VSPGL_GLOSH
ID VSPGL_GLOSH Reviewed; 260 AA.
AC P0C5B4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Thrombin-like enzyme gloshedobin;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Defibrase;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor;
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].
RC TISSUE=Venom gland;
RA Yang Q., Xu X.-M., Li M., Yuan X.-D., Su Z.-G., Janson J.-C., An L.-J.;
RT "Cloning and expression of defibrase cDNA from the venom of Gloydius
RT shedaoensis.";
RL Biotechnol. Lett. 24:135-138(2002).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19286459; DOI=10.1016/j.pep.2009.03.003;
RA Yang D., Peng M., Yang H., Yang Q., Xu J.;
RT "Expression, purification and characterization of Gloydius shedaoensis
RT venom gloshedobin as Hsp70 fusion protein in Pichia pastoris.";
RL Protein Expr. Purif. 66:138-142(2009).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19639313; DOI=10.1007/s00253-009-2141-2;
RA Jiang X., Xu J., Yang Q.;
RT "Soluble expression, purification, and characterization of Gloydius
RT shedaoensis venom gloshedobin in Escherichia coli by using fusion
RT partners.";
RL Appl. Microbiol. Biotechnol. 85:635-642(2010).
RN [4]
RP 3D-STRUCTURE MODELING, INTERACTION WITH PMSF, SITE, AND ACTIVITY
RP REGULATION.
RX PubMed=20969888; DOI=10.1016/j.ijbiomac.2010.10.007;
RA Jiang X., Chen L., Xu J., Yang Q.;
RT "Molecular mechanism analysis of Gloydius shedaoensis venom gloshedobin
RT interaction with inhibitors by homology modeling.";
RL Int. J. Biol. Macromol. 48:129-133(2011).
CC -!- FUNCTION: Thrombin-like snake venom serine protease. The recombinant
CC form clots fibrinogen by cleaving fibrinogen Aalpha chain (FGA), and
CC slowly Bbeta chain (FGB). Has amidolytic activities.
CC {ECO:0000269|PubMed:19286459, ECO:0000269|PubMed:19639313}.
CC -!- ACTIVITY REGULATION: Completely inhibited by PMSF, and N-tosyl-
CC Lphenylalanine chloromethyl ketone (TPCK) and poorly inhibited by
CC benzamidine and derivates. Not inhibited by EDTA, heparin and hirudin.
CC {ECO:0000269|PubMed:19286459, ECO:0000269|PubMed:19639313,
CC ECO:0000269|PubMed:20969888}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:19286459,
CC ECO:0000269|PubMed:19639313};
CC Temperature dependence:
CC Optimum temperature is 40-50 degrees Celsius.
CC {ECO:0000269|PubMed:19286459, ECO:0000269|PubMed:19639313};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Has no activity on gamma chain.
CC {ECO:0000305|PubMed:19639313}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AJ278786; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0C5B4; -.
DR SMR; P0C5B4; -.
DR MEROPS; S01.509; -.
DR BRENDA; 3.4.21.74; 8184.
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 Blood coagulation cascade activating toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000250"
FT /id="PRO_0000308996"
FT CHAIN 25..260
FT /note="Thrombin-like enzyme gloshedobin"
FT /id="PRO_0000296369"
FT DOMAIN 25..252
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 SITE 206
FT /note="Forms a covalent bond with the inhibitor PMSF"
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"
FT CONFLICT 151
FT /note="T -> TT (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 28616 MW; 7B2F42AFE0915449 CRC64;
MVLIRVQANL LILQLSYAQK SSELIIGGDE CNINEHRFLV ALYTSRSRRF YCGGTLINQE
WVLTAAHCDR KNIRIKLGMH SEKVPNEDAE TRVPKEKFFC LSSKTYTKWD KDIMLMRLKR
PVNNSTHIAP VSLPSNPPSV DSVCRVMGWG TITSPQETYP DVPHCANINI LDYEVCQAAH
GGLPATSRTL CAGILKGGKD SCKGDSGGPL ICNGQFQGIA SWGAHPCGQS LKPGVYTKVF
DYTEWIQSII AGNTDATCPP
