ID   PA2HB_OXYMI             Reviewed;         145 AA.
AC   Q45Z46;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Neutral phospholipase A2 paradoxin-like beta chain;
DE            Short=svPLA2;
DE   AltName: Full=Beta paradoxin-like;
DE   Flags: Precursor;
OS   Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX   NCBI_TaxID=111177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16261251; DOI=10.1007/s00018-005-5384-9;
RA   St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.;
RT   "Identification and analysis of venom gland-specific genes from the coastal
RT   taipan (Oxyuranus scutellatus) and related species.";
RL   Cell. Mol. Life Sci. 62:2679-2693(2005).
RN   [2]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=17313963; DOI=10.1016/j.neuropharm.2007.01.002;
RA   Hodgson W.C., Dal Belo C.A., Rowan E.G.;
RT   "The neuromuscular activity of paradoxin: a presynaptic neurotoxin from the
RT   venom of the inland taipan (Oxyuranus microlepidotus).";
RL   Neuropharmacology 52:1229-1236(2007).
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 (PubMed:17313963).
CC       May act by binding in a calcium-dependent fashion to neurotonal
CC       pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to
CC       neuronal pentraxin receptor (NPTXR). Also binds to taipoxin-associated
CC       calcium binding protein 49 (RCN2), a protein localized in the lumen of
CC       endoplasmic reticulum (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:17313963}.
CC   -!- FUNCTION: Monomer (beta chain): Snake venom phospholipase A2 homolog
CC       that is neither toxic nor enzymatically active. Does not bind calcium
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterotrimer of alpha, beta, and gamma chains; non-covalently
CC       linked. {ECO:0000269|PubMed:17313963}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       N49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: The assignment of paradoxin function to this sequence has been
CC       made based on sequence similarity to taipoxin and cannitoxin. The gamma
CC       chain has not yet been sequenced. {ECO:0000305}.
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DR   EMBL; DQ085820; AAZ22638.1; -; mRNA.
DR   AlphaFoldDB; Q45Z46; -.
DR   SMR; Q45Z46; -.
DR   PRIDE; Q45Z46; -.
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   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.
PE   1: Evidence at protein level;
KW   Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..145
FT                   /note="Neutral phospholipase A2 paradoxin-like beta chain"
FT                   /id="PRO_0000420853"
FT   DISULFID        38..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..144
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..125
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        105..116
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   145 AA;  16105 MW;  5023D53E2B63CBAE CRC64;
     MHPAHLLVLL AVCVSLLGAS DIPPLPLNLL QFGFMIECAI RNRQPALDFM NYGCYCGTVG
     HGTPVDDLDR CCKTRNECYA EAEKHGCYPS LTTYRWQCGR VGLHCNSKTQ CEVFVCACDL
     AAAKCLAQED YNPAHFNINT KARCR