ID   VSPH1_PROJR             Reviewed;         260 AA.
AC   Q9DF68;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Snake venom serine protease homolog;
DE   AltName: Full=SP1 {ECO:0000312|EMBL:AAG10788.1};
DE   AltName: Full=Venom serine proteinase-like protein;
DE   Flags: Precursor;
OS   Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=242841;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Lu Q.M., Jin Y., Wei J.F., Wang W.Y., Xiong Y.L.;
RT   "cDNA cloning of serine proteinases from the venom of Trimeresurus
RT   jerdonii.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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:0000305|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- CAUTION: Has lost two of the three essential catalytic residues and so
CC       probably has no enzymatic activity. {ECO:0000305}.
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DR   EMBL; AF292110; AAG10788.1; -; mRNA.
DR   AlphaFoldDB; Q9DF68; -.
DR   SMR; Q9DF68; -.
DR   MEROPS; S01.509; -.
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:InterPro.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Secreted;
KW   Serine protease homolog; Signal; Toxin; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028401"
FT   CHAIN           25..260
FT                   /note="Snake venom serine protease homolog"
FT                   /id="PRO_0000028402"
FT   DOMAIN          25..251
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  28614 MW;  1692283141E12896 CRC64;
     MVLVRVLANL LMLQLSYAQK SSELIIGGDE CNINEHRFLV ALYTFRSRRF HCSGTLINEE
     WVLSAARCDR KNIRIQLGMH STNVINEDVQ TRVPKEKFSC LSSKTYTKWN KDIMLIRLKK
     PVNNSTHIAP VSLPSNPPTL GSVCRVMGWG TISATKETHP DVPLCANINI LDYSVCRAAY
     ARLPATSRTL CAGILEGGID TCKGDPGGPL ICNGQFQGIV SWGSDPCAKP HEPGSYTKVF
     DHLNWIQSII AGNTTATCPP