ID VM1A3_DEIAC Reviewed; 197 AA.
AC P60244;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 22-FEB-2023, entry version 82.
DE RecName: Full=Snake venom metalloproteinase acutolysin-C;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Hemorrhagin III;
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 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-197 IN COMPLEX WITH ZINC ION,
RP AND DISULFIDE BONDS.
RX PubMed=10531480; DOI=10.1107/s0907444999010306;
RA Zhu X.-Y., Teng M.-K., Niu L.-W.;
RT "Structure of acutolysin-C, a haemorrhagic toxin from the venom of
RT Agkistrodon acutus, providing further evidence for the mechanism of the pH-
RT dependent proteolytic reaction of zinc metalloproteinases.";
RL Acta Crystallogr. D 55:1834-1841(1999).
CC -!- FUNCTION: This protein is an alkaline zinc metalloprotease from snake
CC venom that possesses weak hemorrhagic activity.
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:0000269|PubMed:10531480}.
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: Two proteins (AC P60244 and AC Q9PW36) have been independently
CC named acutolysin-C. {ECO:0000305}.
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DR PDB; 1QUA; X-ray; 2.20 A; A=1-197.
DR PDBsum; 1QUA; -.
DR AlphaFoldDB; P60244; -.
DR SMR; P60244; -.
DR MEROPS; M12.303; -.
DR EvolutionaryTrace; P60244; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF32; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 28; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Hemorrhagic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..197
FT /note="Snake venom metalloproteinase acutolysin-C"
FT /id="PRO_0000078188"
FT DOMAIN 5..197
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 142
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000269|PubMed:10531480"
FT DISULFID 156..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000269|PubMed:10531480"
FT DISULFID 158..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000269|PubMed:10531480"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:1QUA"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:1QUA"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1QUA"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:1QUA"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1QUA"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:1QUA"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1QUA"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1QUA"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:1QUA"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1QUA"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1QUA"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1QUA"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:1QUA"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:1QUA"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1QUA"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1QUA"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:1QUA"
SQ SEQUENCE 197 AA; 21437 MW; 22C5BE258AE8CD60 CRC64;
PAPQTSIELF LIVDHSMYAK YNSNSSKITT TLKARVNIMN AIYSSLNLVI TLSGIEMWSA
ADLITVQSSS RNTLKLFASW RETDLLKRTS NDNAQLLTAT NFNGNTVGLA YLKTMCNSKY
SVGLIQDHSA IPLLMAVTMA HELGHNLGMN HDGAGCSCAT CIMAPVLSSG PAKSFSDCSK
HDYQSFLTIH KPQCLLN
//
