VM3DM_DABSI
ID VM3DM_DABSI Reviewed; 25 AA.
AC P0DJH5;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like daborhagin-M;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Fragment;
OS Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=343250;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND MASS
RP SPECTROMETRY.
RC STRAIN=Myanmar; TISSUE=Venom;
RX PubMed=18554518; DOI=10.1016/j.biochi.2008.05.012;
RA Chen H.-S., Tsai H.-Y., Wang Y.-M., Tsai I.-H.;
RT "P-III hemorrhagic metalloproteinases from Russell's viper venom: cloning,
RT characterization, phylogenetic and functional site analyses.";
RL Biochimie 90:1486-1498(2008).
CC -!- FUNCTION: Snake venom zinc metalloprotease that possesses high
CC hemorrhagic activity (minimum hemorrhagic dose, MHD=0.86 ug) when
CC subcutaneously injected into mice. Has potent fibrinogenolytic activity
CC on alpha-chain of fibrinogen (FGA). Hydrolyzes model substrate (beta-
CC chain of insulin) at Ala(14)-Leu(15) and Tyr(16)-Leu(17) followed by
CC His(10)-Leu(11) and Phe(24)-Phe(25). {ECO:0000269|PubMed:18554518}.
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: Inhibited by EDTA, EGTA and 1,10-phenanthroline.
CC Addition of Mg(2+) or Ca(2+) increases the casein hydrolysis rate.
CC {ECO:0000269|PubMed:18554518}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.0 uM for NFF-2 (fluorogenic substrates with cleavage at Ala-
CC Nva);
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18554518}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated.
CC -!- PTM: Contains 16 disulfide bonds. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=65065; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18554518};
CC -!- MISCELLANEOUS: Does not degrade beta- and gamma-chains of fibrinogen.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DJH5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Glycoprotein; Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Secreted; Toxin; Zinc; Zymogen.
FT CHAIN 1..>25
FT /note="Zinc metalloproteinase-disintegrin-like daborhagin-
FT M"
FT /id="PRO_0000417328"
FT DOMAIN 14..>25
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 17
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT NON_TER 25
SQ SEQUENCE 25 AA; 2915 MW; 6CF54DDEFB9BC616 CRC64;
VATSEPNRYF NPYSYVELII TVDHS
