ID VM2MC_GLOBR Reviewed; 476 AA.
AC Q9YI19;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 22-FEB-2023, entry version 103.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase brevilysin L6;
DE Short=SVMP;
DE AltName: Full=Snake venom metalloproteinase Mt-c;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin;
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 185-387, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND PYROGLUTAMATE FORMATION AT GLN-185.
RC TISSUE=Venom;
RX PubMed=9880798; DOI=10.1093/oxfordjournals.jbchem.a022269;
RA Terada S., Hori J., Fujimura S., Kimoto E.;
RT "Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic
RT metalloprotease from Agkistrodon halys brevicaudus venom.";
RL J. Biochem. 125:64-69(1999).
CC -!- FUNCTION: [Snake venom metalloproteinase brevilysin L6]: Shows weak
CC degradation of alpha-fibrinogen, but has no activity on beta- and
CC gamma-chains. Digests luteinizing hormone-releasing hormone (LH-RH) and
CC oxidized insulin at X-Leu, X-Phe, and X-Val bonds as well as X-His
CC bond. Does not show fibrinogen-clotting activity. Does not show
CC hemorrhagic activity. {ECO:0000269|PubMed:9880798}.
CC -!- FUNCTION: [Disintegrin]: Inhibits ADP-induced platelet aggregation.
CC {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 -!- ACTIVITY REGULATION: The metalloproteinase is inhibited by EDTA, o-
CC phenanthroline, and cysteine. Glutathione does not inhibit the
CC enzymatic activity. {ECO:0000269|PubMed:9880798}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is about 9. {ECO:0000269|PubMed:9880798};
CC -!- SUBUNIT: Homodimer; disulfide-linked (disintegrin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IId sub-subfamily. {ECO:0000305}.
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DR EMBL; AF051790; AAD02655.1; -; mRNA.
DR PIR; A59421; A59421.
DR AlphaFoldDB; Q9YI19; -.
DR SMR; Q9YI19; -.
DR MEROPS; M12.178; -.
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; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
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 PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF32; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 28; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Pyrrolidone carboxylic acid; Secreted; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..184
FT /evidence="ECO:0000269|PubMed:9880798"
FT /id="PRO_0000424453"
FT CHAIN 185..387
FT /note="Snake venom metalloproteinase brevilysin L6"
FT /id="PRO_0000424454"
FT PROPEP 388..403
FT /evidence="ECO:0000250"
FT /id="PRO_0000424455"
FT CHAIN 404..476
FT /note="Disintegrin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000424456"
FT DOMAIN 191..387
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 395..476
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 454..456
FT /note="Cell attachment site"
FT ACT_SITE 328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 185
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:9880798"
FT DISULFID 302..382
FT /evidence="ECO:0000250"
FT DISULFID 342..366
FT /evidence="ECO:0000250"
FT DISULFID 344..349
FT /evidence="ECO:0000250"
FT DISULFID 418..441
FT /evidence="ECO:0000250"
FT DISULFID 432..438
FT /evidence="ECO:0000250"
FT DISULFID 437..462
FT /evidence="ECO:0000250"
FT DISULFID 450..469
FT /evidence="ECO:0000250"
FT CONFLICT 231
FT /note="S -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="N -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="E -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..295
FT /note="IGL -> LGI (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="T -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 52802 MW; F06B2E643D15605F CRC64;
MIQVLLVIIC LADFPYQGTS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSKG YSETHYSPDG RKITTNPPVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK HQGEMYLIEP LKLSDSEAHA VYKYENVEKE DEAPKMCGVT QTNWKSDEPI
KASQQQRFPQ RYIELVVVAD HGMFTKYDSN LDTIRTWVHE LVNSINEFYR SLNIDVSLTE
LEIWSNQDLI NVQSAAGDTL EAFGDWRETD LLNRISHDNA QLLTATELDG NTIGLAHVAS
MCDPKRSTGV VQDHSAINLL VAVTMAHETG HNLGMNHDGN QCHCGANSCV MGDVLSEGVS
YEFSDCSENE YQTYLTDRNP QCILNEPLRT DTVSTPVSGN ELLEAGKECD CGAPANPCCD
AETCKLRPGQ QCAEGLCCDQ CRFMKEGTIC QEAKGDWNDD TCNGISAGCP RNGFYG
//
