ID   PA2HA_SISTE             Reviewed;         138 AA.
AC   Q6EAN6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Acidic phospholipase A2 homolog sistruxin A;
DE            Short=SA;
DE            Short=svPLA2;
DE   Contains:
DE     RecName: Full=Sistruxin chain A;
DE   Contains:
DE     RecName: Full=Sistruxin chain B;
DE   Contains:
DE     RecName: Full=Sistruxin chain C;
DE   Flags: Precursor;
OS   Sistrurus tergeminus (Western massasauga) (Sistrurus catenatus tergeminus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Sistrurus.
OX   NCBI_TaxID=8757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15032748; DOI=10.1042/bj20040125;
RA   Chen Y.-H., Wang Y.-M., Hseu M.-J., Tsai I.-H.;
RT   "Molecular evolution and structure-function relationships of crotoxin-like
RT   and asparagine-6-containing phospholipases A2 in pit viper venoms.";
RL   Biochem. J. 381:25-34(2004).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits
CC       neuromuscular transmission by blocking acetylcholine release from the
CC       nerve termini. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of an acidic subunit and a basic chain. The acidic
CC       subunit is non-toxic, without enzymatic activity and comprises 3
CC       peptides that are cross-linked by 7 disulfide bridges. The basic
CC       subunit is toxic, has phospholipase A2 activity and is composed of a
CC       single chain (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AY508693; AAS79431.1; -; mRNA.
DR   AlphaFoldDB; Q6EAN6; -.
DR   SMR; Q6EAN6; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Neurotoxin; Presynaptic neurotoxin;
KW   Pyrrolidone carboxylic acid; Secreted; Signal; Toxin.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000250"
FT   CHAIN           38..77
FT                   /note="Sistruxin chain A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000418581"
FT   PROPEP          78..83
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000418582"
FT   CHAIN           84..118
FT                   /note="Sistruxin chain B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000418583"
FT   PROPEP          119..124
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000418584"
FT   CHAIN           125..138
FT                   /note="Sistruxin chain C"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000418585"
FT   MOD_RES         84
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..131
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  15429 MW;  06843805414E3845 CRC64;
     MRALWIVAVL LLGVEGSLVE FETLIMKIAG RSGVWYYSSY GCYCGTGGQG WPQDASDRCC
     FEHDCCYAKL TGCDPITDVY TYRQEDGEIV CGGEDPCGTQ ICECDKAAAI CFRDSMDTYN
     HKYWRFSLEN CQGESQPC