Protein: Zinc metalloproteinase-disintegrin-like protein F1 (A0A0B4U9L8)
Organism: Vipera ammodytes ammodytes (Western sand viper)
Function: Zinc metalloprotease that has fibrinogenolytic activity. Does not have hemorrhagic activity in rats. Cleaves insulin B chain at '38- Ala-|-Leu-39' and '40-Tyr-|-Leu-41' bonds. Hydrolyzes only partially and weakly isolated extracellular matrix (ECM) bovine fibronectin and basal membrane (BM) protein human collagen IV in vitro. Murine laminin is not hydrolyzed, neither isolated nor in a solubilized BM preparation. Nidogen is hydrolyzed at '350-Ser-|-Phe-351' bond in a solubilized BM preparation. Hydrolyzes plasma proteins involved in blood coagulation in vitro. Has alpha-fibrinogenase activity cleaving human fibrinogen alpha chain at '432-Lys-|-Leu-433' bond, but does not cleave beta or gamma chains. Does not cleave fibrin. Hydrolyzes only partially bovine prothrombin at '200-Ser-|-Gly-201' bond, factor X (FX) heavy chain, and very slowly, FX light chain and plasminogen in vitro, without activating any of them. Has no effect in plasma thrombin generation. Does not inhibit platelet aggregation induced by collagen in vitro. May have a delayed pathological action as an anticoagulant in envenomed patients after they received serotherapy as it is not recognized by the venom antiserum
Subcellular location: Secreted
Sequence: MLQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPQKLTALLKGAIQQPEQKYEDAMQYEFKVNGKPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGHIQNDAHLTASISACNGLKGHFQLRGETYLIEPLKIPDSEAHAVYKYENVEKEDEGPKKCGVTQTNWKSDEPIKASQFILTPEQRAYMNANKYIKLAIVVDNVMFRKYTGNFTAIRTRIYEIVNTLNLIYTILNIHIALVFLEIWSKGDSINVQSVVDVTLNSFGEWRERDLLNRKRHDNAQLLTGINFNGDTIGFGFVGSMCIPKKSVGIVQDHSKTHLLVATTMAHELGHNLGINHDGDSCTCQANSCIMAAKLSHQPSYQFSDCSINELWMYLISHTPRCILNEPLTTDVVSPAVCGNYVVEEGEECDCGSLWYCRNPCCDAATCKLKPGAECGDGVCCYQCRFVTAGTVCRPARSECDIPEYCSGQSVECPMDHIQKNGKPCLMNHGYCYNGRCPIMIHQCIALWGPGTTVSSDVCFQRNESGQGYSYCRRENNQNIPCAPQDVKCGRLYCKFHNVNTLPCNFKYSDFAPDYGLVDHGTKCGDGKVCNSNRQCVDVNTAY
InterPro domains: - IPR024079: Metallopeptidase, catalytic domain superfamily (homologous_superfamily) [189-397]
- IPR001762: Disintegrin domain (domain) [406-492]
- IPR034027: Reprolysin domain, adamalysin-type (domain) [202-396]
- IPR001590: Peptidase M12B, ADAM/reprolysin (domain) [202-398]
- IPR018358: Disintegrin, conserved site (conserved_site) [446-465]
- IPR002870: Peptidase M12B, propeptide (domain) [32-113]
- IPR006586: ADAM, cysteine-rich domain (domain) [491-610]
- IPR036436: Disintegrin domain superfamily (homologous_superfamily) [405-488]
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0003824 (catalytic activity), GO:0043167 (ion binding), GO:0140096 (catalytic activity, acting on a protein), GO:0016787 (hydrolase activity), GO:0043169 (cation binding), GO:0008233 (peptidase activity), GO:0046872 (metal ion binding), GO:0008237 (metallopeptidase activity), GO:0046914 (transition metal ion binding), GO:0008270 (zinc ion binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0071704 (organic substance metabolic process), GO:0043170 (macromolecule metabolic process), GO:1901564 (organonitrogen compound metabolic process), GO:0019538 (protein metabolic process), GO:0006508 (proteolysis)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005576 (extracellular region)