VM3_VIPAA
ID VM3_VIPAA Reviewed; 36 AA.
AC P0DJ44;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like VaH1;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloprotease;
DE Short=SVMP;
DE Flags: Fragments;
OS Vipera ammodytes ammodytes (Western sand viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=8705;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND BLOCKAGE OF N-TERMINUS.
RC TISSUE=Venom;
RX PubMed=11602279; DOI=10.1016/s0041-0101(01)00188-x;
RA Leonardi A., Gubensek F., Krizaj I.;
RT "Purification and characterisation of two hemorrhagic metalloproteinases
RT from the venom of the long-nosed viper, Vipera ammodytes ammodytes.";
RL Toxicon 40:55-62(2002).
CC -!- FUNCTION: Snake venom zinc metalloprotease that exhibits strong
CC hemorrhagic activity. It also degrades alpha-chain of fibrinogen (FGA),
CC but not the beta- and the gamma-chains. Possesses potent
CC azocaseinolytic activity and cleaves insulin B-chain, hydrolyzing it at
CC positions Ala(14)-Leu(15), followed by Tyr(16)-Leu(17) and His(10)-
CC Leu(11). In vivo, subcutaneous injection into mice induces strong
CC hemorrhage. {ECO:0000269|PubMed:11602279}.
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, but not inhibited by
CC iodoacetamide, PMSF and pepstatin A. {ECO:0000269|PubMed:11602279}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:11602279};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11602279}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR BRENDA; 3.4.24.B36; 10997.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0043655; C:host extracellular space; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044485; P:envenomation resulting in fibrinogenolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044358; P:envenomation resulting in hemorrhagic damage in another organism; IDA:UniProtKB.
DR GO; GO:0044481; P:envenomation resulting in proteolysis in another organism; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Glycoprotein; Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT CHAIN <1..>36
FT /note="Zinc metalloproteinase-disintegrin-like VaH1"
FT /id="PRO_0000418197"
FT DOMAIN <1..>36
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 25..?
FT NON_CONS 9..10
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 36
SQ SEQUENCE 36 AA; 4197 MW; B96368629ACCD153 CRC64;
MVTKYSSIFM SPILSNPPIL YFSDCSREXY QKXLTN
