PA2A4_BOTAL
ID PA2A4_BOTAL Reviewed; 121 AA.
AC P86456;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Acidic phospholipase A2 SpII RP4 {ECO:0000303|PubMed:20331996};
DE Short=Ba SpII RP4 {ECO:0000303|PubMed:20331996};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:20331996};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P14418};
OS Bothrops alternatus (Urutu) (Rhinocerophis alternatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=64174;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC STRAIN=Northeast Argentina {ECO:0000303|PubMed:20331996};
RC TISSUE=Venom {ECO:0000269|PubMed:20331996};
RX PubMed=20331996; DOI=10.1016/j.toxicon.2010.02.031;
RA Garcia Denegri M.E., Acosta O.C., Huancahuire-Vega S., Martins-de-Souza D.,
RA Marangoni S., Marunak S.L., Teibler G.P., Leiva L.C., Ponce-Soto L.A.;
RT "Isolation and functional characterization of a new acidic PLA(2) Ba SpII
RT RP4 of the Bothrops alternatus snake venom from Argentina.";
RL Toxicon 56:64-74(2010).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) which exhibits indirect
CC hemolysis, induces mild edema inflammation in the foot pads of mice and
CC slightly delays anticoagulant activities. In mice, not lethal, even at
CC the highest dose, and exhibits low to moderate myotoxicity on muscular
CC fibers. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:20331996}.
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, ECO:0000255|PROSITE-
CC ProRule:PRU10036, ECO:0000269|PubMed:20331996};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P14418};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14418};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20331996}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20331996}.
CC -!- MASS SPECTROMETRY: Mass=14185.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20331996};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P86456; -.
DR SMR; P86456; -.
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; IPR033112; PLipase_A2_Asp_AS.
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; PS00119; PA2_ASP; 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..121
FT /note="Acidic phospholipase A2 SpII RP4"
FT /id="PRO_0000392923"
FT ACT_SITE 46
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 88
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 25..114
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 27..43
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 42..94
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 48..121
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 49..87
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 56..80
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 74..85
FT /evidence="ECO:0000250|UniProtKB:P14418"
SQ SEQUENCE 121 AA; 13743 MW; E81D14D726E107A8 CRC64;
NLVQFKTLIM KIAGRSVVYK YFYGCYCGWG GIGQPRDATD RCCFVHDCCY GKVTNCNPKT
ATYSYTEENG ALVCGGDDPC KKQVCECDRV AAMCFRDNKD TYDNKYWFLP PKNCQEDSEP
C
