ID   VSPH_BOTJR              Reviewed;         260 AA.
AC   Q7T229;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Snake venom serine protease homolog;
DE   AltName: Full=Serine proteinase-like protein;
DE   Flags: Precursor;
OS   Bothrops jararacussu (Jararacussu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15134836; DOI=10.1016/j.biochi.2004.02.002;
RA   Kashima S., Roberto P.G., Soares A.M., Astolfi-Filho S., Pereira J.O.,
RA   Giuliati S., Faria M. Jr., Xavier M.A.S., Fontes M.R.M., Giglio J.R.,
RA   Franca S.C.;
RT   "Analysis of Bothrops jararacussu venomous gland transcriptome focusing on
RT   structural and functional aspects: I -- gene expression profile of highly
RT   expressed phospholipases A2.";
RL   Biochimie 86:211-219(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 86-109, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=15994137; DOI=10.1016/j.jchromb.2005.04.018;
RA   De-Simone S.G., Correa-Netto C., Antunes O.A., De-Alencastro R.B.,
RA   Silva F.P. Jr.;
RT   "Biochemical and molecular modeling analysis of the ability of two p-
RT   aminobenzamidine-based sorbents to selectively purify serine proteases
RT   (fibrinogenases) from snake venoms.";
RL   J. Chromatogr. B 822:1-9(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:0000269|PubMed:15994137}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15994137}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved His residue in position 67 essential for
CC       protease activity. {ECO:0000305}.
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DR   EMBL; AY251282; AAP42416.1; -; mRNA.
DR   AlphaFoldDB; Q7T229; -.
DR   SMR; Q7T229; -.
DR   MEROPS; S01.509; -.
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   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; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Secreted; Serine protease homolog; Signal;
KW   Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000296363"
FT   CHAIN           25..260
FT                   /note="Snake venom serine protease homolog"
FT                   /id="PRO_0000296364"
FT   DOMAIN          25..251
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        52..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        100..258
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        144..212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        176..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        202..227
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        99
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   260 AA;  28654 MW;  9E633F098E51F8CF CRC64;
     MVLIRVLANL LILQLSYAQK ASELIIGGDE CNINEHRFLV ALYTSRSRRF HCSGTLINQE
     WVLTAANCDR KNIRIKLGMH SKNVTNEDEQ TRVPKEKFFC LSSKTYTKWD KDIMLIRLKR
     PVNDSPHIAP ISLPSSPPSV GSVCRIMGWG TISPTKVSYP DVPHCANINL LDYEVCRAAH
     GGLPATSRTL CAGILEGGKD SCQGDSGGPL ICNGQFQGIL SWGVHPCGQR LKPGVYTKVS
     DYTEWIRSII AGNTDVTCPP