PA2HC_PSETE
ID PA2HC_PSETE Reviewed; 145 AA.
AC P30811; Q45Z36; Q45Z37; Q45Z38;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Acidic phospholipase A2 homolog textilotoxin C chain;
DE Short=svPLA2 homolog;
DE Flags: Precursor;
OS Pseudonaja textilis (Eastern brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX NCBI_TaxID=8673;
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 PROTEIN SEQUENCE OF 28-145, FUNCTION, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=8431471; DOI=10.1016/0167-4838(93)90217-f;
RA Pearson J.A., Tyler M.I., Retson K.V., Howden M.E.H.;
RT "Studies on the subunit structure of textilotoxin, a potent presynaptic
RT neurotoxin from the venom of the Australian common brown snake (Pseudonaja
RT textilis). 3. The complete amino-acid sequences of all the subunits.";
RL Biochim. Biophys. Acta 1161:223-229(1993).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=16284125; DOI=10.1074/mcp.m500270-mcp200;
RA Birrell G.W., Earl S., Masci P.P., de Jersey J., Wallis T.P., Gorman J.J.,
RA Lavin M.F.;
RT "Molecular diversity in venom from the Australian Brown snake, Pseudonaja
RT textilis.";
RL Mol. Cell. Proteomics 5:379-389(2006).
RN [4]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=18951409; DOI=10.1002/prot.22259;
RA Aquilina J.A.;
RT "The major toxin from the Australian common brown snake is a hexamer with
RT unusual gas-phase dissociation properties.";
RL Proteins 75:478-485(2009).
CC -!- FUNCTION: Snake venom oligomeric phospholipase A2 that has potent
CC presynaptic neurotoxicity. Chain C is not itself neurotoxic, but it is
CC essential for the neurotoxicity of textilotoxin. Chain C possesses a
CC very low phospholipase activity. {ECO:0000269|PubMed:8431471}.
CC -!- SUBUNIT: Heterohexamer. 2 forms exist: 2 A or 2 B chains, 2 C chains
CC and 2 covalently-linked D chains, and 1 A or 1 B, 1 C, 2 covalently-
CC linked D chains and 2 differentially glycosylated covalently-linked D
CC chains. Textilotoxin was originally described as pentameric
CC (PubMed:8431471). {ECO:0000269|PubMed:18951409,
CC ECO:0000269|PubMed:8431471}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- TOXIC DOSE: Oligomer: LD(50) is 1 ug/kg by intraperitoneal injection
CC into mice. {ECO:0000269|PubMed:8431471}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ085828; AAZ22646.1; -; mRNA.
DR EMBL; DQ085829; AAZ22647.1; -; mRNA.
DR EMBL; DQ085830; AAZ22648.1; -; mRNA.
DR PIR; S29653; S29653.
DR AlphaFoldDB; P30811; -.
DR SMR; P30811; -.
DR Proteomes; UP000472273; Unplaced.
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: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: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; Neurotoxin;
KW Presynaptic neurotoxin; Reference proteome; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..27
FT /evidence="ECO:0000269|PubMed:8431471"
FT /id="PRO_0000420146"
FT CHAIN 28..145
FT /note="Acidic phospholipase A2 homolog textilotoxin C
FT chain"
FT /id="PRO_0000161696"
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"
FT CONFLICT 95
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..103
FT /note="Missing (in Ref. 1; AAZ22648)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="N -> S (in Ref. 1; AAZ22647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 15855 MW; 4094F8DCA92BA162 CRC64;
MHPAHLLVLL GVYVSLLGAA RIPPLPLNLI QFSNMIKCTI PGSQPLLDYA NYGCYCGPGN
NGTPVDDVDR CCQAHDECYD EASNHGCYPE LTLYDYYCDT GVPYCKARTQ CQVFVCGCDL
AVAKCLAGAT YNDENKNINT GERCQ
