ID   PA2HB_OXYSC             Reviewed;         145 AA.
AC   P00615; Q4VRI8;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Neutral phospholipase A2 homolog taipoxin beta chain 1;
DE            Short=svPLA2 homolog;
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Welton R.E., Burnell J.N.;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 28-145.
RC   TISSUE=Venom;
RX   PubMed=6756920; DOI=10.1111/j.1432-1033.1982.tb06933.x;
RA   Lind P.;
RT   "Amino-acid sequence of the beta 1 isosubunit of taipoxin, an extremely
RT   potent presynaptic neurotoxin from the Australian snake taipan (Oxyuranus
RT   s. scutellatus).";
RL   Eur. J. Biochem. 128:71-75(1982).
RN   [3]
RP   PROTEIN SEQUENCE OF 28-31, X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF
RP   28-145, ABSENCE OF ENZYMATIC ACTIVITY OF THE BETA CHAIN, DISULFIDE BONDS,
RP   AND MASS 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   [4]
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   [5]
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   [6]
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=13236.3; 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   EMBL; AY691657; AAY47066.1; -; mRNA.
DR   PIR; A00755; PSOXB.
DR   PDB; 3VC0; X-ray; 2.15 A; A=28-145.
DR   PDBsum; 3VC0; -.
DR   AlphaFoldDB; P00615; -.
DR   SMR; P00615; -.
DR   MINT; P00615; -.
DR   PRIDE; P00615; -.
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.
DR   PROSITE; PS00119; PA2_ASP; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:22776098,
FT                   ECO:0000269|PubMed:6756920"
FT   CHAIN           28..145
FT                   /note="Neutral phospholipase A2 homolog taipoxin beta chain
FT                   1"
FT                   /id="PRO_0000161679"
FT   DISULFID        38..98
FT                   /evidence="ECO:0000269|PubMed:22776098"
FT   DISULFID        54..144
FT                   /evidence="ECO:0000269|PubMed:22776098"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000269|PubMed:22776098"
FT   DISULFID        71..125
FT                   /evidence="ECO:0000269|PubMed:22776098"
FT   DISULFID        78..118
FT                   /evidence="ECO:0000269|PubMed:22776098"
FT   DISULFID        87..111
FT                   /evidence="ECO:0000269|PubMed:22776098"
FT   DISULFID        105..116
FT                   /evidence="ECO:0000269|PubMed:22776098"
FT   HELIX           29..39
FT                   /evidence="ECO:0007829|PDB:3VC0"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:3VC0"
FT   HELIX           46..50
FT                   /evidence="ECO:0007829|PDB:3VC0"
FT   TURN            53..55
FT                   /evidence="ECO:0007829|PDB:3VC0"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:3VC0"
FT   HELIX           67..84
FT                   /evidence="ECO:0007829|PDB:3VC0"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:3VC0"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:3VC0"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:3VC0"
FT   HELIX           110..128
FT                   /evidence="ECO:0007829|PDB:3VC0"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:3VC0"
FT   HELIX           140..143
FT                   /evidence="ECO:0007829|PDB:3VC0"
SQ   SEQUENCE   145 AA;  16008 MW;  F27544BF9A5A3827 CRC64;
     MHPAHLLVLL AVCVSLLGAS DIPPLPLNLV QFGKMIECAI RNRRPALDFM NYGCYCGKGG
     SGTPVDDLDR CCQVHDECYA EAEKHGCYPS LTTYTWECRQ VGPYCNSKTQ CEVFVCACDF
     AAAKCFAQED YNPAHSNINT GERCK