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Basic phospholipase A2 homolog piratoxin-1 (svPLA2 homolog) (Myotoxin SIV-SP5) (Piratoxin-I) (PrTX-I)

 PA2H1_BOTPI             Reviewed;         121 AA.
P58399;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
05-DEC-2001, sequence version 2.
20-DEC-2017, entry version 82.
RecName: Full=Basic phospholipase A2 homolog piratoxin-1;
Short=svPLA2 homolog;
AltName: Full=Myotoxin SIV-SP5;
AltName: Full=Piratoxin-I;
Short=PrTX-I;
Bothrops pirajai (Piraja's lance0 head).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
NCBI_TaxID=113192;
[1]
PROTEIN SEQUENCE, AND LETHAL DOSE.
TISSUE=Venom;
PubMed=9853687; DOI=10.1007/BF02780974;
Toyama M.H., Soares A.M., Vieira C.A., Novello J.C., Oliveira B.,
Giglio J.R., Marangoni S.;
"Amino acid sequence of piratoxin-I, a myotoxin from Bothrops pirajai
snake venom, and its biological activity after alkylation with p-
bromophenacyl bromide.";
J. Protein Chem. 17:713-718(1998).
[2]
PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
PubMed=7660366; DOI=10.1016/0041-0101(95)00012-B;
Mancuso L.C., Correa M.M., Vieira C.A., Cunha O.A., Lachat J.J.,
de Araujo H.S., Ownby C.L., Giglio J.R.;
"Fractionation of Bothrops pirajai snake venom: isolation and
characterization of piratoxin-I, a new myotoxic protein.";
Toxicon 33:615-626(1995).
[3]
FUNCTION, X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH THE
INHIBITOR ROSMARINIC ACID (RA), AND DISULFIDE BONDS.
TISSUE=Venom;
PubMed=22205953; DOI=10.1371/journal.pone.0028521;
Dos Santos J.I., Cardoso F.F., Soares A.M., Dal Pai Silva M.,
Gallacci M., Fontes M.R.;
"Structural and functional studies of a bothropic myotoxin complexed
to rosmarinic acid: new insights into Lys49-PLA(2) inhibition.";
PLoS ONE 6:E28521-E28521(2011).
[4]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=9723838; DOI=10.1016/S0041-0101(98)00017-8;
de Azevedo W.F. Jr., Ward R.J., Canduri F., Soares A., Giglio J.R.,
Arni R.K.;
"Crystal structure of piratoxin-I: a calcium-independent, myotoxic
phospholipase A2-homologue from Bothrops pirajai venom.";
Toxicon 36:1395-1406(1998).
[5]
X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 1-111 IN COMPLEX WITH THE
PLA2 INHIBITOR BPB, AND DISULFIDE BONDS.
TISSUE=Venom;
PubMed=19616648; DOI=10.1016/j.bbapap.2009.07.005;
Marchi-Salvador D.P., Fernandes C.A., Silveira L.B., Soares A.M.,
Fontes M.R.;
"Crystal structure of a phospholipase A(2) homolog complexed with p-
bromophenacyl bromide reveals important structural changes associated
with the inhibition of myotoxic activity.";
Biochim. Biophys. Acta 1794:1583-1590(2009).
-!- FUNCTION: Snake venom phospholipase A2 (PLA2) homolog that lacks
enzymatic activity, but displays myotoxin and edema-inducing
activities in vivo. In vitro neuromuscular activities have also
been observed, but they are not found in vivo and can be explained
by the destabilization of the muscle membrane by the toxin. The
myotoxic activity is inhibited by rosmarinic acid (RA).
{ECO:0000269|PubMed:22205953, ECO:0000269|PubMed:7660366}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19616648,
ECO:0000269|PubMed:22205953}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- TOXIC DOSE: LD(50) is 8 mg/kg by intraperitoneal injection into
mice. {ECO:0000269|PubMed:9853687}.
-!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
subfamily. K49 sub-subfamily. {ECO:0000305}.
-!- CAUTION: Does not bind calcium as one of the calcium-binding sites
is lost (Asp->Lys in position 48, which corresponds to 'Lys-49' in
the current nomenclature). {ECO:0000305}.
-----------------------------------------------------------------------
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PDB; 2OK9; X-ray; 2.34 A; A/B=1-121.
PDB; 3QNL; X-ray; 1.77 A; A/B=1-121.
PDB; 4YU7; X-ray; 1.65 A; A/B=1-121.
PDB; 4YZ7; X-ray; 1.96 A; A/B=1-121.
PDBsum; 2OK9; -.
PDBsum; 3QNL; -.
PDBsum; 4YU7; -.
PDBsum; 4YZ7; -.
ProteinModelPortal; P58399; -.
SMR; P58399; -.
HOVERGEN; HBG008137; -.
BRENDA; 3.1.1.4; 8187.
EvolutionaryTrace; P58399; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
CDD; cd00125; PLA2c; 1.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR001211; PLipase_A2.
InterPro; IPR033112; PLipase_A2_Asp_AS.
InterPro; IPR016090; PLipase_A2_dom.
InterPro; IPR036444; PLipase_A2_dom_sf.
InterPro; IPR033113; PLipase_A2_His_AS.
PANTHER; PTHR11716; PTHR11716; 1.
Pfam; PF00068; Phospholip_A2_1; 1.
PRINTS; PR00389; PHPHLIPASEA2.
SMART; SM00085; PA2c; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00119; PA2_ASP; 1.
PROSITE; PS00118; PA2_HIS; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond; Myotoxin;
Secreted; Toxin.
CHAIN 1 121 Basic phospholipase A2 homolog piratoxin-
1.
/FTId=PRO_0000161627.
DISULFID 26 115 {ECO:0000244|PDB:2OK9,
ECO:0000269|PubMed:19616648}.
DISULFID 28 44 {ECO:0000244|PDB:2OK9,
ECO:0000269|PubMed:19616648}.
DISULFID 43 95 {ECO:0000244|PDB:2OK9,
ECO:0000269|PubMed:19616648}.
DISULFID 49 121 {ECO:0000244|PDB:2OK9,
ECO:0000269|PubMed:19616648}.
DISULFID 50 88 {ECO:0000244|PDB:2OK9,
ECO:0000269|PubMed:19616648}.
DISULFID 57 81 {ECO:0000244|PDB:2OK9,
ECO:0000269|PubMed:19616648}.
DISULFID 75 86 {ECO:0000244|PDB:2OK9,
ECO:0000269|PubMed:19616648}.
HELIX 2 13 {ECO:0000244|PDB:4YU7}.
HELIX 17 21 {ECO:0000244|PDB:4YU7}.
STRAND 22 24 {ECO:0000244|PDB:2OK9}.
TURN 25 27 {ECO:0000244|PDB:4YU7}.
STRAND 28 31 {ECO:0000244|PDB:4YU7}.
HELIX 39 52 {ECO:0000244|PDB:4YU7}.
TURN 59 61 {ECO:0000244|PDB:4YU7}.
STRAND 66 69 {ECO:0000244|PDB:4YU7}.
STRAND 72 75 {ECO:0000244|PDB:4YU7}.
HELIX 80 98 {ECO:0000244|PDB:4YU7}.
HELIX 99 102 {ECO:0000244|PDB:4YU7}.
HELIX 105 107 {ECO:0000244|PDB:4YU7}.
HELIX 112 114 {ECO:0000244|PDB:4YU7}.
SEQUENCE 121 AA; 13729 MW; B51C1BB79639893B CRC64;
SLFELGKMIL QETGKNPAKS YGAYGCNCGV LGRGKPKDAT DRCCYVHKCC YKKLTGCNPK
KDRYSYSWKD KTIVCGENNP CLKELCECDK AVAICLRENL GTYNKLYRYH LKPFCKKADD
C


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