VM3H6_GLOBR
ID VM3H6_GLOBR Reviewed; 610 AA.
AC P0C7B0; Q9YI20;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like brevilysin H6;
DE Short=Mt-a;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Contains:
DE RecName: Full=p45K;
DE Contains:
DE RecName: Full=Disintegrin-like p29K;
DE Flags: Precursor;
OS Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys
OS brevicaudus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=259325;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Jeon O.-H., Kim D.-S.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 192-610, FUNCTION, AUTOPROTEOLYSIS, ACTIVITY
RP REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP PYROGLUTAMATE FORMATION AT GLN-192, GLYCOSYLATION AT ASN-372, AND DISULFIDE
RP BONDS.
RC TISSUE=Venom;
RX PubMed=10920250; DOI=10.1093/oxfordjournals.jbchem.a022737;
RA Fujimura S., Oshikawa K., Terada S., Kimoto E.;
RT "Primary structure and autoproteolysis of brevilysin H6 from the venom of
RT Gloydius halys brevicaudus.";
RL J. Biochem. 128:167-173(2000).
CC -!- FUNCTION: Shows weak hemorrhagic activity. Rapidly degrades the alpha-
CC chain of fibrinogen (FGA). {ECO:0000269|PubMed:10920250}.
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 chelating agents. Calcium ions
CC enhance its activity, they also suppress autoproteolysis, and
CC contribute to the stability of the enzyme against pH, heating, urea and
CC cysteine. {ECO:0000269|PubMed:10920250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.8 in the absence of calcium ions. Optimum pH is 5.6-
CC 8.5 in the presence of calcium ions.;
CC Temperature dependence:
CC The activity is markedly reduced above 40 degrees Celsius. Calcium
CC ions increases the thermal stability by 10 degrees Celsius.;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10920250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:10920250}.
CC -!- PTM: In the absence of calcium ions, is autocatalytically degraded
CC giving 29 (p29K) and 45 kDa (p45K) fragments. In presence of calcium
CC ions, the p45K is not detected (PubMed:10920250).
CC {ECO:0000269|PubMed:10920250}.
CC -!- MISCELLANEOUS: The metalloproteinase domain which is released from the
CC cleavage of the disintegrin bothropasin may be unstable.
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIb sub-subfamily. {ECO:0000305}.
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DR EMBL; AF051787; AAD02652.1; -; mRNA.
DR PIR; A59414; A59414.
DR AlphaFoldDB; P0C7B0; -.
DR SMR; P0C7B0; -.
DR MEROPS; M12.022; -.
DR iPTMnet; P0C7B0; -.
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 Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
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; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Fibrinogenolytic toxin; Glycoprotein; Hemorrhagic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Zinc;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000269|PubMed:10920250"
FT /id="PRO_0000340280"
FT CHAIN 192..610
FT /note="Zinc metalloproteinase-disintegrin-like brevilysin
FT H6"
FT /id="PRO_0000330002"
FT CHAIN 290..610
FT /note="p45K"
FT /id="PRO_0000330003"
FT CHAIN 399..610
FT /note="Disintegrin-like p29K"
FT /id="PRO_0000330004"
FT DOMAIN 198..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 402..488
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 466..468
FT /note="D/ECD-tripeptide"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT MOD_RES 192
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:10920250"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10920250"
FT DISULFID 309..389
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6"
FT /evidence="ECO:0000269|PubMed:10920250"
FT DISULFID 349..373
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6"
FT /evidence="ECO:0000250"
FT DISULFID 351..356
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6"
FT /evidence="ECO:0000250"
FT DISULFID 373..378
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000269|PubMed:10920250"
FT DISULFID 405..434
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 405..424
FT /note="In disintegrin-like p29K; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 416..434
FT /note="In disintegrin-like p29K; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 416..429
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 418..424
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 428..451
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6"
FT /evidence="ECO:0000250"
FT DISULFID 442..448
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6"
FT /evidence="ECO:0000250"
FT DISULFID 447..473
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6"
FT /evidence="ECO:0000250"
FT DISULFID 460..480
FT /note="In both disintegrin-like p29K and zinc
FT metalloproteinase-disintegrin-like brevilysin H6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 467..499
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 467..492
FT /note="In disintegrin-like p29K; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 492..504
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 499..504
FT /note="In disintegrin-like p29K"
FT /evidence="ECO:0000250"
FT DISULFID 511..561
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 511..526
FT /note="In disintegrin-like p29K; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 526..572
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 539..549
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 549..556
FT /note="In disintegrin-like p29K; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 556..598
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 561..572
FT /note="In disintegrin-like p29K"
FT /evidence="ECO:0000250"
FT DISULFID 592..603
FT /note="In zinc metalloproteinase-disintegrin-like
FT brevilysin H6; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 598..603
FT /note="In disintegrin-like p29K"
FT /evidence="ECO:0000250"
FT CONFLICT 199
FT /note="F -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="H -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="H -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="S -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="H -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="E -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="K -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="K -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 610 AA; 68218 MW; DD37EA0B0D20CCDC CRC64;
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYEFK
VNGEPVVLHL GKNKQLFSKD YSETHYSPDG REITTNPPVE DHCYYHGRIE NDADSTRSIS
ACNGLKGHFK LQGETYLIEP LKLSDSEAHA VYKYENILKE DEAPKMCGVT QNWESYEPIK
KASQLNLTPE QQRYNPFRFV ELVLVADKGM VTKNNGDLNK IKTRMYELAN NLNDIYRYMY
IHVALVGVEI WSDGDKITVT PNVDDTLSSF AEWRKTHLLT RKKHDNAQLL TAIDFNGPTI
GYAYIASMCH PKRSVGIVQD YSPINLVLSV VMAHEMGHNL GIHHDHSYCS CGDYACIMGA
TISHEPSTFF SNCSYIQCWD FIMDHNPECI VNEPLGTDIV SPPVCGNELL EVGEECDCGT
PENCQNECCD AATCKLKSGS QCGHGDCCEQ CKFSKSGTEC RESMSECDPA EHCTGQSSEC
PADVFHKNGQ PCLHNYGYCY NGNCPIMYHQ CYALWGADVY EAEDSCFESN KKGNYYGYCR
KENGKKIPCA PEDVKCGRLY CKDNSPGQNN PCKMFYSNED EHKGMVLPGT KCGDGKVCSN
GHCVDVATAY
