ID   VSPR5_BITRH             Reviewed;         259 AA.
AC   D8MIA3;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Snake venom serine protease rhinocerase 5 {ECO:0000303|PubMed:21731776};
DE            Short=BG-RHIN5 {ECO:0000303|PubMed:21731776};
DE            Short=SVSP;
DE            EC=3.4.21.-;
DE   Flags: Precursor; Fragment;
OS   Bitis rhinoceros (West African gaboon viper) (Vipera rhinoceros).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=715877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ISOLATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=21731776; DOI=10.1371/journal.pone.0021532;
RA   Vaiyapuri S., Wagstaff S.C., Harrison R.A., Gibbins J.M., Hutchinson E.G.;
RT   "Evolutionary analysis of novel serine proteases in the venom gland
RT   transcriptome of Bitis gabonica rhinoceros.";
RL   PLoS ONE 6:e21532-e21532(2011).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-38, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=17559253; DOI=10.1021/pr0701714;
RA   Calvete J.J., Escolano J., Sanz L.;
RT   "Snake venomics of Bitis species reveals large intragenus venom toxin
RT   composition variation: application to taxonomy of congeneric taxa.";
RL   J. Proteome Res. 6:2732-2745(2007).
CC   -!- FUNCTION: Snake venom serine protease that may act in the hemostasis
CC       system of the prey. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17559253}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17559253}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
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DR   EMBL; FN868648; CBM40648.1; -; Genomic_DNA.
DR   MEROPS; S01.334; -.
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.
FT   SIGNAL          <1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..23
FT                   /evidence="ECO:0000305|PubMed:17559253"
FT                   /id="PRO_0000455651"
FT   CHAIN           24..259
FT                   /note="Snake venom serine protease rhinocerase 5"
FT                   /id="PRO_5003117916"
FT   DOMAIN          24..250
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        66
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        111
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        205
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        51..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        99..257
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        143..211
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        175..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        201..226
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   259 AA;  28620 MW;  75484514086EA31C CRC64;
     VLIRVLANLL LLQLSYAQES SELVIGGDEC DINEHPFLVA LHTARSKRFH CAGTLLNKEW
     VLTAAHCDME NMQIYLGLHN ISRPNQDQKR RVPKQKFFCL SNKTYTRWDK DIMLIKLNSP
     VPYSTHIAPL SLPSSPPIVG SVCRIMGWGA TKSPNENVPH VPHCANINIL HYSVCRATYG
     RLPAKSRTLC AGIPRRRIGS CLGDSGGPLI CNGQVEGIVS WASKPCVHNG APGMYTKVYD
     YTDWIRSIIG GNTSATCPL