PA2H_BOTDP
ID PA2H_BOTDP Reviewed; 40 AA.
AC P0DUP1;
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 Bneu-I {ECO:0000303|PubMed:10519651};
DE Short=svPLA2 homolog;
DE AltName: Full=B.neuwiedii myotoxin I {ECO:0000303|PubMed:10519651};
DE AltName: Full=Lys49 PLA2-like;
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.
RX PubMed=10519651; DOI=10.1016/s0041-0101(99)00115-4;
RA Geoghegan P., Angulo Y., Cangelosi A., Diaz M., Lomonte B.;
RT "Characterization of a basic phospholipase A2-homologeu myotoxin isolated
RT from the venom of the snake Bothrops neuwiedii (yarara chica) from
RT Argentina.";
RL Toxicon 37:1735-1746(1999).
RN [2]
RP TAXONOMY REVISION.
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 homolog that lacks enzymatic
CC activity (PubMed:10519651). It induces local myotoxicity and shows
CC edema-forming effects in mice (PubMed:10519651). It is not lethal when
CC intravenously injected at high doses (up to 4.7 mg/kg)
CC (PubMed:10519651). {ECO:0000269|PubMed:10519651}.
CC -!- SUBUNIT: Homodimer; probably non-covalently linked.
CC {ECO:0000269|PubMed:10519651}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10519651}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10519651}.
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}.
CC -!- CAUTION: The source organism was originally classified as the Bothrops
CC neuwiedi species. {ECO:0000305|PubMed:29170054}.
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DR AlphaFoldDB; P0DUP1; -.
DR SMR; P0DUP1; -.
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 Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Myotoxin; Secreted; Toxin.
FT CHAIN 1..>40
FT /note="Basic phospholipase A2 homolog Bneu-I"
FT /evidence="ECO:0000269|PubMed:10519651"
FT /id="PRO_0000452902"
FT DISULFID 26..?
FT /evidence="ECO:0000250|UniProtKB:I6L8L6"
FT DISULFID 28..?
FT /evidence="ECO:0000250|UniProtKB:I6L8L6"
FT NON_TER 40
FT /evidence="ECO:0000305|PubMed:10519651"
SQ SEQUENCE 40 AA; 4157 MW; AA67223C69895D07 CRC64;
SLVELGKMIL QETGKNPVTS YGAYGCNCGV LGRGKPKDAT
