ID   PA2HS_VIPRE             Reviewed;         138 AA.
AC   F8QN50;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Basic phospholipase A2 homolog Vur-S49 {ECO:0000303|PubMed:21185324, ECO:0000303|PubMed:25522251};
DE            Short=svPLA2 homolog;
DE   Flags: Precursor;
OS   Vipera renardi (Steppe viper) (Vipera ursinii renardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=927686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=21185324; DOI=10.1016/j.toxicon.2010.12.012;
RA   Tsai I.-H., Wang Y.M., Cheng A.C., Starkov V., Osipov A., Nikitin I.,
RA   Makarova Y., Ziganshin R., Utkin Y.;
RT   "cDNA cloning, structural, and functional analyses of venom phospholipases
RT   A and a Kunitz-type protease inhibitor from steppe viper Vipera ursinii
RT   renardi.";
RL   Toxicon 57:332-341(2011).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=25522251; DOI=10.1371/journal.pone.0115428;
RA   Vulfius C.A., Kasheverov I.E., Starkov V.G., Osipov A.V., Andreeva T.V.,
RA   Filkin S.Y., Gorbacheva E.V., Astashev M.E., Tsetlin V.I., Utkin Y.N.;
RT   "Inhibition of nicotinic acetylcholine receptors, a novel facet in the
RT   pleiotropic activities of snake venom phospholipases A2.";
RL   PLoS ONE 9:e115428-e115428(2014).
CC   -!- FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic
CC       activity (PubMed:25522251). Is able to suppress the acetylcholine
CC       (ACh)-evoked current mediated by alpha-7-similar nAChRs in L.stagnalis
CC       neurons (IC(50)=2.18 uM) (PubMed:25522251). This activity is only
CC       partially reversible and seems to be non-competitive (PubMed:25522251).
CC       {ECO:0000269|PubMed:25522251}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25522251}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:25522251}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       S49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: This protein is not found in the crude venom.
CC       {ECO:0000305|PubMed:21185324}.
CC   -!- CAUTION: Does not bind calcium as one of the calcium-binding sites is
CC       lost (Asp->Ser in position 64, which corresponds to 'Ser-49' in the
CC       current nomenclature). {ECO:0000305}.
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DR   EMBL; GQ304904; ADG86228.1; -; mRNA.
DR   AlphaFoldDB; F8QN50; -.
DR   SMR; F8QN50; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
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   Acetylcholine receptor inhibiting toxin; Disulfide bond; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000250"
FT   CHAIN           17..138
FT                   /note="Basic phospholipase A2 homolog Vur-S49"
FT                   /id="PRO_0000419641"
FT   REGION          121..133
FT                   /note="Important for membrane-damaging activities in
FT                   eukaryotes and bacteria; heparin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        42..131
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        59..111
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        65..138
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        66..104
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        73..97
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
SQ   SEQUENCE   138 AA;  15659 MW;  C0860C9476E75940 CRC64;
     MRALWIVAVC LIGVEGSMIE FGKMIQEETE KNPITSYSLY GCHCGLGSKG KPKDATDRCC
     FVHSCCYAKL SDCSPKTNRY EYHRENGTIV CGSSTFCKKQ ICECDRAAAI CFRENLKTYN
     KKYKVYLRFK CKGVPEKC