VM3_NAJKA
ID VM3_NAJKA Reviewed; 600 AA.
AC Q9PVK7;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like cobrin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Naja kaouthia (Monocled cobra) (Naja siamensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Bambai B., Bredehorst R., Vogel C.-W.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=3045125; DOI=10.1016/s0021-9258(18)37808-6;
RA O'Keefe M.C., Caporale L.H., Vogel C.-W.;
RT "A novel cleavage product of human complement component C3 with structural
RT and functional properties of cobra venom factor.";
RL J. Biol. Chem. 263:12690-12697(1988).
RN [3]
RP REVIEW.
RX PubMed=20417224; DOI=10.1016/j.toxicon.2010.04.007;
RA Vogel C.-W., Fritzinger D.C.;
RT "Cobra venom factor: Structure, function, and humanization for therapeutic
RT complement depletion.";
RL Toxicon 56:1198-1222(2010).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that may cleave complement
CC protein C3 into C3c-like (C3o). {ECO:0000269|PubMed:3045125}.
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.
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; AF063190; AAF00693.1; -; mRNA.
DR AlphaFoldDB; Q9PVK7; -.
DR SMR; Q9PVK7; -.
DR MEROPS; M12.159; -.
DR PRIDE; Q9PVK7; -.
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; 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; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Calcium; Complement system impairing toxin; Disulfide bond; Glycoprotein;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal;
KW Toxin; Zinc; Zymogen.
FT SIGNAL 1..8
FT /evidence="ECO:0000255"
FT PROPEP 9..179
FT /evidence="ECO:0000255"
FT /id="PRO_0000418033"
FT CHAIN 180..600
FT /note="Zinc metalloproteinase-disintegrin-like cobrin"
FT /id="PRO_0000418034"
FT DOMAIN 193..388
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 396..482
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 460..462
FT /note="D/ECD-tripeptide"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 405
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 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 304..383
FT /evidence="ECO:0000250"
FT DISULFID 344..367
FT /evidence="ECO:0000250"
FT DISULFID 346..351
FT /evidence="ECO:0000250"
FT DISULFID 399..428
FT /evidence="ECO:0000250"
FT DISULFID 410..423
FT /evidence="ECO:0000250"
FT DISULFID 412..418
FT /evidence="ECO:0000250"
FT DISULFID 422..445
FT /evidence="ECO:0000250"
FT DISULFID 436..442
FT /evidence="ECO:0000250"
FT DISULFID 441..467
FT /evidence="ECO:0000250"
FT DISULFID 454..474
FT /evidence="ECO:0000250"
FT DISULFID 461..492
FT /evidence="ECO:0000250"
FT DISULFID 486..497
FT /evidence="ECO:0000250"
FT DISULFID 504..554
FT /evidence="ECO:0000250"
FT DISULFID 519..562
FT /evidence="ECO:0000250"
FT DISULFID 532..542
FT /evidence="ECO:0000250"
FT DISULFID 549..588
FT /evidence="ECO:0000250"
FT DISULFID 582..593
FT /evidence="ECO:0000250"
SQ SEQUENCE 600 AA; 67662 MW; C7C0D45EBC694290 CRC64;
MIQLSWSSII LESGNVNDYE VVYPQKVPAL LKGGVQNPQP ETKYEDTMQY EFQVNGEPVV
LHLERNKGLF SEDYTETHYA PDGREITTSP PVQDHCYYHG YFQNEADSSA VISACDGLKG
HFKLQGEIYF IEPLKISDSE AHAIYKDENV EEEDETPKIC GVTDTTWESD EPIKKTSLLT
NTPEQDRYLQ AEKYIEFYMV VDNIMYRHYK RNQLVIKRKV YEMINTMNMI YRRLNFHIAL
IGLEIWSNIN EINVQSDVKA TLDLFGEWRE KKLLPRKRND NAQLLTGIDF NGTPVGLAYI
GSICNPKTSA AVVQDYSKST RMVAITMAHE MGHNLGMNHD KGFCTCGFNK CVMSTRRTKP
AYQFSSCSVR EHQRYLLRDR PQCILNKPLS TDIVSPPICG NYFVEVGEEC DCGSPADCQS
ACCNATTCKL QHEAQCDSEE CCEKCKFKGA GAECRAAKDD CDLPELCTGQ SAECPTDVFQ
RNGLPCQNNG YCYNGKCPIM TNQCIALRGP GVKVSRDSCF TLNQRTRGCG LCRMEYGRKI
PCAAKDVKCG RLFCKKRNSM ICNCSISPRD PSYGMVEPGT KCGDGMVCSN RQCVDVKTAY
