ID   PA2HD_PSETE             Reviewed;         152 AA.
AC   P23028; Q45Z39; Q45Z40;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Acidic phospholipase A2 homolog textilotoxin D 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 20-152, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=2015288; DOI=10.1016/0167-4838(91)90051-z;
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). 2. The amino acid sequence and toxicity studies of subunit D.";
RL   Biochim. Biophys. Acta 1077:147-150(1991).
RN   [3]
RP   PROTEIN SEQUENCE OF 20-53.
RC   TISSUE=Venom;
RX   PubMed=3651474; DOI=10.1016/0167-4838(87)90302-5;
RA   Tyler M.I., Barnett D., Nicholson P., Spence I., Howden M.E.H.;
RT   "Studies on the subunit structure of textilotoxin, a potent neurotoxin from
RT   the venom of the Australian common brown snake (Pseudonaja textilis).";
RL   Biochim. Biophys. Acta 915:210-216(1987).
RN   [4]
RP   PROTEIN SEQUENCE OF 20-33, AND 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   [5]
RP   TOXIC DOSE, AND GLYCOSYLATION.
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   [6]
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 D is not itself neurotoxic, but it is
CC       essential for the neurotoxicity of textilotoxin. Chain D possesses a
CC       very low phospholipase activity. {ECO:0000269|PubMed:2015288}.
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; DQ085826; AAZ22644.1; -; mRNA.
DR   EMBL; DQ085827; AAZ22645.1; -; mRNA.
DR   PIR; S14728; S14728.
DR   AlphaFoldDB; P23028; -.
DR   SMR; P23028; -.
DR   iPTMnet; P23028; -.
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; Glycoprotein; Neurotoxin;
KW   Presynaptic neurotoxin; Reference proteome; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:16284125,
FT                   ECO:0000269|PubMed:2015288, ECO:0000269|PubMed:3651474"
FT   CHAIN           20..152
FT                   /note="Acidic phospholipase A2 homolog textilotoxin D
FT                   chain"
FT                   /id="PRO_0000161697"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8431471"
FT   DISULFID        38..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        42
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
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        30
FT                   /note="M -> N (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="C -> N (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="D -> N (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145
FT                   /note="I -> T (in Ref. 1; AAZ22645)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   152 AA;  16848 MW;  AEE028414F865415 CRC64;
     MHPAHLLVLL GVCVSLLGAA SIPRPSLNIM LFGNMIQCTI PCEQSWLGYL DYGCYCGSGS
     SGIPVDDVDK CCKTHDECYY KAGQIPGCSV QPNEVFNVDY SYECNEGQLT CNESNNECEM
     AVCNCDRAAA ICFARFPYNK NYWSINTEIH CR