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VM1A3_DEIAC
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   03-AUG-2022, entry version 81.
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; -; 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   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
 
 
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