VSP_BITAR
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}.
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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