ID   VSPH_BOTJA              Reviewed;         253 AA.
AC   Q5W958;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Snake venom serine protease homolog HS120;
DE   AltName: Full=Venom serine proteinase-like HS120;
DE   Flags: Precursor;
OS   Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15876446; DOI=10.1016/j.toxicon.2005.03.011;
RA   Saguchi K., Hagiwara-Saguchi Y., Murayama N., Ohi H., Fujita Y.,
RA   Camargo A.C.M., Serrano S.M.T., Higuchi S.;
RT   "Molecular cloning of serine proteinases from Bothrops jararaca venom
RT   gland.";
RL   Toxicon 46:72-83(2005).
CC   -!- FUNCTION: Snake venom serine protease homolog that may act in the
CC       hemostasis system of the prey. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:15876446}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15876446}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved His residue in position 64 essential for
CC       protease activity. {ECO:0000305}.
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DR   EMBL; AB178323; BAD66929.1; -; mRNA.
DR   AlphaFoldDB; Q5W958; -.
DR   SMR; Q5W958; -.
DR   MEROPS; S01.456; -.
DR   PRIDE; Q5W958; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; 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   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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Secreted;
KW   Serine protease homolog; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000294990"
FT   CHAIN           25..253
FT                   /note="Snake venom serine protease homolog HS120"
FT                   /id="PRO_5000051173"
FT   DOMAIN          25..244
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        49..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        98..251
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        137..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        169..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        195..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   253 AA;  27815 MW;  C79EF86998DF356C CRC64;
     MVLIRVIANL LILQLSYAQK SSELVIGGDE CNINEHPFLA FLYTGWIFCS GTLINKEWVL
     TVKQCNNRRP MRIYLGMHTR SVPNDDEEIR YPKEMFICPN KKKNDIMLIR LNRPVNNSEH
     IAPLSLPSNP PSVGSVCRIM GWGTITPSKA TYPDVPHCAN INLFNYTVCR GAHAGLPVTS
     RKLCAGVLEG GIDTCSADSG GPLICNGQLQ GIVSWRGGSC AQPHKPGLYT KVFDYLPWIQ
     SIIAGSTTAT CPP