VSPA_MACLB
ID VSPA_MACLB Reviewed; 258 AA.
AC Q8JH85;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Alpha-fibrinogenase;
DE Short=VLAF;
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 gland;
RX PubMed=12719779; DOI=10.1267/THRO03050826;
RA Siigur E., Aaspollu A., Siigur J.;
RT "Anticoagulant serine fibrinogenases from Vipera lebetina venom: structure-
RT function relationships.";
RL Thromb. Haemost. 89:826-831(2003).
RN [2]
RP PROTEIN SEQUENCE OF 25-43, GLYCOSYLATION, SIALIC ACID CONTENT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
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.
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).
RN [4]
RP FUNCTION, SUBUNIT, AND ACTIVITY REGULATION.
RC TISSUE=Venom;
RX PubMed=3304428; DOI=10.1016/0304-4165(87)90192-9;
RA Mahar A., Siigur E., Siigur J.;
RT "Purification and properties of a proteinase from Vipera lebetina (snake)
RT venom.";
RL Biochim. Biophys. Acta 925:272-281(1987).
CC -!- FUNCTION: Degrades alpha chain of fibrinogen (FGA), and has strong
CC caseinolytic activity. Cleaves oxidized insulin B-chain at '40-Tyr-|-
CC Leu-41', '48-Phe-|-Phe-49' and '49-Phe-|-Tyr-50', and glucagon at the
CC bonds '62-Tyr-|-Ser-63', 66-Leu-|-Asp-67' and '78-Leu-|-Met-79' bonds.
CC {ECO:0000269|PubMed:11910177, ECO:0000269|PubMed:3304428}.
CC -!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP) and
CC PMSF, and partially by soybean trypsin inhibitor, but not by EDTA.
CC {ECO:0000269|PubMed:3304428}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3304428}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Glycosylated. Contains 8.5% of hexoses, 5.8% of hexosamines and
CC 0.8% of sialic acids. {ECO:0000269|PubMed:11602278}.
CC -!- MASS SPECTROMETRY: Mass=31100; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12719779};
CC -!- MISCELLANEOUS: Lacks esterolytic activity.
CC {ECO:0000305|PubMed:12719779}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF528193; AAM96674.1; -; mRNA.
DR AlphaFoldDB; Q8JH85; -.
DR SMR; Q8JH85; -.
DR MEROPS; S01.334; -.
DR BRENDA; 3.4.21.74; 6665.
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_0000295003"
FT CHAIN 25..258
FT /note="Alpha-fibrinogenase"
FT /id="PRO_0000295004"
FT DOMAIN 25..249
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 98..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 142..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 174..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 200..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 258 AA; 28608 MW; 0BB7B9A912FDFD3C CRC64;
MVLIRVLANL VMLHLSYGEK SSELVIGGRP CNINQHRSLA LLYNSSGFLC GGTLINQQWV
LSAAHCDMEN MQIYLGLHNF SLPNMDQKRR VAEEKFFCLS NKSYTKWDKD IMLIKLNRRV
KTSTHIAPLS LPSNPPRLRS VCRIMGWGSI TSPRETLPYV PHCANIMILR YWVCRAIYGS
LPAKSRTLCA GVPRRRIGSC LGDSGGPLIC NGQIQGIASW GSDPCVNHGA PGVYTKVFDY
NDWIQSIIAG NTAATCPP
