VM1L4_MACLB
ID VM1L4_MACLB Reviewed; 217 AA.
AC Q3ZD74;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Snake venom metalloproteinase lebetase-4;
DE Short=Le-4;
DE Short=Le4;
DE EC=3.4.24.-;
DE Flags: Precursor; Fragment;
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=16098553; DOI=10.1016/j.toxicon.2005.07.001;
RA Aaspollu A., Siigur J., Siigur E.;
RT "cDNA cloning of a novel P-I lebetase isoform Le-4.";
RL Toxicon 46:591-594(2005).
CC -!- FUNCTION: Snake venom zinc metalloprotease that hydrolyzes the Aalpha-
CC chain and more slowly the Bbeta-chain of fibrin and fibrinogen. Also
CC hydrolyzes casein and B-chain of oxidized insulin. Its fibrinolytic
CC activity is direct, without any plasminogen activation. Inhibits ADP-
CC induced and collagen-induced platelet aggregation. Shows low
CC hemorrhagic activity. Cleaves the plasma proteinase inhibitors
CC alpha(2)-macroglobulin (A2M) and alpha(2)M-related pregnancy zone
CC protein (PZP), and is inhibited by them (By similarity). {ECO:0000250}.
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: Fibrinolytic and caseinolytic activities are
CC inhibited by Cd(2+), Cu(2+) and Co(2+) ions. Not inhibited by Mg(2+),
CC Ca(2+) and Ba(2+). Also inhibited by EDTA, EGTA and 1,10-phenanthroline
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR EMBL; AY987816; AAY45880.1; -; mRNA.
DR AlphaFoldDB; Q3ZD74; -.
DR SMR; Q3ZD74; -.
DR MEROPS; M12.164; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Fibrinogenolytic toxin; Fibrinolytic toxin;
KW Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Platelet aggregation inhibiting toxin; Protease;
KW Pyrrolidone carboxylic acid; Secreted; Toxin; Zinc; Zymogen.
FT PROPEP <1..14
FT /evidence="ECO:0000250"
FT /id="PRO_0000318584"
FT CHAIN 15..217
FT /note="Snake venom metalloproteinase lebetase-4"
FT /id="PRO_0000318585"
FT DOMAIN 21..217
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 132..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 172..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 174..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT NON_TER 1
SQ SEQUENCE 217 AA; 24487 MW; 77BD005989848363 CRC64;
SCRKKASQLN LTPEQQRFDP RYIELVIVAD HSMVTKYDGD LAAIRTWAHQ LVNNIIVFYR
DLNVHITLSA VEVWTNGDLI NVQPAASVTL NLFGEWRERD LLNRRMHDHA QLLTAINLDD
NTIGLAYNEG MCDPKYSVGI VQDHSAINRM VAATMAHEIG HNLGMDHDGN QCNCGANGCV
MSAVITQQRS YQFSDCSKNK YQTYLTNHNP QCILNQP
