ID   PA2H1_BOTDP             Reviewed;          68 AA.
AC   P0DUP0;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Basic phospholipase A2 homolog BdipTx-I {ECO:0000303|PubMed:29170054};
DE            Short=svPLA2 homolog;
DE   Flags: Fragment;
OS   Bothrops diporus (Chaco lancehead) (Bothrops neuwiedi diporus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=1107943;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=29170054; DOI=10.1016/j.toxicon.2017.11.007;
RA   Teixera L.F., de Carvalho L.H., de Castro O.B., Bastos J.S.F., Nery N.M.,
RA   Oliveira G.A., Kayano A.M., Soares A.M., Zuliani J.P.;
RT   "Local and systemic effects of BdipTX-I, a Lys-49 phospholipase A2 isolated
RT   from Bothrops diporus snake venom.";
RL   Toxicon 141:55-64(2018).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that lacks enzymatic
CC       activity. Is myotoxic, induces edema, and causes systemic effects
CC       (renal changes that lead to proteinuria) on mice (PubMed:29170054). A
CC       model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is
CC       activated by the entrance of a hydrophobic molecule (e.g. fatty acid)
CC       at the hydrophobic channel of the protein leading to a reorientation of
CC       a monomer (By similarity). This reorientation causes a transition
CC       between 'inactive' to 'active' states, causing alignment of C-terminal
CC       and membrane-docking sites (MDoS) side-by-side and putting the
CC       membrane-disruption sites (MDiS) in the same plane, exposed to solvent
CC       and in a symmetric position for both monomers (By similarity). The MDoS
CC       region stabilizes the toxin on membrane by the interaction of charged
CC       residues with phospholipid head groups (By similarity). Subsequently,
CC       the MDiS region destabilizes the membrane with penetration of
CC       hydrophobic residues (By similarity). This insertion causes a
CC       disorganization of the membrane, allowing an uncontrolled influx of
CC       ions (i.e. calcium and sodium), and eventually triggering irreversible
CC       intracellular alterations and cell death (By similarity).
CC       {ECO:0000250|UniProtKB:I6L8L6, ECO:0000269|PubMed:29170054}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29170054}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29170054}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       K49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: Does not bind calcium as one of the calcium-binding sites is
CC       lost (Asp->Lys in position 48, which corresponds to 'Lys-49' in the
CC       current nomenclature). {ECO:0000305}.
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DR   AlphaFoldDB; P0DUP0; -.
DR   SMR; P0DUP0; -.
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:InterPro.
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   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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Myotoxin; Secreted; Toxin.
FT   CHAIN           1..>68
FT                   /note="Basic phospholipase A2 homolog BdipTx-I"
FT                   /evidence="ECO:0000269|PubMed:29170054"
FT                   /id="PRO_0000452901"
FT   DISULFID        26..?
FT                   /evidence="ECO:0000250|UniProtKB:Q90249"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000250|UniProtKB:Q90249"
FT   DISULFID        43..?
FT                   /evidence="ECO:0000250|UniProtKB:Q90249"
FT   DISULFID        49..?
FT                   /evidence="ECO:0000250|UniProtKB:Q90249"
FT   DISULFID        50..?
FT                   /evidence="ECO:0000250|UniProtKB:Q90249"
FT   DISULFID        57..?
FT                   /evidence="ECO:0000250|UniProtKB:Q90249"
FT   NON_TER         68
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   68 AA;  7663 MW;  4C74C0EF65D19364 CRC64;
     SLFELGKMIL QETGKNPAKS YGAYGCNCGV LGRGKPKEAT QRCCYVHKCC YKKLTGCDPK
     KDRYSYSW