VSP5_PROMU
ID VSP5_PROMU Reviewed; 257 AA.
AC Q91511;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Beta-fibrinogenase mucrofibrase-5;
DE EC=3.4.21.-;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE AltName: Full=Tm-5;
DE AltName: Full=Tm-IIG;
DE Flags: Precursor;
OS Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=103944;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RC TISSUE=Venom, and Venom gland;
RX PubMed=7811255; DOI=10.1006/bbrc.1994.2865;
RA Hung C.-C., Huang K.F., Chiou S.-H.;
RT "Characterization of one novel venom protease with beta-fibrinogenase
RT activity from the Taiwan habu (Trimeresurus mucrosquamatus): purification
RT and cDNA sequence analysis.";
RL Biochem. Biophys. Res. Commun. 205:1707-1715(1994).
RN [2]
RP FUNCTION, AND PEPTIDASE ACTIVITY.
RX PubMed=10973823; DOI=10.1006/bbrc.2000.3411;
RA Hung C.C., Chiou S.H.;
RT "Expression of a kallikrein-like protease from the snake venom: engineering
RT of autocatalytic site in the fusion protein to facilitate protein
RT refolding.";
RL Biochem. Biophys. Res. Commun. 275:924-930(2000).
RN [3]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom;
RX PubMed=11237764; DOI=10.1006/bbrc.2001.4452;
RA Hung C.C., Chiou S.H.;
RT "Fibrinogenolytic proteases isolated from the snake venom of Taiwan habu:
RT serine proteases with kallikrein-like and angiotensin-degrading
RT activities.";
RL Biochem. Biophys. Res. Commun. 281:1012-1018(2001).
CC -!- FUNCTION: Snake venom serine protease with strong beta-fibrinogenolytic
CC activities, angiotensin I (AGT)-degrading activities and strong
CC kallikrein-like activities in vitro, releasing bradykinin from
CC kininogen (KNG1). Intravenous injection mildly lowers blood pressure in
CC experimental rats, which may be explained by the action on angiotensin
CC I and kininogen. Exhibits amidase activity against N-benzoyl-Pro-Phe-
CC Arg-p-nitroanilide in vitro (PubMed:10973823).
CC {ECO:0000269|PubMed:10973823, ECO:0000269|PubMed:11237764,
CC ECO:0000269|PubMed:7811255}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Heat-stable to about 95 degrees Celsius.
CC {ECO:0000269|PubMed:11237764};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7811255}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not have activity on gamma-chains of fibrinogen
CC (FGG) (PubMed:7811255), and does not coagulate human plasma. Does not
CC induce or inhibit platelet aggregation (PubMed:11237764).
CC {ECO:0000305|PubMed:11237764, ECO:0000305|PubMed:7811255}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: The correspondence between the sequence (indicated in
CC PubMed:7811255) and the function (from PubMed:11237764) has not been
CC clearly demonstrated. {ECO:0000305}.
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DR EMBL; X83225; CAA58225.1; -; mRNA.
DR AlphaFoldDB; Q91511; -.
DR SMR; Q91511; -.
DR MEROPS; S01.345; -.
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 GO; GO:0008217; P:regulation of blood pressure; 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 Disulfide bond; Fibrinogenolytic toxin; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Hypotensive agent; Protease;
KW Secreted; Serine protease; Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..24
FT /evidence="ECO:0000250"
FT /id="PRO_0000028415"
FT CHAIN 25..257
FT /note="Beta-fibrinogenase mucrofibrase-5"
FT /id="PRO_0000028416"
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 102
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"
SQ SEQUENCE 257 AA; 28164 MW; FCCF64A8EAF2827D CRC64;
MVLIRVLANL LILQLSYAQK SSELIIGGDE CNINEHPFLV LVYYDDYQCG GTLINEEWVL
TAAHCNGENM EIYLGMHSKK VPNKDRRRRV PKEKFFCDSS KNYTKWNKDI MLIRLNRPVR
KSAHIAPLSL PSSPPSVGSV CRIMGWGTIS PTKVTLPDVP RCANINLLDY EVCRAAYAGL
PATSRTLCAG ILEGGKDSCG GDSGGPLICN GQFQGIVSWG GDPCAQPHEP GLYTNVFDHL
DWIKGIIAGN TDATCPP
