ID   VSPH1_BITGA             Reviewed;         260 AA.
AC   Q6T6S7;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Snake venom serine protease homolog 1;
DE   AltName: Full=Venom serine proteinase-like protein 1;
DE   Flags: Precursor;
OS   Bitis gabonica (Gaboon adder) (Gaboon viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15276202; DOI=10.1016/j.gene.2004.03.024;
RA   Francischetti I.M.B., My-Pham V., Harrison J., Garfield M.K.,
RA   Ribeiro J.M.C.;
RT   "Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the
RT   full-length transcripts (cDNA) and proteins.";
RL   Gene 337:55-69(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 50-59; 83-95; 109-117 AND 157-169, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17203976; DOI=10.1021/pr060494k;
RA   Calvete J.J., Marcinkiewicz C., Sanz L.;
RT   "Snake venomics of Bitis gabonica gabonica. Protein family composition,
RT   subunit organization of venom toxins, and characterization of dimeric
RT   disintegrins bitisgabonin-1 and bitisgabonin-2.";
RL   J. Proteome Res. 6:326-336(2007).
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:17203976}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:17203976}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved His residue in position 67 and the
CC       conserved Ser residue in position 206 essential for protease activity.
CC       {ECO:0000305}.
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DR   EMBL; AY430410; AAR24534.1; -; mRNA.
DR   AlphaFoldDB; Q6T6S7; -.
DR   SMR; Q6T6S7; -.
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   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.
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_0000294982"
FT   CHAIN           25..260
FT                   /note="Snake venom serine protease homolog 1"
FT                   /id="PRO_0000294983"
FT   DOMAIN          25..251
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        253
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"
SQ   SEQUENCE   260 AA;  28982 MW;  2D668E4927640F9C CRC64;
     MVLIRVLANL LLLQLSYAQE SSELVIGGDE CDINEHPFLV ALHTARSKRF HCAGTLLNKE
     WVLTAARCDR KNIRIKFGVH NKNVQNEDEE MRVPKEKHFC VSSKTYTRWD KDIMLIRLKR
     PVNDGTHIAP LSLPSNPPSV GSVCRIMGWG SITTTKVTYP DVPHCANIKL FDYSVCRDAY
     KGLPEKSRTL CAGILEGGID SCKVDNGGPL ICNGQFQGIG SWEGHPCAQP LKPALYTNVF
     EYTDWIEGII ARNTTVTCPP