ID   VM1AC_DEIAC             Reviewed;         417 AA.
AC   Q9PW36;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Snake venom metalloproteinase acutolysin-C;
DE            Short=SVMP;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=12075438;
RA   Liu Q.-D., Xu W.-H., Cheng X., Liu J.;
RT   "Molecular cloning and sequence analysis of cDNA encoding acutolysin C, a
RT   hemorrhagic metalloproteinase, from Agkistrodon acutus.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 32:425-429(2000).
CC   -!- FUNCTION: This protein is an alkaline zinc metalloprotease from snake
CC       venom that possesses weak hemorrhagic activity. {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: Two proteins (AC P60244 and AC Q9PW36) have been independently
CC       named acutolysin-C. {ECO:0000305}.
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DR   EMBL; AF174391; AAD51823.1; -; mRNA.
DR   AlphaFoldDB; Q9PW36; -.
DR   SMR; Q9PW36; -.
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                   /note="Activation peptide"
FT                   /id="PRO_0000028953"
FT   CHAIN           190..392
FT                   /note="Snake venom metalloproteinase acutolysin-C"
FT                   /id="PRO_0000028954"
FT   PROPEP          393..417
FT                   /id="PRO_0000028955"
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:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-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:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        349..371
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        351..354
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   417 AA;  47149 MW;  C3DA126D6C85058C CRC64;
     MIQVLLVTIC LAALPYQGSS IMLESGKVND YEVVYPQRLA PLPEGAVQQK YEDTMQYEFK
     VNGETIVLHL EKNKGLFSKD YSETHYSPDG RKITTYPSVE DHCYYHGRIE NYEDSTASIS
     ACNGLKGHFK IQGETYFIES LKLSDSEAHA VLKYENVGKE DETHQICGVT LNWKSYDPIK
     RPSRLNLTPK QQTWPQTSVN LQLIVDHSMY AKYNSNSEKI TKTVQERVNI MKEIFKPLNF
     DITLSGIEMW DKKDLITVKT AATDTLKLFA KWRQTDLLKR IDNDNAQLQT AVDFDGETVG
     LAFKSTMCDK RYSAGIIQDH SAIPLLMAVT IAHELGHNLG MDHDDTSKCN CNVCIMAPRL
     NTNPSKTFSD CSNNDYQKFL TDKKPKCIHK KSLKTDTVST SVSGNEPLDD NVDGFHA