ID   PA2AP_PROFL             Reviewed;         138 AA.
AC   Q92147;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Acidic phospholipase A2 pgPLA 1b/pgPLA 2b;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor;
OS   Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=88087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=7765285; DOI=10.1271/bbb.58.1510;
RA   Nakashima K., Nobuhisa I., Ogawa T., Hattori M., Sakaki Y., Kihara H.,
RA   Ohno M.;
RT   "Polymorphisms of Trimeresurus flavoviridis venom gland phospholipase A2
RT   isozyme genes.";
RL   Biosci. Biotechnol. Biochem. 58:1510-1511(1994).
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 {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; D10723; BAA01566.1; -; Genomic_DNA.
DR   EMBL; D10725; BAA01568.1; -; Genomic_DNA.
DR   PIR; C48188; F48188.
DR   AlphaFoldDB; Q92147; -.
DR   SMR; Q92147; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Calcium; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Metal-binding; Secreted; Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000250"
FT   CHAIN           17..138
FT                   /note="Acidic phospholipase A2 pgPLA 1b/pgPLA 2b"
FT                   /id="PRO_0000022955"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000250|UniProtKB:P06859"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000250|UniProtKB:P06859"
FT   BINDING         43
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   BINDING         45
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        42..131
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        59..111
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        65..138
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        66..104
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        73..97
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
SQ   SEQUENCE   138 AA;  15708 MW;  AAD7DC04A6EDA975 CRC64;
     MRTLWIMAVL LVGVKGHLMQ FENMIKKVTG RSGIWWYGSY GCYCGKGGEG RPQDPSDRCC
     FVHDCCYGKV TGCDPKDDFY IYSSENGDIV CGDDDLCKKE VCECDKAAAI CFRDNMDTYQ
     NKYWFYPASN CKEESEPC