ID   VSP_BITAR               Reviewed;          32 AA.
AC   Q9PRY9;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Snake venom serine proteinase;
DE            Short=SVSP;
DE   AltName: Full=Kallidin-releasing enzyme;
DE            EC=3.4.21.-;
DE   Flags: Fragment;
OS   Bitis arietans (African puff adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8692;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=8274016; DOI=10.1006/abbi.1993.1593;
RA   Nikai T., Momose M., Okumura Y., Ohara A., Komori Y., Sugihara H.;
RT   "Kallidin-releasing enzyme from Bitis arietans (puff adder) venom.";
RL   Arch. Biochem. Biophys. 307:304-310(1993).
CC   -!- FUNCTION: Cleaves a kininogen analog with the release of kallidin
CC       (lysyl-bradykinin). Completely cleaves fibrinogen Aalpha chain,
CC       partially cleaves Bbeta chain and has no activity on gamma chain.
CC       {ECO:0000269|PubMed:8274016}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.3 mM for tosyl-L-arginine methyl ester
CC         {ECO:0000269|PubMed:8274016};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8274016}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 6 disulfide bonds. {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:8274016}.
CC   -!- MISCELLANEOUS: The molecular weight was determined to be 58 kDa with an
CC       isoelectric point of 4.4.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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   PIR; S39785; S39785.
DR   SABIO-RK; Q9PRY9; -.
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.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW   Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW   Serine protease; Toxin.
FT   CHAIN           1..>32
FT                   /note="Snake venom serine proteinase"
FT                   /id="PRO_0000408028"
FT   DOMAIN          1..>32
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   UNSURE          7
FT                   /note="Assigned by comparison with orthologs"
FT   UNSURE          26
FT                   /note="Assigned by comparison with orthologs"
FT   UNSURE          29
FT                   /note="Assigned by comparison with orthologs"
FT   NON_TER         32
SQ   SEQUENCE   32 AA;  3347 MW;  F33663F675A4BC72 CRC64;
     VIGGDECDIN EHRFLVFLTX ASGLACGGTL IN