ID   VSPSN_GLOHA             Reviewed;         260 AA.
AC   O73800; O93502;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Snake venom serine protease salmobin;
DE            Short=SVSP;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=8714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=11166806; DOI=10.1016/s0141-0229(00)00315-x;
RA   Jeong H., Yoo S., Kim E.;
RT   "Cell surface display of salmobin, a thrombin-like enzyme from Agkistrodon
RT   halys venom on Escherichia coli using ice nucleation protein.";
RL   Enzyme Microb. Technol. 28:155-160(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Chung K.H., Koh Y.S., Yun Y.D., Kim D.-S.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Snake venom serine protease that may act in the hemostasis
CC       system of the prey. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; AF056033; AAC13280.1; -; mRNA.
DR   EMBL; AF015727; AAC61838.1; -; mRNA.
DR   AlphaFoldDB; O73800; -.
DR   SMR; O73800; -.
DR   MEROPS; S01.338; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW   Protease; Secreted; Serine protease; Signal; Toxin; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000296197"
FT   CHAIN           25..260
FT                   /note="Snake venom serine protease salmobin"
FT                   /id="PRO_0000296198"
FT   DOMAIN          25..251
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        67
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        112
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        206
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        52..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        102..258
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        144..212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        176..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        202..227
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        5..10
FT                   /note="KVLANH -> RVIANL (in Ref. 2; AAC61838)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="D -> V (in Ref. 2; AAC61838)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257
FT                   /note="N -> T (in Ref. 2; AAC61838)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   260 AA;  29219 MW;  E185EAA1BC5FAC10 CRC64;
     MVLIKVLANH LILQLSYAQK SSELVIGGDE CNINEHRFLV ALYHSRSRTF LCGGTLINQE
     WVLTAAHCDR FLMYIRLGMH NKNVKFDDEQ RRFPKEKYFF ACSNNFTKWD KDIMLIRLNR
     PVNNSEHIAP LSLPSNPPSV GSVCRVMGWG TITSPNETLP DVPHCANINL LHYSVCQAAY
     PKLPVTRRLL CAGILEGGID SCHRDSGGPL ICNGQFQGIV SWGRYPCAQP RVPGIYIKVF
     DYTDWIQSII AGNTAVNCPP