CRC64;
GAFIMPGTLW CGAGNAASDY SQLGTEKDTD MCCRDHDHCS DTMAALEYKH GMRNYRPHTV
SHCDCDNQFR SCLMNVKDRT ADLVGMTYFT VLKISCFELE EGEGCVDNNF SQQCTKSEIM
PVAKLVSAAP YQAQAETQSG EG
