ID   VSPSH_GLOSH             Reviewed;         238 AA.
AC   Q6T5L0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Alpha-fibrinogenase shedaoenase;
DE            EC=3.4.21.-;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
OS   Gloydius shedaoensis (Shedao island pit viper) (Agkistrodon shedaoensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=88083;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-10, FUNCTION, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=16331328; DOI=10.1111/j.1745-7270.2005.00119.x;
RA   Jiao H.-M., Yang L.-X., Lu B., Wu Y.-Q., Zhou Y.-C.;
RT   "Shedaoenase, a novel fibrinogenase from the venom of Agkistrodon
RT   shedaoenthesis Zhao.";
RL   Acta Biochim. Biophys. Sin. 37:835-842(2005).
CC   -!- FUNCTION: Snake venom protease that shows fibrinogenolytic activities.
CC       Preferentially degrades the alpha-chain of human fibrinogen (FGA) and
CC       slowly degrades the beta-chain (FGB). Has no effect on the gamma-chain.
CC       Can hydrolyze fibrinogen without forming fibrin clots and also can
CC       degrade fibrin. Hydrolyzes the substrate of plasmin more potently than
CC       the substrate of thrombin. Shows a preferential cleavage at Lys-|-Xaa
CC       instead of Arg-|-Xaa bonds. {ECO:0000269|PubMed:16331328}.
CC   -!- ACTIVITY REGULATION: Its activity is completely inhibited by PMSF, and
CC       almost not inhibited by EDTA. {ECO:0000269|PubMed:16331328}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16331328}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:16331328}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAR11859.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY434726; AAR11859.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q6T5L0; -.
DR   SMR; Q6T5L0; -.
DR   MEROPS; S01.335; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW   Fibrinolytic toxin; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW   Protease; Secreted; Serine protease; Toxin.
FT   CHAIN           1..238
FT                   /note="Alpha-fibrinogenase shedaoenase"
FT                   /id="PRO_0000296368"
FT   DOMAIN          1..229
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   MOTIF           181..183
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        43
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        88
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        184
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        7..141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        76..236
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        120..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        152..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        180..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        2
FT                   /note="I -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   238 AA;  26416 MW;  0D3183F17AE1E4BD CRC64;
     VIGGDECNIN EHRFLVALYT SRFRTLFCGG TLINQEWVLT AAHCDRKNFR IKLGIHSKKV
     PNEDEQTRVP KEKFFCLSSK NYTLWDKDIM LIRLDSPVKN STHIAPFSLP SSPPSVGSVC
     RIMGWGRISP TEETYPDVPH CVNINLLEYE MCRVPYPEFG LPATSRTLCA GILEGGKDTC
     RGDSGGPLIC NGQFQGIASW GDDPCAQPHK PAAYTKVFDH LDWIKSIIAG NTDASCPP