ID   PA2BW_PROFL             Reviewed;         138 AA.
AC   Q02517;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Basic phospholipase A2 PL-X';
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 [MRNA].
RC   STRAIN=Tokunoshima; TISSUE=Venom gland;
RX   PubMed=1528861; DOI=10.1073/pnas.89.18.8557;
RA   Ogawa T., Oda N., Nakashima K., Sasaki H., Hattori M., Sakaki Y.,
RA   Kihara H., Ohno M.;
RT   "Unusually high conservation of untranslated sequences in cDNAs for
RT   Trimeresurus flavoviridis phospholipase A2 isozymes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8557-8561(1992).
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 II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; D10721; BAA01564.1; -; mRNA.
DR   AlphaFoldDB; Q02517; -.
DR   SMR; Q02517; -.
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   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Metal-binding; Secreted; Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..138
FT                   /note="Basic phospholipase A2 PL-X'"
FT                   /id="PRO_0000022957"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
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;  15733 MW;  471B01878CCA1ED1 CRC64;
     MRTLWIMAVL LVGVEGHLLQ FRKMIKKMTG KEPIVSYAFY GCYCGKGGRG KPKDATDRCC
     FVHDCCYEKV TGCDPKWDYY TYSSENGDIV CGGDNPCTKE VCECDKAAAI CFRDNLKTYK
     KRYMTFPDIF CTDPTEKC