ID   VSP2_PROJR              Reviewed;         258 AA.
AC   Q9DF67;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Snake venom serine protease 2;
DE            Short=SP2;
DE            Short=SVSP;
DE            EC=3.4.21.-;
DE   AltName: Full=Jerdonobin-II;
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-60, FUNCTION, CATALYTIC
RP   ACTIVITY, SUBSTRATE SPECIFICITY, AND ACTIVITY REGULATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15683874; DOI=10.1016/j.toxicon.2004.11.006;
RA   Jin Y., Lu Q.M., Chen R.Q., Wu J.B., Xiong Y.L.;
RT   "Molecular characterization of a weak fibrinogen-clotting enzyme from
RT   Trimeresurus jerdonii venom.";
RL   Toxicon 45:353-360(2005).
CC   -!- FUNCTION: Snake venom serine protease that may act in the hemostasis
CC       system of the prey (By similarity). Has weak fibrinogen clotting
CC       activity. Possesses amidolysis activity towards S-2251 (substrate for
CC       plasmin) but has no hydrolytic activity with S-2302 (plasma kalikrein
CC       substrate) or S-2238 (thrombin substrate). {ECO:0000250,
CC       ECO:0000269|PubMed:15683874}.
CC   -!- ACTIVITY REGULATION: Inhibited by PMSF at 2 mM concentration but not by
CC       EDTA. {ECO:0000269|PubMed:15683874}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not activate nor degrade plasminogen or prothrombin
CC       (F2). Does not activate factor XIII.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; AF292111; AAG10789.1; -; mRNA.
DR   AlphaFoldDB; Q9DF67; -.
DR   SMR; Q9DF67; -.
DR   MEROPS; S01.186; -.
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   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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fibrinolytic toxin;
KW   Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Toxin; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000269|PubMed:15683874"
FT                   /id="PRO_0000028403"
FT   CHAIN           25..258
FT                   /note="Snake venom serine protease 2"
FT                   /id="PRO_0000028404"
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   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
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;  28104 MW;  B36C72EFF0E72C53 CRC64;
     MVLIRVLANL LILQLSYAQK SSELVFGGRP CNINEHRSLV VLFNSSGFLC GGTLINQDWV
     VTAAHCDSEN FQLLFGVHSK KILNEDEQTR DPKEKFFCPN RKNDDEVDKD IMLIKLDSSV
     SNSTHIAPLS LPSSPPSVGS VCRIMGWGKT IPTKEIYPDV PHCANINILD HAVCRAAYSW
     RTVANTTLCA GILQGGKDTC HADSGGPLIC NGQVQGIVSW GGHPCGQPRE PGVYTKVLDY
     NDWVQSIIAG NTEATCPP