ID   VSPG_GLOUS              Reviewed;         260 AA.
AC   Q8UVX1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Snake venom serine protease gussurobin;
DE            Short=SVSP;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Gloydius ussuriensis (Ussuri mamushi) (Gloydius blomhoffii ussuriensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=35671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Zhao Y., Fang K., Sun K.;
RT   "cDNA for thrombin-like serine protease from venom gland of Agkistrodon
RT   ussuriensis.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=11958136;
RA   Yang Q., Hu X.-J., Xu X.-M., An L.-J., Yuan X.-D., Su Z.-G.;
RT   "Cloning, expression and purification of gussurobin, a thrombin-like enzyme
RT   from the snake venom of Gloydius ussuriensis.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:6-10(2002).
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 {ECO:0000250}.
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}.
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DR   EMBL; AF336126; AAL68708.1; -; mRNA.
DR   EMBL; AF370124; AAM46086.1; -; mRNA.
DR   AlphaFoldDB; Q8UVX1; -.
DR   SMR; Q8UVX1; -.
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: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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000295821"
FT   CHAIN           25..260
FT                   /note="Snake venom serine protease gussurobin"
FT                   /id="PRO_0000295822"
FT   DOMAIN          25..251
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        67
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        112
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        206
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
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;  28530 MW;  00514BE487B6F84C CRC64;
     MVLIRVLANL LILQLSYAQK SSELIIGGDE CNINEHRFLV ALYTSRSRRF YCGGTLINQE
     WVLTAAHCDR KNIRIKLGMH SEKVPNEDAQ TRVPKEKFFC LSSKTYTKWD KDIMLMRLKR
     PVNNSTHIAP VSLPSNPPSV GSVCRVMGWG TITSPQETYP DVPHCANINI LDYEVCQAAH
     GGLPATSRTL CAGILKGGKD SCKGDSGGPL ICNGQFQGIA SWGAHPCGQS LKPGVYTKVF
     DYTEWIQSTI AGNTDATCPP