PA2HC_OXYSC
ID PA2HC_OXYSC Reviewed; 118 AA.
AC P0CG57;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Neutral phospholipase A2 homolog taipoxin beta chain 2;
DE Short=svPLA2 homolog;
OS Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX NCBI_TaxID=8667;
RN [1]
RP PROTEIN SEQUENCE OF 1-4, X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS), ABSENCE OF
RP ENZYMATIC ACTIVITY OF THE BETA CHAIN, DISULFIDE BONDS, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=22776098; DOI=10.1111/j.1742-4658.2012.08691.x;
RA Cendron L., Micetic I., Polverino de Laureto P., Paoli M.;
RT "Structural analysis of trimeric phospholipase A2 neurotoxin from the
RT Australian taipan snake venom.";
RL FEBS J. 279:3121-3135(2012).
RN [2]
RP FUNCTION, SUBUNIT, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=976268; DOI=10.1111/j.1432-1033.1976.tb10833.x;
RA Fohlman J., Eaker D., Karlsoon E., Thesleff S.;
RT "Taipoxin, an extremely potent presynaptic neurotoxin from the venom of the
RT australian snake taipan (Oxyuranus s. scutellatus). Isolation,
RT characterization, quaternary structure and pharmacological properties.";
RL Eur. J. Biochem. 68:457-469(1976).
RN [3]
RP FUNCTION AS RCN2 BINDING PROTEIN.
RX PubMed=7722520; DOI=10.1046/j.1471-4159.1995.64052339.x;
RA Dodds D., Schlimgen A.K., Lu S.Y., Perin M.S.;
RT "Novel reticular calcium binding protein is purified on taipoxin columns.";
RL J. Neurochem. 64:2339-2344(1995).
RN [4]
RP FUNCTION AS PENTRAXIN BINDING PROTEIN.
RX PubMed=10748068; DOI=10.1074/jbc.m002254200;
RA Kirkpatrick L.L., Matzuk M.M., Dodds D.C., Perin M.S.;
RT "Biochemical interactions of the neuronal pentraxins. Neuronal pentraxin
RT (NP) receptor binds to taipoxin and taipoxin-associated calcium-binding
RT protein 49 via NP1 and NP2.";
RL J. Biol. Chem. 275:17786-17792(2000).
CC -!- FUNCTION: Heterotrimer: Snake venom phospholipase A2 (PLA2)
CC heterotrimer that acts as a potent presynaptic neurotoxin by blocking
CC synaptic transmission and synaptic vesicle recycling. May act by
CC binding in a calcium-dependent fashion to neurotonal pentraxin-1
CC (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuronal
CC pentraxin receptor (NPTXR). Also binds to taipoxin-associated calcium
CC binding protein 49 (RCN2), a protein localized in the lumen of
CC endoplasmic reticulum.
CC -!- FUNCTION: Monomer (beta chain): Snake venom phospholipase A2 homolog
CC that is neither toxic nor enzymatically active. Does not bind calcium.
CC -!- SUBUNIT: Heterotrimer of alpha, beta, and gamma chains; non-covalently
CC linked. {ECO:0000269|PubMed:976268}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13307.3; Mass_error=0.1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:22776098};
CC -!- TOXIC DOSE: Heterotrimer: LD(50) is 2 ug/kg by intravenous injection
CC into mice. {ECO:0000269|PubMed:976268}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR PDB; 3VBZ; X-ray; 1.76 A; A/B=1-118.
DR PDBsum; 3VBZ; -.
DR AlphaFoldDB; P0CG57; -.
DR SMR; P0CG57; -.
DR PRIDE; P0CG57; -.
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: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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Secreted.
FT CHAIN 1..118
FT /note="Neutral phospholipase A2 homolog taipoxin beta chain
FT 2"
FT /id="PRO_0000420858"
FT DISULFID 11..71
FT /evidence="ECO:0000269|PubMed:22776098"
FT DISULFID 27..117
FT /evidence="ECO:0000269|PubMed:22776098"
FT DISULFID 29..45
FT /evidence="ECO:0000269|PubMed:22776098"
FT DISULFID 44..98
FT /evidence="ECO:0000269|PubMed:22776098"
FT DISULFID 51..91
FT /evidence="ECO:0000269|PubMed:22776098"
FT DISULFID 60..84
FT /evidence="ECO:0000269|PubMed:22776098"
FT DISULFID 78..89
FT /evidence="ECO:0000269|PubMed:22776098"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:3VBZ"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:3VBZ"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:3VBZ"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:3VBZ"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3VBZ"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3VBZ"
FT HELIX 40..57
FT /evidence="ECO:0007829|PDB:3VBZ"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3VBZ"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3VBZ"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3VBZ"
FT HELIX 83..101
FT /evidence="ECO:0007829|PDB:3VBZ"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:3VBZ"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:3VBZ"
SQ SEQUENCE 118 AA; 13313 MW; B31BC46837CF0B5A CRC64;
NLVQFGFMIE CAIRNRRPAL DFMNYGCYCG TVGRGTPVDD LDRCCQVHDE CYATAEKHGC
YPSLTTYQWE CRQVGNECNS KTQCEVFVCA CDLAAAKCLA QEDYNPAHFN INTGERCK
