PA2A_BUNMU
ID PA2A_BUNMU Reviewed; 145 AA.
AC P00606;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Acidic phospholipase A2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Bungarus multicinctus (Many-banded krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=8616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=2388841; DOI=10.1093/nar/18.15.4608;
RA Danse J.-M.;
RT "Nucleotide sequence encoding for non-toxic phospholipase-A2 from Bungarus
RT multicinctus.";
RL Nucleic Acids Res. 18:4608-4608(1990).
RN [2]
RP PROTEIN SEQUENCE OF 28-145.
RC TISSUE=Venom;
RX PubMed=7217037; DOI=10.1093/oxfordjournals.jbchem.a133201;
RA Kondo K., Toda H., Narita K.;
RT "Amino acid sequence of phospholipase A from Bungarus multicinctus venom.";
RL J. Biochem. 89:37-47(1981).
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, ECO:0000255|PROSITE-
CC ProRule:PRU10036};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; X53406; CAA37482.1; -; mRNA.
DR PIR; S10981; PSKF2U.
DR AlphaFoldDB; P00606; -.
DR SMR; P00606; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
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; PS00119; PA2_ASP; 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; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..27
FT /evidence="ECO:0000269|PubMed:7217037"
FT /id="PRO_0000022833"
FT CHAIN 28..145
FT /note="Acidic phospholipase A2"
FT /id="PRO_0000022834"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
FT ACT_SITE 119
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 38..97
FT /evidence="ECO:0000250"
FT DISULFID 52..144
FT /evidence="ECO:0000250"
FT DISULFID 54..70
FT /evidence="ECO:0000250"
FT DISULFID 69..125
FT /evidence="ECO:0000250"
FT DISULFID 76..118
FT /evidence="ECO:0000250"
FT DISULFID 86..111
FT /evidence="ECO:0000250"
FT DISULFID 104..116
FT /evidence="ECO:0000250"
SQ SEQUENCE 145 AA; 15593 MW; F7959376589967CA CRC64;
MNPAHLLILS AVCVSLLGAA NVPPQHLNLY QFKNMIVCAG TRPWIGYVNY GCYCGAGGSG
TPVDELDRCC YVHDNCYGEA EKIPGCNPKT KTYSYTCTKP NLTCTDAAGT CARIVCDCDR
TAAICFAAAP YNINNFMISS STHCQ
