VM1AC_CROAT
ID VM1AC_CROAT Reviewed; 414 AA.
AC Q90392;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Snake venom metalloproteinase atrolysin-C;
DE Short=SVMP;
DE EC=3.4.24.42;
DE AltName: Full=Hemorrhagic metalloproteinase atrolysin C;
DE AltName: Full=Hemorrhagic toxin C;
DE Short=HT-C;
DE Flags: Precursor;
OS Crotalus atrox (Western diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8730;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8311451; DOI=10.1006/abbi.1994.1026;
RA Hite L.A., Jia L.-G., Bjarnason J.B., Fox J.W.;
RT "cDNA sequences for four snake venom metalloproteinases: structure,
RT classification, and their relationship to mammalian reproductive
RT proteins.";
RL Arch. Biochem. Biophys. 308:182-191(1994).
RN [2]
RP PROTEIN SEQUENCE OF 366-378, AND FUNCTION.
RX DOI=10.1016/0167-4838(87)90077-X;
RA Bjarnason J.B., Fox J.W.;
RT "Characterization of two hemorrhagic zinc proteinases, toxin c and toxin d,
RT from western diamondback rattlesnake (Crotalus atrox) venom.";
RL Biochim. Biophys. Acta 911:356-363(1987).
RN [3]
RP PROTEIN SEQUENCE OF 198-208; 224-236 AND 351-363, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19371136; DOI=10.1021/pr900249q;
RA Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.;
RT "Exploring the venom proteome of the western diamondback rattlesnake,
RT Crotalus atrox, via snake venomics and combinatorial peptide ligand library
RT approaches.";
RL J. Proteome Res. 8:3055-3067(2009).
RN [4]
RP FUNCTION.
RX PubMed=2817904; DOI=10.1016/0003-9861(89)90350-0;
RA Baramova E.N., Shannon J.D., Bjarnason J.B., Fox J.W.;
RT "Degradation of extracellular matrix proteins by hemorrhagic
RT metalloproteinases.";
RL Arch. Biochem. Biophys. 275:63-71(1989).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that causes hemorrhage by
CC provoking the degradation of the sub-endothelial matrix proteins
CC (fibronectin, laminin, type IV collagen, nidogen, and gelatins).
CC {ECO:0000269|PubMed:2817904, ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15,
CC 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 of insulin B chain. With small
CC molecule substrates prefers hydrophobic residue at P2' and small
CC residue such as Ala, Gly at P1.; EC=3.4.24.42;
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 -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR EMBL; U01236; AAA03328.1; -; mRNA.
DR PIR; S41609; S41609.
DR AlphaFoldDB; Q90392; -.
DR SMR; Q90392; -.
DR MEROPS; M12.144; -.
DR BRENDA; 3.4.24.42; 1710.
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:0030574; P:collagen catabolic process; 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; 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 1: Evidence at protein level;
KW Calcium; Collagen degradation; Direct protein sequencing; Disulfide bond;
KW Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Pyrrolidone carboxylic acid; Secreted; Signal;
KW Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..190
FT /evidence="ECO:0000250"
FT /id="PRO_0000322609"
FT CHAIN 191..393
FT /note="Snake venom metalloproteinase atrolysin-C"
FT /id="PRO_0000322610"
FT PROPEP 394..414
FT /evidence="ECO:0000250"
FT /id="PRO_0000322611"
FT DOMAIN 197..393
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
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 BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 191
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 308..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 348..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 414 AA; 46769 MW; 3C5EBDDE61888C71 CRC64;
MIEVVLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYELK
VNGEPVVLHL EKNKELFSKD YSETHYSPDG RKITTNPSVE DHCYYRGRIE NDADSTASIS
ACNGLKGHFK LQGELYLIEP LELSDSEAHA VFKLENVEKE DEAPKMCGVT QNWESYEPIK
KASDLNLNPD QQNLPQRYIE LVVVADHRVF MKYNSDLNTI RTRVHEIVNF INGFYRSLNI
HVSLTDLEIW SNEDQINIQS ASSDTLNAFA EWRETDLLNR KSHDNAQLLT AIELDEETLG
LAPLGTMCDP KLSIGIVQDH SPINLLMGVT MAHELGHNLG MEHDGKDCLR GASLCIMRPG
LTKGRSYEFS ADSMHYYERF LKQYKPQCIL NKPLRIDPVS TPVSGNELLE AGEE
