ID   PA2H_BOTMA              Reviewed;          33 AA.
AC   P0DI92;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Phospholipase A2 homolog BmarPLA2 {ECO:0000303|PubMed:19944711};
DE            Short=svPLA2 homolog;
DE   Flags: Fragment;
OS   Bothrops marajoensis (Marajo lancehead).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=157554;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=19944711; DOI=10.1016/j.toxicon.2009.11.013;
RA   Costa Torres A.F., Dantas R.T., Toyama M.H., Diz Filho E.B., Zara F.J.,
RA   Rodrigues de Queiroz M.G., Pinto Nogueira N.A., Rosa de Oliveira M.,
RA   de Oliveira Toyama D., Monteiro H.S.A., Martins A.M.C.;
RT   "Antibacterial and antiparasitic effects of Bothrops marajoensis venom and
RT   its fractions: phospholipase A2 and L-amino acid oxidase.";
RL   Toxicon 55:795-804(2010).
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=20036276; DOI=10.1016/j.toxicon.2009.12.004;
RA   Evangelista I.L., Martins A.M., Nascimento N.R., Havt A., Evangelista J.S.,
RA   de Noroes T.B., Toyama M.H., Diz-Filho E.B., de Oliveira Toyama D.,
RA   Fonteles M.C., Monteiro H.S.A.;
RT   "Renal and cardiovascular effects of Bothrops marajoensis venom and
RT   phospholipase A2.";
RL   Toxicon 55:1061-1070(2010).
CC   -!- FUNCTION: Snake phospholipase A2 homolog that lacks enzymatic activity
CC       (PubMed:19944711, PubMed:20036276). May display myotoxin activity
CC       (Probable). In isolated heart decreases cardiac frequency
CC       (PubMed:20036276). Also decreases mean arterial pressure
CC       (PubMed:19944711). Does not show antimicrobial activity
CC       (PubMed:19944711). Does not change renal parameters (such as perfusion
CC       pressure, renal vascular resistance, urinary flow, glomerular
CC       filtration rate and sodium tubular transport) (PubMed:20036276).
CC       {ECO:0000269|PubMed:19944711, ECO:0000269|PubMed:20036276,
CC       ECO:0000305}.
CC   -!- SUBUNIT: Homodimer; non-covalently linked.
CC       {ECO:0000269|PubMed:19944711}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19944711,
CC       ECO:0000269|PubMed:20036276}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19944711, ECO:0000305|PubMed:20036276}.
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 which corresponds to 'Lys-49' in the current
CC       nomenclature). {ECO:0000305}.
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DR   AlphaFoldDB; P0DI92; -.
DR   SMR; P0DI92; -.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Myotoxin; Secreted; Toxin.
FT   CHAIN           1..>33
FT                   /note="Phospholipase A2 homolog BmarPLA2"
FT                   /evidence="ECO:0000269|PubMed:19944711,
FT                   ECO:0000269|PubMed:20036276"
FT                   /id="PRO_0000412606"
FT   DISULFID        26..?
FT                   /evidence="ECO:0000305"
FT   DISULFID        28..?
FT                   /evidence="ECO:0000305"
FT   NON_TER         33
SQ   SEQUENCE   33 AA;  3505 MW;  0AD0BBF37AD16349 CRC64;
     SLLELGKMIL QETGKMPSKS YGAYGCNCGV LGR