VM1AT_CROAT
ID VM1AT_CROAT Reviewed; 203 AA.
AC Q91401;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Snake venom metalloproteinase atroxase;
DE Short=SVMP;
DE EC=3.4.24.43;
DE AltName: Full=Nonhemorrhagic metalloprotease atroxase;
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] OF 1-199, PROTEIN SEQUENCE OF 1-28; 64-70 AND
RP 186-203, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=7893150; DOI=10.1006/abbi.1995.1175;
RA Baker B.J., Wongvibulsin S., Nyborg J., Tu A.T.;
RT "Nucleotide sequence encoding the snake venom fibrinolytic enzyme atroxase
RT obtained from a Crotalus atrox venom gland cDNA library.";
RL Arch. Biochem. Biophys. 317:357-364(1995).
RN [2]
RP PROTEIN SEQUENCE OF 10-20; 25-33; 36-48; 76-85; 94-109; 114-123 AND
RP 163-177, AND IDENTIFICATION BY 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 [3]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=3167016; DOI=10.1021/bi00413a028;
RA Willis T.W., Tu A.T.;
RT "Purification and biochemical characterization of atroxase, a
RT nonhemorrhagic fibrinolytic protease from western diamondback rattlesnake
RT venom.";
RL Biochemistry 27:4769-4777(1988).
RN [4]
RP FUNCTION.
RX PubMed=2646751; DOI=10.1016/0049-3848(89)90112-6;
RA Willis T.W., Tu A.T., Miller C.W.;
RT "Thrombolysis with a snake venom protease in a rat model of venous
RT thrombosis.";
RL Thromb. Res. 53:19-29(1989).
CC -!- FUNCTION: Snake venom zinc metalloprotease that has Aalpha, Bbeta
CC fibrin(ogen)olytic activities. It cleaves the Aalpha chain of
CC fibrinogen first followed by the Bbeta chain and shows no effect on the
CC gamma chain. Does not induce or inhibit platelet aggregation, and is
CC unable to activate plasminogen. Exhibits low lethality when tested on
CC mice. Intravenous administration results in thrombolysis within one
CC hour followed by recanalization. Fibrinogenolytic activity results in a
CC 60% decrease in the rat's plasma fibrinogen level. Histological
CC examination of kidney, liver, heart and lung tissue shows no necrosis
CC nor hemorrhage. {ECO:0000269|PubMed:2646751,
CC ECO:0000269|PubMed:3167016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of 5-His-|-Leu-6, 9-Ser-|-His-10, 10-His-|-Leu-11,
CC 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in insulin B chain.;
CC EC=3.4.24.43;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and alpha2-macroglobulin.
CC {ECO:0000269|PubMed:3167016}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:3167016};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:3167016};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3167016}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7893150}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7893150}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR EMBL; S77086; AAB33788.2; -; mRNA.
DR PIR; I51280; I51280.
DR MEROPS; M12.147; -.
DR KEGG; ag:AAB33788; -.
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: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 Calcium; Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Fibrinolytic toxin; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Potassium; Protease;
KW Pyrrolidone carboxylic acid; Secreted; Toxin; Zinc.
FT CHAIN 1..203
FT /note="Snake venom metalloproteinase atroxase"
FT /id="PRO_0000322604"
FT DOMAIN 9..203
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid (Glu)"
FT /evidence="ECO:0000250"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CONFLICT 3
FT /note="Q -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 7..9
FT /note="SQR -> PPQK (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="V -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="G -> H (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..191
FT /note="QS -> ER (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="Q -> C (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 23204 MW; 7720847D90D7A4E1 CRC64;
EDQQNLSQRY IELVVVADHR VFMKYNSDLN IIRKRVHELV NTINGFYRSL NIDVSLTDLE
IWSDQDFITV DSSAKNTLNS FGEWREADLL RRKSHDHAQL LTAINFEGKI IGRAYTSSMC
NPRKSVGIXK DHSPINLLVG VTMAHELGHN LGMNHDGEKC LRGASLCIMR PGLTPGRSYE
FSDDSMGYYQ SFLKQYNPQI XNK
