ID   VSPAF_DABSI             Reviewed;         258 AA.
AC   E5L0E3;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Alpha-fibrinogenase-like {ECO:0000303|PubMed:21640745};
DE            Short=RVAF {ECO:0000303|PubMed:21640745};
DE            EC=3.4.21.-;
DE   AltName: Full=Snake venom serine protease {ECO:0000305};
DE            Short=SVSP {ECO:0000305};
DE   Flags: Precursor;
OS   Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX   NCBI_TaxID=343250;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=21640745; DOI=10.1016/j.toxicon.2011.05.014;
RA   Sukkapan P., Jia Y., Nuchprayoon I., Perez J.C.;
RT   "Phylogenetic analysis of serine proteases from Russell's viper (Daboia
RT   russelli siamensis) and Agkistrodon piscivorus leucostoma venom.";
RL   Toxicon 58:168-178(2011).
CC   -!- FUNCTION: Degrades alpha chain of fibrinogen (FGA), and has strong
CC       caseinolytic activity. Cleaves oxidized insulin B-chain at '40-Tyr-|-
CC       Leu-41', '48-Phe-|-Phe-49' and '49-Phe-|-Tyr-50', and glucagon at the
CC       bonds '62-Tyr-|-Ser-63', 66-Leu-|-Asp-67' and '78-Leu-|-Met-79' bonds.
CC       {ECO:0000250|UniProtKB:Q8JH85}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8JH85}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8JH85}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
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DR   EMBL; HQ270464; ADP88559.1; -; mRNA.
DR   AlphaFoldDB; E5L0E3; -.
DR   SMR; E5L0E3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Fibrinogenolytic toxin; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW   Signal; Toxin; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250|UniProtKB:Q8JH85"
FT                   /id="PRO_0000432330"
FT   CHAIN           25..258
FT                   /note="Alpha-fibrinogenase-like"
FT                   /id="PRO_0000432331"
FT   DOMAIN          25..249
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        110
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        98..256
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        142..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        174..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        200..225
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   258 AA;  28496 MW;  AAD91ECD283787EF CRC64;
     MVLIRVLANL LVLQLSYAQK SSELVVGGHP CNIYEHHFLA FMYNSSGFMC SGTLINQQWV
     LSAAHCDMEN MHIYLGLHSF KLPNKDQKKR VAKEKFFCLS SKSYTKWDKD IMLIKLNKPV
     TYSTHIASLS LPSNPPRVGS VCRIMGWGSI TSPKKILPFV PHCANINIVP YTVCRVIYRP
     LPEQSRTLCA GVSGRRIGSC LGDSGGPLIC NGQIQGIVSW GSDPCVNRGA PSIYTKVFDY
     TDWIHSIIAG NTAATCPS