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Thrombin-like enzyme gloshedobin (SVTLE) (EC 3.4.21.-) (Defibrase) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)

 VSPGL_GLOSH             Reviewed;         260 AA.
P0C5B4;
24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
10-MAY-2017, entry version 35.
RecName: Full=Thrombin-like enzyme gloshedobin;
Short=SVTLE;
EC=3.4.21.-;
AltName: Full=Defibrase;
AltName: Full=Fibrinogen-clotting enzyme;
AltName: Full=Snake venom serine protease;
Short=SVSP;
Flags: Precursor;
Gloydius shedaoensis (Shedao island pit viper) (Agkistrodon
shedaoensis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
NCBI_TaxID=88083;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
Yang Q., Xu X.-M., Li M., Yuan X.-D., Su Z.-G., Janson J.-C.,
An L.-J.;
"Cloning and expression of defibrase cDNA from the venom of Gloydius
shedaoensis.";
Biotechnol. Lett. 24:135-138(2002).
[2]
FUNCTION, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19286459; DOI=10.1016/j.pep.2009.03.003;
Yang D., Peng M., Yang H., Yang Q., Xu J.;
"Expression, purification and characterization of Gloydius shedaoensis
venom gloshedobin as Hsp70 fusion protein in Pichia pastoris.";
Protein Expr. Purif. 66:138-142(2009).
[3]
FUNCTION, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19639313; DOI=10.1007/s00253-009-2141-2;
Jiang X., Xu J., Yang Q.;
"Soluble expression, purification, and characterization of Gloydius
shedaoensis venom gloshedobin in Escherichia coli by using fusion
partners.";
Appl. Microbiol. Biotechnol. 85:635-642(2010).
[4]
3D-STRUCTURE MODELING, INTERACTION WITH PMSF, SITE, AND ENZYME
REGULATION.
PubMed=20969888; DOI=10.1016/j.ijbiomac.2010.10.007;
Jiang X., Chen L., Xu J., Yang Q.;
"Molecular mechanism analysis of Gloydius shedaoensis venom
gloshedobin interaction with inhibitors by homology modeling.";
Int. J. Biol. Macromol. 48:129-133(2011).
-!- FUNCTION: Thrombin-like snake venom serine protease. The
recombinant form clots fibrinogen by cleaving fibrinogen Aalpha
chain (FGA), and slowly Bbeta chain (FGB). Has amidolytic
activities. {ECO:0000269|PubMed:19286459,
ECO:0000269|PubMed:19639313}.
-!- ENZYME REGULATION: Completely inhibited by PMSF, and N-tosyl-
Lphenylalanine chloromethyl ketone (TPCK) and poorly inhibited by
benzamidine and derivates. Not inhibited by EDTA, heparin and
hirudin. {ECO:0000269|PubMed:19286459,
ECO:0000269|PubMed:19639313, ECO:0000269|PubMed:20969888}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:19286459,
ECO:0000269|PubMed:19639313};
Temperature dependence:
Optimum temperature is 40-50 degrees Celsius.
{ECO:0000269|PubMed:19286459, ECO:0000269|PubMed:19639313};
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- MISCELLANEOUS: Has no activity on gamma chain.
{ECO:0000305|PubMed:19639313}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; AJ278786; -; NOT_ANNOTATED_CDS; mRNA.
ProteinModelPortal; P0C5B4; -.
SMR; P0C5B4; -.
MEROPS; S01.509; -.
HOVERGEN; HBG013304; -.
BRENDA; 3.4.21.74; 8184.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Blood coagulation cascade activating toxin; Disulfide bond;
Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease;
Secreted; Serine protease; Signal; Toxin; Zymogen.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 24 {ECO:0000250}.
/FTId=PRO_0000308996.
CHAIN 25 260 Thrombin-like enzyme gloshedobin.
/FTId=PRO_0000296369.
DOMAIN 25 252 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 67 67 Charge relay system. {ECO:0000250}.
ACT_SITE 112 112 Charge relay system. {ECO:0000250}.
ACT_SITE 206 206 Charge relay system. {ECO:0000250}.
SITE 206 206 Forms a covalent bond with the inhibitor
PMSF.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 31 165 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 52 68 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 100 258 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 144 212 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 176 191 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 202 227 {ECO:0000255|PROSITE-ProRule:PRU00274}.
CONFLICT 151 151 T -> TT (in Ref. 1). {ECO:0000305}.
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


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