ID   PA2BX_PROFL             Reviewed;         122 AA.
AC   P06860;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Basic phospholipase A2 PL-X;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
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   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=3564060; DOI=10.1016/0041-0101(86)90138-8;
RA   Kini R.M., Kawabata S., Iwanaga S.;
RT   "Comparison of amino terminal region of three isoenzymes of phospholipases
RT   A2 (TFV PL-Ia, TFV PL-Ib, TFV PL-X) from Trimeresurus flavoviridis (habu
RT   snake) venom and the complete amino acid sequence of the basic
RT   phospholipase, TFV PL-X.";
RL   Toxicon 24:1117-1129(1986).
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. {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   PIR; A25500; PSTVXF.
DR   AlphaFoldDB; P06860; -.
DR   SMR; P06860; -.
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; 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; 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; Toxin.
FT   CHAIN           1..122
FT                   /note="Basic phospholipase A2 PL-X"
FT                   /id="PRO_0000161701"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   BINDING         31
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   BINDING         48
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        26..115
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        43..95
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        49..122
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        50..88
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        57..81
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000250|UniProtKB:O42187"
SQ   SEQUENCE   122 AA;  13981 MW;  A9D652276C5D0DF0 CRC64;
     HLLQFRKMIK KMTGKEPIVS YAFYGCYCGK GGRGKPKDAT DRCCFVHDCC YEKVTGCDPK
     WSYYTYSLEN GDIVCGGDPY CTKVKCECDK KAAICFRDNL KTYKNRYMTF PDIFCTDPTE
     GC