VSPSH_GLOSH
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