VM1A_DEIAC
ID VM1A_DEIAC Reviewed; 202 AA.
AC Q7LZS9;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Snake venom metalloproteinase Ac1;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Ac1-proteinase;
OS Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX NCBI_TaxID=36307;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=7655443; DOI=10.1248/bpb.18.631;
RA Nikai T., Kato C., Komori Y., Nodani H., Homma M., Sugihara H.;
RT "Primary structure of Ac1-proteinase from the venom of Deinagkistrodon
RT acutus (hundred-pace snake) from Taiwan.";
RL Biol. Pharm. Bull. 18:631-633(1995).
CC -!- FUNCTION: Snake venom metalloproteinase that impairs hemostasis in the
CC envenomed animal. {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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks a Cys at position 158 preventing the formation of a
CC third disulfide bond. {ECO:0000305}.
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DR PIR; JC2550; JC2550.
DR AlphaFoldDB; Q7LZS9; -.
DR SMR; Q7LZS9; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..202
FT /note="Snake venom metalloproteinase Ac1"
FT /id="PRO_0000415607"
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 DISULFID 117..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 157..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 202 AA; 22945 MW; 7C7AD02D009DFE00 CRC64;
STEFQRYMEI VIVVDHSMVK KYNGDSPKIK AWVYEMINTI TEGYRDLYID IILSGLEIWS
EKDLINVEAS AGNTLKSFGE WRAKDLIHRI SHDNAQLLTA TDFDGPTIGL AYVASMCEPK
LSVGVIQDHS SVNRLVAITL AHEMAHNLGV RHDEKDCVGV VYLCIMRIPV VEDKRSYFSD
CSYIQCREYI SKENPPCILN KP
