VM3_BUNFA
ID VM3_BUNFA Reviewed; 605 AA.
AC A8QL48;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like BfMP;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor; Fragment;
OS Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=8613;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=17337026; DOI=10.1016/j.toxicon.2007.01.003;
RA Guo X.-X., Zeng L., Lee W.-H., Zhang Y., Jin Y.;
RT "Isolation and cloning of a metalloproteinase from king cobra snake
RT venom.";
RL Toxicon 49:954-965(2007).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that inhibits platelet
CC aggregation and degrades fibrinogen. {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 -!- 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-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; EF080829; ABN72536.1; -; mRNA.
DR AlphaFoldDB; A8QL48; -.
DR SMR; A8QL48; -.
DR MEROPS; M12.159; -.
DR PRIDE; A8QL48; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043655; C:host extracellular space; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044485; P:envenomation resulting in fibrinogenolysis in another organism; ISS:UniProtKB.
DR GO; GO:0044358; P:envenomation resulting in hemorrhagic damage in another organism; ISS:UniProtKB.
DR GO; GO:0044477; P:envenomation resulting in negative regulation of platelet aggregation in another organism; ISS:UniProtKB.
DR GO; GO:0044481; P:envenomation resulting in proteolysis in another organism; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell adhesion impairing toxin; Disulfide bond; Fibrinogenolytic toxin;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Platelet aggregation inhibiting toxin; Protease; Secreted;
KW Signal; Toxin; Zinc; Zymogen.
FT SIGNAL <1..11
FT /evidence="ECO:0000255"
FT PROPEP 12..179
FT /evidence="ECO:0000250"
FT /id="PRO_0000417639"
FT CHAIN 180..605
FT /note="Zinc metalloproteinase-disintegrin-like BfMP"
FT /id="PRO_0000417640"
FT DOMAIN 196..392
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 400..486
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 464..466
FT /note="D/ECD-tripeptide"
FT ACT_SITE 333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 307..387
FT /evidence="ECO:0000250"
FT DISULFID 347..371
FT /evidence="ECO:0000250"
FT DISULFID 350..355
FT /evidence="ECO:0000250"
FT DISULFID 403..432
FT /evidence="ECO:0000250"
FT DISULFID 414..427
FT /evidence="ECO:0000250"
FT DISULFID 416..422
FT /evidence="ECO:0000250"
FT DISULFID 426..449
FT /evidence="ECO:0000250"
FT DISULFID 440..446
FT /evidence="ECO:0000250"
FT DISULFID 445..471
FT /evidence="ECO:0000250"
FT DISULFID 458..478
FT /evidence="ECO:0000250"
FT DISULFID 465..497
FT /evidence="ECO:0000250"
FT DISULFID 490..502
FT /evidence="ECO:0000250"
FT DISULFID 509..559
FT /evidence="ECO:0000250"
FT DISULFID 524..567
FT /evidence="ECO:0000250"
FT DISULFID 537..547
FT /evidence="ECO:0000250"
FT DISULFID 554..593
FT /evidence="ECO:0000250"
FT DISULFID 587..598
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 605 AA; 68202 MW; E3436362EADA5C78 CRC64;
MLVVFPYQGS SIILESGNVN DYEVVYPQKV PSLPKGGVQN PQPETKYEDT MQYEFHVNGE
PVVPHLEKNK GLFSEDYTET HYASDGREIT TSPSVQDHCY YYGYIQNEAD SSAAISACDG
LKGHFKHQGE TYFIEPLKLS NSEAHAIYKD ENVEEEDETP KICGLTQTTW ESDEPFKNTS
LLIYTPEQNR YLQAKKYIEF YVAVDNRMYR HYKRNKTVIK RRVYELVNIL NTIFRRLNFY
IALIGLEIWS KRDKVNVQSD VKVTLKSFGK WREKKVAATQ KEYNAQLLTR IDFNGNTVGL
AALGALCSVK YSVAVIQDYS KRTSMVASTM AHEMGHNLGI NHDRASCTSC GSNKCIMSTK
RTKPAYRFSS CSVREHRRYL LRDRPQCILN KPLITDIVAP AICGNYFVEV GEECDCGSPR
DCQSACCNAA TCKLKHGAQC DSGECCRKCK FKKAGAKCRA VKDDCDLPER CTGRSAECPT
DIFRRNGLPC QNNQGYCYNG KCPTLTNQCI AFMGPNVKVS RDSCFTLNQR GKGCGYCRMQ
NGAKFPCAAK DIKCGKLFCK KRNSKICNCL ISPDDPNYGM VEPGTKCGDG VVCSNRKCVK
LQRVY
