VM3_NAJAT
ID VM3_NAJAT Reviewed; 621 AA.
AC A8QL59;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like NaMP;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Naja atra (Chinese cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8656;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF080840; ABN72547.1; -; mRNA.
DR AlphaFoldDB; A8QL59; -.
DR SMR; A8QL59; -.
DR MEROPS; M12.331; -.
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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..188
FT /evidence="ECO:0000250"
FT /id="PRO_0000417641"
FT CHAIN 189..621
FT /note="Zinc metalloproteinase-disintegrin-like NaMP"
FT /id="PRO_0000417642"
FT DOMAIN 206..402
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 410..496
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 474..476
FT /note="D/ECD-tripeptide"
FT ACT_SITE 343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 317..397
FT /evidence="ECO:0000250"
FT DISULFID 357..381
FT /evidence="ECO:0000250"
FT DISULFID 359..364
FT /evidence="ECO:0000250"
FT DISULFID 413..442
FT /evidence="ECO:0000250"
FT DISULFID 424..437
FT /evidence="ECO:0000250"
FT DISULFID 426..432
FT /evidence="ECO:0000250"
FT DISULFID 436..459
FT /evidence="ECO:0000250"
FT DISULFID 450..456
FT /evidence="ECO:0000250"
FT DISULFID 455..481
FT /evidence="ECO:0000250"
FT DISULFID 468..488
FT /evidence="ECO:0000250"
FT DISULFID 475..507
FT /evidence="ECO:0000250"
FT DISULFID 500..512
FT /evidence="ECO:0000250"
FT DISULFID 519..569
FT /evidence="ECO:0000250"
FT DISULFID 534..579
FT /evidence="ECO:0000250"
FT DISULFID 547..557
FT /evidence="ECO:0000250"
FT DISULFID 564..605
FT /evidence="ECO:0000250"
FT DISULFID 599..610
FT /evidence="ECO:0000250"
SQ SEQUENCE 621 AA; 69403 MW; 6F558D941AC13737 CRC64;
MIQPLLVAIC LVVFPYQGSS TILESGKVRD YEVVYPQKIP SLPKGRLQRR EEKTKYENTM
KYEFKVNGEP VVLNLEKNKR LFSKDYTETH YSPDGREITT SPPVQDHCYY HGHIQNDADS
TAVIRACDGL NGYFKSNGEM YIIEPLKLSD SEAHAVFKYE SLEKEDETPK TCGAIHNSGE
SDETIKKISN TFVTPEKGEE YLEAEKHIEL YMVADNLVYR KYSSNITVVR MRIFEILNYV
NLYYKILNIH VVLIGLEVWS DEDKILINGS SELTVRSFAA WRHSDLLKHK RNDNAQLLTG
IHFDKRVLGI AFIGGMCNNF TSVGAIQDNS IHAVLIAATM THELGHNLGM NHDTDSCTCN
TGPCIMKAAL NFKPPYEFSS CSYWDFQNYI MTKSAQCILN DPLTTDIVPT AICGNGFVEE
GEECDCGPPE ICKNECCEAA TCKLKPEAQC ASGACCEECQ FRRAGELCRA AKDDCDLDEL
CTGQSAECPM NHFHMNGHPC QNNQGYCFRG TCPTLTKQCI ALWGPDAEVA PDGCFMNNQK
GNYYGYCKKK NGTNIPCEPE NVKCGRLYCI DDSTEENSCK FHFSNENANS GMVQPGTKCG
EGMVCGFGEC IGLETALGIN Q
