ID   VM11_DEIAC              Reviewed;         417 AA.
AC   Q9W7S2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Snake venom metalloproteinase aculysin-1;
DE            Short=SVMP;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=wbfib {ECO:0000312|EMBL:CAB46429.1};
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] {ECO:0000312|EMBL:CAB46429.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland {ECO:0000269|Ref.1};
RA   Fan C.Y., Qian Y.C., Gong Y., Yang S.L.;
RT   "Cloning and sequence analysis the cDNA of aculysin1 from Agkistrodon
RT   acutus.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is an alkaline zinc metalloprotease from snake
CC       venom that possesses weak hemorrhagic activity.
CC       {ECO:0000250|UniProtKB:P60244}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P60244};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P60244};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P60244}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ223284; CAB46429.1; -; mRNA.
DR   AlphaFoldDB; Q9W7S2; -.
DR   SMR; Q9W7S2; -.
DR   MEROPS; M12.337; -.
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; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc;
KW   Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..189
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000235849"
FT   CHAIN           190..392
FT                   /note="Snake venom metalloproteinase aculysin-1"
FT                   /id="PRO_0000235850"
FT   PROPEP          393..417
FT                   /evidence="ECO:0000250|UniProtKB:Q9PW36"
FT                   /id="PRO_0000235851"
FT   DOMAIN          197..392
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   REGION          398..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        334
FT                   /evidence="ECO:0000250|UniProtKB:P60244,
FT                   ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-
FT                   ProRule:PRU10095"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        308..387
FT                   /evidence="ECO:0000250|UniProtKB:P60244,
FT                   ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        349..371
FT                   /evidence="ECO:0000250|UniProtKB:P60244,
FT                   ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        351..354
FT                   /evidence="ECO:0000250|UniProtKB:P60244,
FT                   ECO:0000255|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   417 AA;  47305 MW;  359950B27622BC97 CRC64;
     MIQVLLVTIC LAAFPYQGSS IMLESGKVND YEVVYPQRLA PLPEGAVQQK YEDTMQYEFK
     VNGETIVLHL EKNKGLFSKD YSETHYSPDG RKITTYPSVE DHCYYHGRIE NYEDSTASIS
     ACNGLKGHFK IQGETYFIES LKLSDSEAHA VFKYENVEKE DETHKICGVT QNWKSYDPIK
     KPSWLNLTPK QQTWPQTSVN LQLIVDHSMY AKYNSNSEKI TKTLQERVNI MKEIFKPLNL
     DITLSGIEMW DKKDLITVKT AATDTLKLFA KWRQTDLLKR IDNDNAQLQT AVDFDGETVG
     LAFKSTMCDK RYSAGIIQDH SAIPLLMAVT MAHELGHNLG MDHDDTSKCN CNVCIMAPRL
     NTNPSKTFSD CSNNDYQKFL TDKKPKCIHK KSLKTDTVST SVSGNEPLDD NVDGFHA