VSPB_GLOBL
ID VSPB_GLOBL Reviewed; 233 AA.
AC Q9PT51;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Beta-fibrinogenase brevinase;
DE EC=3.4.21.-;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Contains:
DE RecName: Full=Beta-fibrinogenase brevinase chain A;
DE Contains:
DE RecName: Full=Beta-fibrinogenase brevinase chain B;
OS Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=242054;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=10845699; DOI=10.1006/abbi.2000.1782;
RA Lee J.-W., Park W.;
RT "cDNA cloning of brevinase, a heterogeneous two-chain fibrinolytic enzyme
RT from Agkistrodon blomhoffii brevicaudus snake venom, by serial
RT hybridization-polymerase chain reaction.";
RL Arch. Biochem. Biophys. 377:234-240(2000).
RN [2]
RP PROTEIN SEQUENCE OF 1-30 AND 78-107, FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=10403823; DOI=10.1006/bbrc.1999.0977;
RA Lee J.-W., Seu J.-H., Rhee I.-K., Jin I., Kawamura Y., Park W.;
RT "Purification and characterization of brevinase, a heterogeneous two-chain
RT fibrinolytic enzyme from the venom of Korean snake, Agkistrodon blomhoffii
RT brevicaudus.";
RL Biochem. Biophys. Res. Commun. 260:665-670(1999).
CC -!- FUNCTION: Snake venom serine protease that has fibrinogenolytic
CC activities. Preferentially cleaves the Bbeta-chain (FGB) and more
CC slowly the Aa-chain (FGA) of fibrinogen, but does not affect the gamma-
CC chain. Has also fibrinolytic activity. May play a role in
CC antithrombotic reaction as well as thrombolytic reaction.
CC {ECO:0000269|PubMed:10403823}.
CC -!- ACTIVITY REGULATION: The fibrinolytic activity is completely inhibited
CC by PMSF, diisopropylfluorophosphate (DFP), pefabloc, dithiothreitol
CC (DTT) and Zn(2+), but not by Pepstatin A, E64, iodoacetate,
CC chymostatin, tosyl-Lphenylalanine chloromethyl ketone (TPCK), soybean
CC trypsin inhibitor (SBTI), phosphoramidon, Ca(2+), Co(2+), Cu(2+),
CC Fe(2+), Mg(2+), Mn(2+), K(+), and Na(+). {ECO:0000269|PubMed:10403823}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is from 5.5 to 8.5. {ECO:0000269|PubMed:10403823};
CC -!- SUBUNIT: Heterodimer of the brevinase A chain and the brevinase B
CC chain. {ECO:0000269|PubMed:10403823}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10403823}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:10403823}.
CC -!- MISCELLANEOUS: Is devoid of fibrinogen clotting and caseinolytic
CC activities. {ECO:0000305|PubMed:10403823}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AJ243757; CAB65936.1; -; mRNA.
DR AlphaFoldDB; Q9PT51; -.
DR SMR; Q9PT51; -.
DR MEROPS; S01.341; -.
DR PRIDE; Q9PT51; -.
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..77
FT /note="Beta-fibrinogenase brevinase chain A"
FT /id="PRO_0000294978"
FT CHAIN 78..233
FT /note="Beta-fibrinogenase brevinase chain B"
FT /id="PRO_0000294979"
FT DOMAIN 1..224
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MOTIF 176..178
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 40
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 77..78
FT /note="Cleavage"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 7..138
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 25..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 73..231
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 117..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 149..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 175..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 233 AA; 25725 MW; 1676DC5AF0AB5A42 CRC64;
VIGGDECNIN EHRFLALLYS ERFQCGGTLI NEEWVLTAAH CDMGNMYIYL GVHNVSVQYD
DEQRRYPKKK YFCLSSRNYN QWDNDIMLIR LNRPVRNSAH IAPLSLPSGP PSVGSVCRVM
GWGTITSPNE TYPDVPHCAN INILDYEVCR AAYAGLPATS RTLCAGILEG GKDSCRGDSG
GPLICNGEIQ GIVSWGGNIC AQPREPGLYT KVFDYIDWIQ SIIAGNTTVN CPP
