VSPBF_MACLB
ID VSPBF_MACLB Reviewed; 257 AA.
AC E0Y419;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Beta-fibrinogenase;
DE Short=VLBF;
DE EC=3.4.21.-;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor;
OS Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX NCBI_TaxID=8709;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom;
RX PubMed=20950666; DOI=10.1016/j.biochi.2010.10.004;
RA Siigur E., Tonismagi K., Trummal K., Samel M., Vija H., Aaspollu A.,
RA Ronnholm G., Subbi J., Kalkkinen N., Siigur J.;
RT "A new tyrosine-specific chymotrypsin-like and angiotensin-degrading serine
RT proteinase from Vipera lebetina snake venom.";
RL Biochimie 93:321-330(2011).
RN [2]
RP PROTEIN SEQUENCE OF 25-43, GLYCOSYLATION, SIALIC ACID CONTENT, AND MASS
RP SPECTROMETRY.
RX PubMed=11602278; DOI=10.1016/s0041-0101(01)00187-8;
RA Samel M., Subbi J., Siigur J., Siigur E.;
RT "Biochemical characterization of fibrinogenolytic serine proteinases from
RT Vipera lebetina snake venom.";
RL Toxicon 40:51-54(2002).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom;
RX PubMed=2028469; DOI=10.1016/0041-0101(91)90043-q;
RA Siigur E., Mahar A., Siigur J.;
RT "Beta-fibrinogenase from the venom of Vipera lebetina.";
RL Toxicon 29:107-118(1991).
RN [4]
RP FUNCTION.
RX PubMed=11910177; DOI=10.1159/000048055;
RA Siigur J., Aaspollu A., Tonismagi K., Trummal K., Samel M., Vija H.,
RA Subbi J., Siigur E.;
RT "Proteases from Vipera lebetina venom affecting coagulation and
RT fibrinolysis.";
RL Haemostasis 31:123-132(2001).
CC -!- FUNCTION: Snake venom serine protease that has fibrinogenolytic
CC activities by hydrolyzing the beta chain of fibrinogen (FGB). Typical
CC arginine esterase which hydrolyzes esters and amides of arginine.
CC {ECO:0000269|PubMed:11910177, ECO:0000269|PubMed:2028469}.
CC -!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP) and
CC PMSF. {ECO:0000269|PubMed:2028469}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=77 uM for N-alpha-benzoyl-L-arginine ethyl ester (BAEE) (at pH 8.5
CC and 25 degrees Celsius) {ECO:0000269|PubMed:2028469};
CC KM=0.36 mM for Tosyl-L-arginine methyl ester (TAME) (at pH 8.5 and 25
CC degrees Celsius) {ECO:0000269|PubMed:2028469};
CC KM=0.18 mM for BAPNA (at pH 8.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:2028469};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Glycosylated. Contains 23.0% of hexoses, 8.3% of hexosamines and
CC 1.0% of sialic acids. {ECO:0000269|PubMed:11602278}.
CC -!- MASS SPECTROMETRY: Mass=42200; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11602278};
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; GU570566; ADN04917.1; -; mRNA.
DR AlphaFoldDB; E0Y419; -.
DR SMR; E0Y419; -.
DR MEROPS; S01.520; -.
DR BRENDA; 3.4.21.74; 6665.
DR SABIO-RK; E0Y419; -.
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 Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW Serine protease; Sialic acid; Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000269|PubMed:11602278"
FT /id="PRO_0000416403"
FT CHAIN 25..257
FT /note="Beta-fibrinogenase"
FT /id="PRO_0000416404"
FT DOMAIN 25..248
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 49..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 97..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 141..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 173..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 199..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 33
FT /note="I -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 28297 MW; D8DB292C98AF5AA4 CRC64;
MVLIRVLANL LLLQLSHAQK SSELVVGGDE CNINEHRSLV FLYNSSFGCG GTLINQEWVL
SAAHCDMENM RIYLGWHNFS LPNMNQKRRV AKEKFFCLSS KNYTEWDKDI MLIKMNRPVT
YSTHVAPLSL PSSPPSVGSV CRIMGWGAIT SPNETYPDVP HCANINILNY TVCRAAHPWL
PAQSRTLCAG ILQGGIDTCK GDSGGPLICN GQIQGIVSWG DNPCAQPLKP GHYTNVFDYT
DWIQSIIAGN TTATCPP
