ID   PA2B1_PROEL             Reviewed;         137 AA.
AC   Q2PG81; Q2PG82;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Basic phospholipase A2 PeBP(R)-I/II;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor;
OS   Protobothrops elegans (Elegant pitviper) (Trimeresurus elegans).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=88086;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-63, AND FUNCTION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=16962627; DOI=10.1016/j.toxicon.2006.06.021;
RA   Chijiwa T., Tokunaga E., Ikeda R., Terada K., Ogawa T., Oda-Ueda N.,
RA   Hattori S., Nozaki M., Ohno M.;
RT   "Discovery of novel [Arg49]phospholipase A2 isozymes from Protobothrops
RT   elegans venom and regional evolution of Crotalinae snake venom
RT   phospholipase A2 isozymes in the southwestern islands of Japan and
RT   Taiwan.";
RL   Toxicon 48:672-682(2006).
CC   -!- FUNCTION: Snake venom phospholipases A2 that have myotoxic, and edema-
CC       inducing activity, as well as extremely weak lipolytic activity. PLA2
CC       catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-
CC       sn-phosphoglycerides. {ECO:0000269|PubMed:16962627}.
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: The sequence shown is that of PeBP(R)-I. PeBP(R)-II
CC       differs at two positions.
CC   -!- MISCELLANEOUS: Does not show hemorrhagic activity.
CC       {ECO:0000305|PubMed:16962627}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       R49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AB219806; BAE72889.1; -; mRNA.
DR   EMBL; AB219807; BAE72890.1; -; mRNA.
DR   AlphaFoldDB; Q2PG81; -.
DR   SMR; Q2PG81; -.
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:InterPro.
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   Direct protein sequencing; Disulfide bond; Hydrolase; Myotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:16962627"
FT   CHAIN           17..137
FT                   /note="Basic phospholipase A2 PeBP(R)-I/II"
FT                   /id="PRO_0000419050"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..131
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..137
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000250"
FT   VARIANT         19
FT                   /note="V -> I (in PeBP(R)-II)"
SQ   SEQUENCE   137 AA;  15486 MW;  CF1E1555B9E7AA97 CRC64;
     MRTLWIMAVL LLGVEGSLVE LWKMVFQETG KEAVKNYGLY GCNCGVGKRG KPVDATDRCC
     FVHRCCYKKV TGCDPKKDRY SYSWENKAIV CGEKNPCLKQ VCECDKAVAI CLRENLGTYN
     KNHRVTVKFL CKAPESC