VM1F_MACLB
ID VM1F_MACLB Reviewed; 202 AA.
AC P83255;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Snake venom metalloproteinase fibrolase;
DE Short=SVMP;
DE EC=3.4.24.72;
DE AltName: Full=Fibrinolytic proteinase;
DE AltName: Full=Non-hemorrhagic fibrinolytic metalloproteinase;
DE AltName: Full=VlF;
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 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=10962108; DOI=10.1016/s0167-4838(00)00128-x;
RA Gasmi A., Srairi N., Karoui H., El Ayeb M.;
RT "Amino acid sequence of VlF: identification in the C-terminal domain of
RT residues common to non-hemorrhagic metalloproteinases from snake venoms.";
RL Biochim. Biophys. Acta 1481:209-212(2000).
RN [2] {ECO:0000305}
RP FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Venom;
RX PubMed=1926182; DOI=10.1016/0041-0101(91)90219-h;
RA Gasmi A., Karoui M., Benlasfar Z., Karoui H., El Ayeb M., Dellagi K.;
RT "Purification and characterization of a fibrinogenase from Vipera lebetina
RT (desert adder) venom.";
RL Toxicon 29:827-836(1991).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=9175244; DOI=10.1016/s0049-3848(97)00066-2;
RA Gasmi A., Chabchoub A., Guermazi S., Karoui H., El Ayeb M., Dellagi K.;
RT "Further characterization and thrombolytic activity in a rat model of a
RT fibrinogenase from Vipera lebetina venom.";
RL Thromb. Res. 86:233-242(1997).
CC -!- FUNCTION: Has fibrino(geno)lytic activity on the alpha and beta chains
CC of fibrinogen (FGA and FGB). Inhibits human ADP- and collagen-induced
CC platelet aggregation on platelet-rich plasma but does not affect the
CC thrombin-induced aggregation of rabbit washed platelets. Slightly
CC degrades plasminogen. {ECO:0000269|PubMed:1926182,
CC ECO:0000269|PubMed:9175244}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of 14-Ala-|-Leu-15 in insulin B chain and 413-
CC Lys-|-Leu-414 in alpha-chain of fibrinogen.; EC=3.4.24.72;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by calcium and magnesium ions. Inhibited
CC by EDTA, DTT and L-cysteine. Activity is not affected by PMSF or
CC heparin. {ECO:0000269|PubMed:1926182}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:1926182}.
CC -!- MASS SPECTROMETRY: Mass=22830; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10962108};
CC -!- MISCELLANEOUS: Has no hemorrhagic activity. Has no activity toward
CC factor X (F10), prothrombin (F2) and protein C (PROC).
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P83255; -.
DR SMR; P83255; -.
DR MEROPS; M12.164; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; TAS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0030193; P:regulation of blood coagulation; TAS:UniProtKB.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF01421; Reprolysin; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Fibrinolytic toxin; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Magnesium; Metal-binding; Metalloprotease; Plasminogen activation;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..202
FT /note="Snake venom metalloproteinase fibrolase"
FT /id="PRO_0000078198"
FT DOMAIN 6..202
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 9
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 157..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 159..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 202 AA; 22851 MW; 8EAAD4EFC6D7BE75 CRC64;
ERFAPRYIEL VIVADHSVAT KYNDNVTAIL SWVHQLVNNI ILFYRDLNVH FTLSAVEVWS
NGDLINVQPE ATVTLNLFGE WRERDLLNRR MHDNAQLLNN VALDDNTIGL AYDEGMCDPK
YSVGIVKDHS AINRMVAATM AHEIGHNLGM NHDGSQCNCG GNGCVMSAVL MQQHSYQFSD
CSKDEYQRYL TNHNPQCILN QP
