ID   PA2H2_BOTMT             Reviewed;          28 AA.
AC   P0DMK0;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Basic phospholipase A2 homolog BmatTX-II {ECO:0000303|PubMed:24724078};
DE            Short=svPLA2 homolog;
DE   AltName: Full=Lys49 PLA2-like;
DE   Flags: Fragment;
OS   Bothrops matogrossensis (Pitviper) (Bothrops neuwiedi matogrossensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=1171125;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=24724078; DOI=10.1155/2014/195356;
RA   de Moura A.A., Kayano A.M., Oliveira G.A., Setubal S.S., Ribeiro J.G.,
RA   Barros N.B., Nicolete R., Moura L.A., Fuly A.L., Nomizo A., da Silva S.L.,
RA   Fernandes C.F., Zuliani J.P., Stabeli R.G., Soares A.M., Calderon L.A.;
RT   "Purification and biochemical characterization of three myotoxins from
RT   Bothrops mattogrossensis snake venom with toxicity against Leishmania and
RT   tumor cells.";
RL   Biomed. Res. Int. 2014:1-13(2014).
CC   -!- FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic
CC       activity (PubMed:24724078). Shows high myotoxic activity, neutrophil
CC       activation (demonstrated by activation induction of IL-1beta
CC       production), and slight cytotoxicity against tumor cell lines (T
CC       leukemia and breast adenocarcinoma) (PubMed:24724078). A model of
CC       myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by
CC       the entrance of a hydrophobic molecule (e.g. fatty acid) at the
CC       hydrophobic channel of the protein leading to a reorientation of a
CC       monomer (By similarity). This reorientation causes a transition between
CC       'inactive' to 'active' states, causing alignment of C-terminal and
CC       membrane-docking sites (MDoS) side-by-side and putting the membrane-
CC       disruption sites (MDiS) in the same plane, exposed to solvent and in a
CC       symmetric position for both monomers (By similarity). The MDoS region
CC       stabilizes the toxin on membrane by the interaction of charged residues
CC       with phospholipid head groups (By similarity). Subsequently, the MDiS
CC       region destabilizes the membrane with penetration of hydrophobic
CC       residues (By similarity). This insertion causes a disorganization of
CC       the membrane, allowing an uncontrolled influx of ions (i.e. calcium and
CC       sodium), and eventually triggering irreversible intracellular
CC       alterations and cell death (By similarity).
CC       {ECO:0000250|UniProtKB:I6L8L6, ECO:0000269|PubMed:24724078}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24724078}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24724078}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24724078}.
CC   -!- MASS SPECTROMETRY: Mass=13623; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:24724078};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       K49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DMK0; -.
DR   SMR; P0DMK0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Myotoxin; Secreted; Toxin.
FT   CHAIN           1..>28
FT                   /note="Basic phospholipase A2 homolog BmatTX-II"
FT                   /id="PRO_0000429741"
FT   DISULFID        26..?
FT                   /evidence="ECO:0000250|UniProtKB:Q90249"
FT   DISULFID        28..?
FT                   /evidence="ECO:0000250|UniProtKB:Q90249"
FT   NON_TER         28
SQ   SEQUENCE   28 AA;  3023 MW;  11750D2F7CAB0103 CRC64;
     SLFELGKMIL QETGKNPAQS YGAYGCNC