PA2N_GLOHA
ID PA2N_GLOHA Reviewed; 122 AA.
AC P14421;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Neutral phospholipase A2 agkistrodotoxin;
DE Short=AGTX;
DE Short=ATX;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=8714;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=2656663; DOI=10.1093/oxfordjournals.jbchem.a122639;
RA Kondo K., Zhang J.-K., Xu K., Kagamiyama H.;
RT "Amino acid sequence of a presynaptic neurotoxin, agkistrodotoxin, from the
RT venom of Agkistrodon halys pallas.";
RL J. Biochem. 105:196-203(1989).
RN [2]
RP PROTEIN SEQUENCE OF 1-52.
RC TISSUE=Venom;
RX PubMed=3617077; DOI=10.1016/0041-0101(87)90073-0;
RA Chen Y.-C., Maraganore J.M., Reardon I., Heinrikson R.L.;
RT "Characterization of the structure and function of three phospholipases A2
RT from the venom of Agkistrodon halys pallas.";
RL Toxicon 25:401-409(1987).
RN [3]
RP PROTEIN SEQUENCE OF 1-23, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=15032748; DOI=10.1042/bj20040125;
RA Chen Y.-H., Wang Y.-M., Hseu M.-J., Tsai I.-H.;
RT "Molecular evolution and structure-function relationships of crotoxin-like
RT and asparagine-6-containing phospholipases A2 in pit viper venoms.";
RL Biochem. J. 381:25-34(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=9733637; DOI=10.1006/jmbi.1998.1987;
RA Tang L., Zhou Y.-C., Lin Z.-J.;
RT "Crystal structure of agkistrodotoxin, a phospholipase A2-type presynaptic
RT neurotoxin from Agkistrodon halys pallas.";
RL J. Mol. Biol. 282:1-11(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH CALCIUM ION,
RP COFACTOR, AND DISULFIDE BONDS.
RX PubMed=10666574; DOI=10.1107/s0907444999012603;
RA Tang L., Zhou Y.C., Lin Z.J.;
RT "Structure of agkistrodotoxin in an orthorhombic crystal form with six
RT molecules per asymmetric unit.";
RL Acta Crystallogr. D 55:1986-1996(1999).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits
CC neuromuscular transmission by blocking acetylcholine release from the
CC nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the
CC 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:15032748}.
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};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000305|PubMed:10666574};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:10666574};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13938; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15032748};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR PIR; C26279; C26279.
DR PIR; JX0063; JX0063.
DR PDB; 1A2A; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-122.
DR PDB; 1BJJ; X-ray; 2.80 A; A/B/C/D/E/F=1-122.
DR PDBsum; 1A2A; -.
DR PDBsum; 1BJJ; -.
DR AlphaFoldDB; P14421; -.
DR SMR; P14421; -.
DR EvolutionaryTrace; P14421; -.
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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Neurotoxin;
KW Presynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..122
FT /note="Neutral phospholipase A2 agkistrodotoxin"
FT /id="PRO_0000161599"
FT ACT_SITE 47
FT /evidence="ECO:0000305|PubMed:9733637"
FT ACT_SITE 89
FT /evidence="ECO:0000305|PubMed:9733637"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10666574,
FT ECO:0007744|PDB:1BJJ"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10666574,
FT ECO:0007744|PDB:1BJJ"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10666574,
FT ECO:0007744|PDB:1BJJ"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10666574,
FT ECO:0007744|PDB:1BJJ"
FT DISULFID 26..115
FT /evidence="ECO:0000269|PubMed:10666574,
FT ECO:0000269|PubMed:9733637, ECO:0007744|PDB:1A2A,
FT ECO:0007744|PDB:1BJJ"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:10666574,
FT ECO:0000269|PubMed:9733637, ECO:0007744|PDB:1A2A,
FT ECO:0007744|PDB:1BJJ"
FT DISULFID 43..95
FT /evidence="ECO:0000269|PubMed:10666574,
FT ECO:0000269|PubMed:9733637, ECO:0007744|PDB:1A2A,
FT ECO:0007744|PDB:1BJJ"
FT DISULFID 49..122
FT /evidence="ECO:0000269|PubMed:10666574,
FT ECO:0000269|PubMed:9733637, ECO:0007744|PDB:1A2A,
FT ECO:0007744|PDB:1BJJ"
FT DISULFID 50..88
FT /evidence="ECO:0000269|PubMed:10666574,
FT ECO:0000269|PubMed:9733637, ECO:0007744|PDB:1A2A,
FT ECO:0007744|PDB:1BJJ"
FT DISULFID 57..81
FT /evidence="ECO:0000269|PubMed:10666574,
FT ECO:0000269|PubMed:9733637, ECO:0007744|PDB:1A2A,
FT ECO:0007744|PDB:1BJJ"
FT DISULFID 75..86
FT /evidence="ECO:0000269|PubMed:10666574,
FT ECO:0000269|PubMed:9733637, ECO:0007744|PDB:1A2A,
FT ECO:0007744|PDB:1BJJ"
FT CONFLICT 30
FT /note="G -> W (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:1A2A"
FT TURN 18..22
FT /evidence="ECO:0007829|PDB:1A2A"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1A2A"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1A2A"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:1A2A"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1A2A"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1BJJ"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1BJJ"
FT HELIX 80..99
FT /evidence="ECO:0007829|PDB:1A2A"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1A2A"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1A2A"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1BJJ"
SQ SEQUENCE 122 AA; 13869 MW; BB0B7BE5266221F4 CRC64;
NLLQFNKMIK EETGKNAIPF YAFYGCYCGG GGQGKPKDGT DRCCFVHDCC YGRLVNCNTK
SDIYSYSLKE GYITCGKGTN CEEQICECDR VAAECFRRNL DTYNNGYMFY RDSKCTETSE
EC
