ID   VSP_PHIOL               Reviewed;         261 AA.
AC   Q09GK1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Philodryas olfersii (Green snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Dipsadidae; Philodryas.
OX   NCBI_TaxID=120305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16857193; DOI=10.1016/j.febslet.2006.07.010;
RA   Ching A.T.C., Rocha M.M.T., Paes Leme A.F., Pimenta D.C., Furtado M.F.D.,
RA   Serrano S.M.T., Ho P.L., Junqueira-de-Azevedo I.L.M.;
RT   "Some aspects of the venom proteome of the Colubridae snake Philodryas
RT   olfersii revealed from a Duvernoy's (venom) gland transcriptome.";
RL   FEBS Lett. 580:4417-4422(2006).
RN   [2]
RP   ERRATUM OF PUBMED:16857193.
RA   Ching A.T.C., Rocha M.M.T., Paes Leme A.F., Pimenta D.C., Furtado M.F.D.,
RA   Serrano S.M.T., Ho P.L., Junqueira-de-Azevedo I.L.M.;
RL   FEBS Lett. 580:5122-5123(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ912657; ABI74694.1; -; mRNA.
DR   AlphaFoldDB; Q09GK1; -.
DR   SMR; Q09GK1; -.
DR   MEROPS; S01.481; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW   Protease; Secreted; Serine protease; Signal; Toxin; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000296370"
FT   CHAIN           25..261
FT                   /note="Snake venom serine protease"
FT                   /id="PRO_0000296371"
FT   DOMAIN          25..249
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        110
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        98..256
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        142..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        174..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        200..225
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   261 AA;  28447 MW;  B49A9358935DF874 CRC64;
     MALIGVLANL LILCLSYART APDRIIGGLE CNQNEHRSLV LLYNSGGFFC SGTLINHEWV
     LTAAHCNREN IQIKLGVHNI HVPNEDEQIR VPKEKVCCLG TMNCTQWNQD IMLIRLNSSV
     NYSTHIAPLS LPSNPPSVGS VCRVMGWGTI TSPEVTYPEV PHCVNIQILH KELCEAAYPI
     LLGNSNILCA GKLLGDKDSC KGDSGGPLIC NGQIQGIVSW GGFPCAQILE PGVYTKVFDY
     IDWIQDIMAG NANVICPGDN F