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Basic phospholipase A2 homolog MT1 (svPLA2 homolog) (ACL Myotoxin)

 PA2H1_AGKCL             Reviewed;         137 AA.
P49121;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
20-DEC-2017, entry version 98.
RecName: Full=Basic phospholipase A2 homolog MT1;
Short=svPLA2 homolog;
AltName: Full=ACL Myotoxin;
Flags: Precursor;
Agkistrodon contortrix laticinctus (Broad-banded copperhead)
(Agkistrodon mokasen laticinctus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
Agkistrodon.
NCBI_TaxID=37195;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 17-36.
TISSUE=Venom, and Venom gland;
PubMed=8579368; DOI=10.1006/abbi.1996.0042;
de Araujo H.S.S., White S.P., Ownby C.L.;
"cDNA cloning and sequence analysis of a lysine-49 phospholipase A2
myotoxin from Agkistrodon contortrix laticinctus snake venom.";
Arch. Biochem. Biophys. 326:21-30(1996).
[2]
X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 17-137, AND DISULFIDE BONDS.
TISSUE=Venom;
PubMed=15596433; DOI=10.1074/jbc.M410588200;
Ambrosio A.L.B., Nonato M.C., de Araujo H.S.S., Arni R., Ward R.J.,
Ownby C.L., de Souza D.H.F., Garratt R.C.;
"A molecular mechanism for Lys49-phospholipase A2 activity based on
ligand-induced conformational change.";
J. Biol. Chem. 280:7326-7335(2005).
-!- FUNCTION: Snake venom phospholipase A2 homolog that has myotoxic
activities. Lacks enzymatic activity.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- 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 64, which corresponds to 'Lys-49' in
the current nomenclature). {ECO:0000305}.
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EMBL; U21335; AAC59887.1; -; mRNA.
PIR; S68429; S68429.
PDB; 1S8G; X-ray; 2.30 A; A=17-137.
PDB; 1S8H; X-ray; 1.80 A; A=17-137.
PDB; 1S8I; X-ray; 1.61 A; A=17-137.
PDBsum; 1S8G; -.
PDBsum; 1S8H; -.
PDBsum; 1S8I; -.
ProteinModelPortal; P49121; -.
SMR; P49121; -.
HOVERGEN; HBG008137; -.
EvolutionaryTrace; P49121; -.
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; Signal; Toxin.
SIGNAL 1 16 {ECO:0000269|PubMed:8579368}.
CHAIN 17 137 Basic phospholipase A2 homolog MT1.
/FTId=PRO_0000022775.
DISULFID 42 131 {ECO:0000269|PubMed:15596433}.
DISULFID 44 60 {ECO:0000269|PubMed:15596433}.
DISULFID 59 111 {ECO:0000269|PubMed:15596433}.
DISULFID 65 137 {ECO:0000269|PubMed:15596433}.
DISULFID 66 104 {ECO:0000269|PubMed:15596433}.
DISULFID 73 97 {ECO:0000269|PubMed:15596433}.
DISULFID 91 102 {ECO:0000269|PubMed:15596433}.
HELIX 18 29 {ECO:0000244|PDB:1S8I}.
HELIX 33 37 {ECO:0000244|PDB:1S8I}.
STRAND 38 40 {ECO:0000244|PDB:1S8I}.
TURN 41 43 {ECO:0000244|PDB:1S8I}.
STRAND 44 47 {ECO:0000244|PDB:1S8G}.
HELIX 55 68 {ECO:0000244|PDB:1S8I}.
TURN 75 77 {ECO:0000244|PDB:1S8I}.
STRAND 82 85 {ECO:0000244|PDB:1S8I}.
STRAND 88 91 {ECO:0000244|PDB:1S8I}.
HELIX 96 114 {ECO:0000244|PDB:1S8I}.
HELIX 116 118 {ECO:0000244|PDB:1S8I}.
HELIX 121 124 {ECO:0000244|PDB:1S8I}.
HELIX 126 128 {ECO:0000244|PDB:1S8I}.
SEQUENCE 137 AA; 15775 MW; 8537C670E4AFAA86 CRC64;
MRTLWIVALL LVGVEGSLLE LGKMILQETG KNAITSYGSY GCNCGWGHRG QPKDATDRCC
FVHKCCYKKL TDCNHKTDRY SYSWKNKAII CEEKNPCLKE MCECDKAVAI CLRENLDTYN
KKYKAYFKFK CKKPETC


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