ID   VSPJF_PROJR             Reviewed;          20 AA.
AC   P0DMU1;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Beta-fibrinogenase jerdofibrase;
DE            EC=3.4.21.-;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
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, SUBUNIT, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Venom;
RX   PubMed=11306131; DOI=10.1016/s0041-0101(00)00261-0;
RA   Jin Y., Lu Q.M., Wei J.F., Li D.S., Wang W.Y., Xiong Y.L.;
RT   "Purification and characterization of jerdofibrase, a serine protease from
RT   the venom of Trimeresurus jerdonii snake.";
RL   Toxicon 39:1203-1210(2001).
RN   [2]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=12091097; DOI=10.1016/s1096-4959(02)00069-6;
RA   Jin Y., Lu Q.M., Wang W.Y., Xiong Y.L.;
RT   "Actions of two serine proteases from Trimeresurus jerdonii venom on
RT   chromogenic substrates and fibrinogen.";
RL   Comp. Biochem. Physiol. 132:529-534(2002).
CC   -!- FUNCTION: Fibrin(ogen)olytic serine protease degrades Bbeta-chain of
CC       human fibrinogen (FGB) and shows a lower activity on Aa-chain (FGA).
CC       Also degrades fibrin directly. Releases fibrinopeptide B and a small
CC       amount of fibrinopeptide A. Has also be shown to catalyze the
CC       hydrolysis of some chromogenic substrates such as S2238, S2160, S2302
CC       and S2251. {ECO:0000269|PubMed:11306131}.
CC   -!- ACTIVITY REGULATION: Inhibited by PMSF and soybean trypsin inhibitor.
CC       Partially inhibited by DTT and cysteine. Not affected by EDTA.
CC       {ECO:0000269|PubMed:11306131}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.8 uM for S-2160 (Bz-Ile-Glu-Gly-Arg-pNA)
CC         {ECO:0000269|PubMed:11306131};
CC         KM=27 uM for S-2302 (H-D-Pro-Phe-Arg-pNA)
CC         {ECO:0000269|PubMed:11306131, ECO:0000269|PubMed:12091097};
CC         KM=46.7 uM for S-2238 (H-D-Phe-Pip-Arg-pNA)
CC         {ECO:0000269|PubMed:11306131, ECO:0000269|PubMed:12091097};
CC         KM=399.2 uM for S-2251 (H-D-Val-Leu-Lys-pNA)
CC         {ECO:0000269|PubMed:11306131, ECO:0000269|PubMed:12091097};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11306131}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11306131}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Does not show coagulant activity. Does not show activity
CC       on gamma-chain of fibrinogen (PubMed:11306131, PubMed:12091097). Does
CC       not activate Lys-plasminogen. Does not show hemorrhagic activity.
CC       Neither causes rabbit platelet aggregation nor inhibits platelet
CC       aggregation induced by ADP and collagen (PubMed:11306131).
CC       {ECO:0000269|PubMed:11306131, ECO:0000269|PubMed:12091097}.
CC   -!- MISCELLANEOUS: Its molecular weight is estimated to be 32000.
CC       {ECO:0000269|PubMed:11306131, ECO:0000269|PubMed:12091097}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P0DMU1; -.
DR   SABIO-RK; P0DMU1; -.
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; Hemostasis impairing toxin; Hydrolase; Protease;
KW   Secreted; Serine protease; Toxin.
FT   CHAIN           1..>20
FT                   /note="Beta-fibrinogenase jerdofibrase"
FT                   /id="PRO_0000432790"
FT   DOMAIN          1..>20
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000250|UniProtKB:Q91507"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2295 MW;  2219FA880343F392 CRC64;
     VIGGDECNIN EHPFLVLVYY