ID   VSPJN_PROJR             Reviewed;          21 AA.
AC   P0DMU0;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Snake venom serine protease jerdonase;
DE            Short=SVSP;
DE            EC=3.4.21.- {ECO:0000269|PubMed:12897962};
DE   Flags: Fragment;
OS   Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=242841;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, ACTIVITY REGULATION, AND GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=12897962;
RA   Jia Y.H., Jin Y., Lue Q.M., Li D.S., Wang W.Y., Xiong Y.L.;
RT   "Jerdonase, a novel serine protease with kinin-releasing and
RT   fibrinogenolytic activity from Trimeresurus jerdonii venom.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:689-694(2003).
CC   -!- FUNCTION: Multifunctional venom serine protease that has
CC       fibrino(geno)lytic activity towards the A alpha-chain of human
CC       fibrinogen (FGA) and a slow activity towards the B beta-chain (FGB).
CC       Also hydrolyzes bovine low-molecular-mass kininogen and releases
CC       bradykinin. Catalyzes the hydrolysis of BAEE, S-2238 and S-2302.
CC       {ECO:0000269|PubMed:12897962}.
CC   -!- ACTIVITY REGULATION: Inhibited by PMSF and soybean trypsin inhibitor.
CC       Partially inhibited by L-cysteine and DTT. Not affected by EDTA.
CC       {ECO:0000269|PubMed:12897962}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.25 uM for S-2302 (plasma kallikrein substrate)
CC         {ECO:0000269|PubMed:12897962};
CC         KM=41.6 uM for S-2238 (thrombin substrate)
CC         {ECO:0000269|PubMed:12897962};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12897962}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- PTM: Glycosylated; contains 35.8% neutral carbohydrate.
CC       {ECO:0000269|PubMed:12897962}.
CC   -!- MISCELLANEOUS: The enzyme does not catalyze S-2251 (a plasminogen
CC       activator substrate). Has little effect on digesting gamma-chain of
CC       fibrinogen. {ECO:0000269|PubMed:12897962}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P0DMU0; -.
DR   SABIO-RK; P0DMU0; -.
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; Fibrinogenolytic toxin;
KW   Fibrinolytic toxin; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW   Protease; Secreted; Serine protease; Toxin.
FT   CHAIN           1..>21
FT                   /note="Snake venom serine protease jerdonase"
FT                   /id="PRO_0000432787"
FT   DOMAIN          1..>21
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000250|UniProtKB:P05620"
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2304 MW;  ADE3E9EF749F93F3 CRC64;
     IIGGDECNIN EHPFLVALYD A