VM3K_NAJKA
ID VM3K_NAJKA Reviewed; 401 AA.
AC P82942;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Hemorrhagic metalloproteinase-disintegrin-like kaouthiagin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
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 {ECO:0000305};
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND GLYCOSYLATION AT ASN-112.
RC TISSUE=Venom;
RX PubMed=11284707; DOI=10.1021/bi0022700;
RA Ito M., Hamako J., Sakurai Y., Matsumoto M., Fujimura Y., Suzuki M.,
RA Hashimoto K., Titani K., Matsui T.;
RT "Complete amino acid sequence of kaouthiagin, a novel cobra venom
RT metalloproteinase with two disintegrin-like sequences.";
RL Biochemistry 40:4503-4511(2001).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=9759634;
RA Hamako J., Matsui T., Nishida S., Nomura S., Fujimura Y., Ito M., Ozeki Y.,
RA Titani K.;
RT "Purification and characterization of kaouthiagin, a von Willebrand factor-
RT binding and -cleaving metalloproteinase from Naha kaouthia cobra venom.";
RL Thromb. Haemost. 80:499-505(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: Snake venom zinc protease that inhibits hemostasis by binding
CC and cleaving the vWF in humans. Has also and inhibitory effect on the
CC collagen-induced platelet aggregation. {ECO:0000269|PubMed:11284707}.
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:0000269|PubMed:9759634}.
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 AlphaFoldDB; P82942; -.
DR SMR; P82942; -.
DR iPTMnet; P82942; -.
DR PRIDE; P82942; -.
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; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF01421; Reprolysin; 1.
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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..401
FT /note="Hemorrhagic metalloproteinase-disintegrin-like
FT kaouthiagin"
FT /id="PRO_0000078193"
FT DOMAIN 14..208
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 216..285
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 263..265
FT /note="D/ECD-tripeptide"
FT ACT_SITE 150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 17
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11284707"
FT DISULFID 125..203
FT /evidence="ECO:0000250"
FT DISULFID 164..187
FT /evidence="ECO:0000250"
FT DISULFID 166..171
FT /evidence="ECO:0000250"
FT DISULFID 219..248
FT /evidence="ECO:0000250"
FT DISULFID 230..243
FT /evidence="ECO:0000250"
FT DISULFID 232..238
FT /evidence="ECO:0000250"
FT DISULFID 257..277
FT /evidence="ECO:0000250"
FT DISULFID 264..296
FT /evidence="ECO:0000250"
FT DISULFID 289..301
FT /evidence="ECO:0000250"
FT DISULFID 308..358
FT /evidence="ECO:0000250"
FT DISULFID 323..366
FT /evidence="ECO:0000250"
FT DISULFID 336..346
FT /evidence="ECO:0000250"
FT DISULFID 353..389
FT /evidence="ECO:0000250"
FT DISULFID 383..394
FT /evidence="ECO:0000250"
SQ SEQUENCE 401 AA; 44493 MW; 0D71172E78E4BED2 CRC64;
TNTPEQDRYL QAEKYIEFYV IVDNRMYRYY NYDKPAIKIR VYEMINAVNT KFRPLKIHIA
LIGLEIWSNE DKFEVKPAAS VTLKSFREWR QTVLLPRKRN DNAQLLTGIN LNGTAVGIAY
PGSLCTQRSV FVVQDYNRRM SLVASTMTHE LGHNLGIHHD EASCICIPGP CIMLKKRTAP
AFQFSSCSIR DYQEYLLRDR PQCILNKPLS TDIVSPAICG NYFVEEGEEC DCGSPAACQS
ACCDAATCKF NGAGAECRAA KHDCDLPELC TGQSAECPTD SLQRNGHPCQ NNQGYCYNGK
CPTLTNQCIA LLGPHFTVSP KGCFDLNMRG DDGSFCRMED GTKIPCAAKD VKCGRLYCTE
KNTMSCLIPP NPDGIMAEPG TKCGDGMVCS KGQCVDVQTA Y
