ID   VSPR1_BITRH             Reviewed;          89 AA.
AC   P86497;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Snake venom serine protease rhinocerase {ECO:0000303|PubMed:20300193};
DE            Short=SVSP rhinocerase {ECO:0000303|PubMed:20300193};
DE            EC=3.4.21.-;
DE   AltName: Full=Rhinocerase 1 {ECO:0000305};
DE   Flags: Fragments;
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   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=20300193; DOI=10.1371/journal.pone.0009687;
RA   Vaiyapuri S., Harrison R.A., Bicknell A.B., Gibbins J.M., Hutchinson G.;
RT   "Purification and functional characterisation of rhinocerase, a novel
RT   serine protease from the venom of Bitis gabonica rhinoceros.";
RL   PLoS ONE 5:E9687-E9687(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-15, 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 cleaves fibrinogen alpha and
CC       beta chains (FGA and FGB), but not gamma chains. Exhibits fibrinolytic
CC       and kininogenolytic. Preferentially cleaves after Arg and Lys residues.
CC       {ECO:0000269|PubMed:20300193}.
CC   -!- ACTIVITY REGULATION: Inhibited by PMSF. Not inhibited by benzamidine.
CC       {ECO:0000269|PubMed:20300193}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=80.05 uM for Arg-AMC {ECO:0000269|PubMed:20300193};
CC         KM=20.29 uM for Ala-Leu-Lys-AMC {ECO:0000269|PubMed:20300193};
CC         KM=32.19 uM for Ala-Leu-Arg-AMC {ECO:0000269|PubMed:20300193};
CC       pH dependence:
CC         Optimum pH is 7.4. {ECO:0000269|PubMed:20300193};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:20300193};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17559253,
CC       ECO:0000269|PubMed:20300193}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17559253, ECO:0000305|PubMed:20300193}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:20300193}.
CC   -!- MISCELLANEOUS: Does not have clotting activities. Does not stimulate
CC       platelet aggregation. Does not act on plasminogen (PubMed:20300193).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P86497; -.
DR   SMR; P86497; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fibrinolytic toxin;
KW   Glycoprotein; Hemostasis impairing toxin; Hydrolase; Hypotensive agent;
KW   Protease; Secreted; Serine protease; Toxin.
FT   CHAIN           1..>89
FT                   /note="Snake venom serine protease rhinocerase"
FT                   /id="PRO_0000394443"
FT   DOMAIN          1..>89
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        45
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P09872,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT                   ProRule:PRU10078, ECO:0000255|PROSITE-ProRule:PRU10079"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000250|UniProtKB:P09872,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        27..?
FT                   /evidence="ECO:0000250|UniProtKB:P09872,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        ?..53
FT                   /evidence="ECO:0000250|UniProtKB:P09872,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        64..69
FT                   /evidence="ECO:0000250|UniProtKB:P09872,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_CONS        37..38
FT                   /evidence="ECO:0000305"
FT   NON_CONS        50..51
FT                   /evidence="ECO:0000305"
FT   NON_CONS        66..67
FT                   /evidence="ECO:0000305"
FT   NON_TER         89
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   89 AA;  9978 MW;  E5941447CCA57BE2 CRC64;
     VIGGAECDIN EHPSLALIYS TSMRFHCAGT LLNQEWVSFT MWDKDIMLIR TLCAGVLEGG
     KDTCLAHPCA QPLLPAFYTK VFDYIPWIK