ID   VSP1_DABRR              Reviewed;          16 AA.
AC   P86530;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Vipera russelli proteinase RVV-V homolog 1;
DE            Short=RVV-V 1 {ECO:0000303|PubMed:20203422};
DE            EC=3.4.21.-;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   Flags: Fragment;
OS   Daboia russelii (Russel's viper) (Vipera russelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX   NCBI_TaxID=8707;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000269|PubMed:20203422};
RX   PubMed=20203422; DOI=10.2220/biomedres.31.71;
RA   Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G.,
RA   Athauda S.B., Moriyama A.;
RT   "Molecular diversity in venom proteins of the Russell's viper (Daboia
RT   russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka.";
RL   Biomed. Res. 31:71-81(2010).
CC   -!- FUNCTION: Snake venom serine protease that may act in the hemostasis
CC       system of the prey. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20203422}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:20203422}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P86530; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Hydrolase; Protease; Secreted; Serine protease; Toxin.
FT   CHAIN           1..>16
FT                   /note="Vipera russelli proteinase RVV-V homolog 1"
FT                   /id="PRO_0000394726"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000250|UniProtKB:P09872,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         16
FT                   /evidence="ECO:0000303|PubMed:20203422"
SQ   SEQUENCE   16 AA;  1728 MW;  CC53F3926227D52F CRC64;
     VIGGDECNIN EHPFLA