ID   PA2HG_OXYSC             Reviewed;         152 AA.
AC   P00616; Q4VRI6;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Acidic phospholipase A2 homolog taipoxin gamma chain;
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 20-152, AND GLYCOSYLATION AT ASN-97.
RC   TISSUE=Venom;
RX   PubMed=563806; DOI=10.1016/0014-5793(77)80726-6;
RA   Fohlman J., Lind P., Eaker D.;
RT   "Taipoxin, an extremely potent presynaptic snake venom neurotoxin.
RT   Elucidation of the primary structure of the acidic carbohydrate-containing
RT   taipoxin-subunit, a prophospholipase homolog.";
RL   FEBS Lett. 84:367-371(1977).
RN   [3]
RP   PROTEIN SEQUENCE OF 20-23, AND ABSENCE OF ENZYMATIC ACTIVITY OF THE GAMMA
RP   CHAIN.
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, CARBOHYDRATE CONTENT, 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 (gamma chain): Snake venom phospholipase A2 homolog
CC       that is neither toxic nor enzymatically active. Does not bind calcium
CC       (PubMed:22776098). {ECO:0000269|PubMed:10748068,
CC       ECO:0000269|PubMed:22776098, ECO:0000269|PubMed:7722520,
CC       ECO:0000269|PubMed:976268}.
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   -!- PTM: Contains 0.9% fucose, 2.2% manose, 4.2% N-acetyl-D-glucosamine,
CC       3.5% galactose, and 3.8% N-acetyl-neuraminic acid (sialic acid).
CC       {ECO:0000269|PubMed:976268}.
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; AY691659; AAY47068.1; -; mRNA.
DR   PIR; A00756; PSOXG.
DR   AlphaFoldDB; P00616; -.
DR   SMR; P00616; -.
DR   iPTMnet; P00616; -.
DR   PRIDE; P00616; -.
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   Direct protein sequencing; Disulfide bond; Glycoprotein; Secreted;
KW   Sialic acid; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:22776098,
FT                   ECO:0000269|PubMed:563806"
FT   CHAIN           20..152
FT                   /note="Acidic phospholipase A2 homolog taipoxin gamma
FT                   chain"
FT                   /id="PRO_0000161680"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:563806"
FT   DISULFID        38..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..46
FT                   /evidence="ECO:0000305"
FT   DISULFID        54..151
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..132
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..125
FT                   /evidence="ECO:0000250"
FT   DISULFID        88..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        111..123
FT                   /evidence="ECO:0000250"
FT   CONFLICT        22
FT                   /note="I -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27
FT                   /note="L -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44..45
FT                   /note="ES -> SE (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141..142
FT                   /note="LN -> DL (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150..151
FT                   /note="HC -> CH (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   152 AA;  16558 MW;  E548A6DAF900F81F CRC64;
     MHPAHLLVLL AVCVSLLGSS EIPQPSLDFE QFSNMIQCTI PCGESCLAYM DYGCYCGPGG
     SGTPIDDLDR CCKTHDECYA EAGKLSACKS VLSEPNNDTY SYECNEGQLT CNDDNDECKA
     FICNCDRTAV TCFAGAPYND LNYNIGMIEH CK