ID   VSPH_PROJR              Reviewed;         260 AA.
AC   B0ZT25;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Snake venom serine protease homolog {ECO:0000303|PubMed:18590752};
DE            Short=TjsvSPH {ECO:0000303|PubMed:18590752};
DE   AltName: Full=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], PROTEIN SEQUENCE OF 25-67, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=18590752; DOI=10.1016/j.toxicon.2008.05.013;
RA   Wu J., Jin Y., Zhong S., Chen R., Zhu S., Wang W., Lu Q., Xiong Y.;
RT   "A unique group of inactive serine protease homologues from snake venom.";
RL   Toxicon 52:277-284(2008).
CC   -!- FUNCTION: Snake venom serine protease homolog (PubMed:18590752). May
CC       act in the hemostasis system of the prey (Probable).
CC       {ECO:0000269|PubMed:18590752, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18590752}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18590752}.
CC   -!- MISCELLANEOUS: Is devoid of arginine esterase, fibrinogenolytic and
CC       proteolytic activities. {ECO:0000269|PubMed:18590752}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Arg-67 is present instead of the conserved His which is
CC       expected to be an active site residue. {ECO:0000305}.
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DR   EMBL; EU400543; ABZ04157.1; -; mRNA.
DR   AlphaFoldDB; B0ZT25; -.
DR   SMR; B0ZT25; -.
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   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:0000269|PubMed:18590752"
FT                   /id="PRO_0000359441"
FT   CHAIN           25..260
FT                   /note="Snake venom serine protease homolog"
FT                   /id="PRO_5000311702"
FT   DOMAIN          25..251
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        112
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        206
FT                   /note="Charge relay system"
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   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;  28794 MW;  5C80B816B80CDA41 CRC64;
     MVLVRVLANL LMLQLSYAQK SSELIIGGDE CNINEHRFLV ALYTFRSRRF HCSGTLINEE
     WVLSAARCDR KNIRIQLGMH STNVINEDVQ TRVPKEKFFC LSSKTYTKWN KDIMLIRLKK
     PVNNSTHIAP VSLPSNPPSL GSVCRVMGWG TISATKETHP DVPYCANINI LDYSVCRAAY
     ARLPATSRTL CAGILEGGKD SCLTDSGGPL ICNGQFQGIV SWGGHPCGQP RKPGLYTKVF
     DHLDWIKSII AGNKDATCPP