ID   VSP1_CROAT              Reviewed;         262 AA.
AC   Q8QHK3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Snake venom serine protease catroxase-1;
DE            Short=SVSP;
DE            EC=3.4.21.-;
DE   AltName: Full=Catroxase I;
DE   Flags: Precursor;
OS   Crotalus atrox (Western diamondback rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Tsai I.-H., Hsu J.-C., Wang Y.-M.;
RT   "Catroxase I and II, the serine proteases of Crotalus atrox venom: cloning,
RT   complete sequencing and functional characterization.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 25-46 AND 143-187, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=19371136; DOI=10.1021/pr900249q;
RA   Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.;
RT   "Exploring the venom proteome of the western diamondback rattlesnake,
RT   Crotalus atrox, via snake venomics and combinatorial peptide ligand library
RT   approaches.";
RL   J. Proteome Res. 8:3055-3067(2009).
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   -!- MASS SPECTROMETRY: Mass=25930; Method=Unknown; Note=Average mass.;
CC       Evidence={ECO:0000269|PubMed:19371136};
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; AF227153; AAL77226.1; -; mRNA.
DR   AlphaFoldDB; Q8QHK3; -.
DR   SMR; Q8QHK3; -.
DR   MEROPS; S01.330; -.
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   InterPro; IPR033116; TRYPSIN_SER.
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.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW   Signal; Toxin; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000269|PubMed:19371136"
FT                   /id="PRO_0000296304"
FT   CHAIN           25..262
FT                   /note="Snake venom serine protease catroxase-1"
FT                   /id="PRO_5000057802"
FT   DOMAIN          25..250
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        64
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        109
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        205
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        49..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        97..257
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        141..211
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        173..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        201..226
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   262 AA;  28625 MW;  AC4A259A08D804F6 CRC64;
     MVLIRVLANL LILQLSYAQK SSEPIIGGDE CNRNEHRFLA LVSSDGNQCG GTLINEEWVL
     TAAHCEGNKM KIHLGVHSKK VPNKDKQTRV AKEKFFCVSS KNYTFWDKDI MLIRLDRPVS
     NSEHIAPLSL PSSPPSVGSV CRIMGWGTIS PTKVILPDVP HCVNINLLNY SVCRAAYPEY
     GLPATSRTLC AGILEGGKDT CVGDSGGPLI CNGQFQGIAS WGSPNCGYVR EPALYTKVFD
     HLDWIQSIIA GNTDATCPFV NF