VM1V1_AGKPL
ID VM1V1_AGKPL Reviewed; 411 AA.
AC B7U492;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Snake venom metalloproteinase VMP1;
DE Short=AplVMP-I;
DE Short=AplVMP1;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Flags: Precursor;
OS Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias
OS leucostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=459671;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Venom gland;
RX PubMed=19375443; DOI=10.1016/j.toxicon.2009.04.008;
RA Jia Y., Lucena S., Cantu E. Jr., Sanchez E.E., Perez J.C.;
RT "cDNA cloning, expression and fibrin(ogen)olytic activity of two low-
RT molecular weight snake venom metalloproteinases.";
RL Toxicon 54:233-243(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=19799929; DOI=10.1016/j.toxicon.2009.09.016;
RA Jia Y., Perez J.C.;
RT "Molecular cloning and characterization of cDNAs encoding
RT metalloproteinases from snake venom glands.";
RL Toxicon 55:462-469(2010).
CC -!- FUNCTION: This venom zinc protease has fibrinolytic activity. The
CC recombinant enzyme cleaves both alpha- (FGA) and beta-chains (FGB) of
CC fibrinogen, but not the gamma-chain. The recombinant protein does not
CC produce hemorrhage in mice and does not have effect on ADP- or
CC collagen-stimulated platelet aggregation.
CC {ECO:0000269|PubMed:19375443}.
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 1,10-phenanthroline, but not
CC by PMSF. {ECO:0000269|PubMed:19375443}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
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; FJ429179; ACJ61244.1; -; mRNA.
DR AlphaFoldDB; B7U492; -.
DR SMR; B7U492; -.
DR MEROPS; M12.133; -.
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; 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 Calcium; Disulfide bond; Fibrinogenolytic toxin; Fibrinolytic toxin;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..189
FT /evidence="ECO:0000250"
FT /id="PRO_0000407746"
FT CHAIN 190..411
FT /note="Snake venom metalloproteinase VMP1"
FT /id="PRO_0000407747"
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 CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 308..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 348..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 350..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 411 AA; 46583 MW; E36379A19A023086 CRC64;
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEIVYPRKVT PVPRGAVQPK YEDAMQYELK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPLVE DHCYYHGRIE NDADSTASIS
TCNGLKGHFK LQGEMYLIEP LELSDSEAHA VYKYENVEKE DEAPKMCGVT QNWESYEPTK
KAFQLNLTPE QQGFPQRYVE LVIIADHRMY MKYKRDSNKI TQWVHQMVNT INEIYRPLNI
QFALVGLEIW SNQDLITVTS VSDDTLISFA NWRETVLLRR KSHDNAQLLT AIVFDEGIIG
RAPLAGMCDP NRSVGTVQDH SKINFRVAII MAHEIGHNLG MGHDDNSCTC GGYSCIMLPR
LSKQPSKLFS DCSKKDYLTF LKVKNPQCIL NKPLRTDTVS TPVSGNELLE A
