VM3B_NAJAT
ID VM3B_NAJAT Reviewed; 593 AA.
AC D6PXE8; D3YRL5;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like atrase-B;
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], PROTEIN SEQUENCE OF 192-211, FUNCTION, ACTIVITY
RP REGULATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom gland;
RX PubMed=20837040; DOI=10.1016/j.toxicon.2010.08.013;
RA Sun Q.Y., Bao J.;
RT "Purification, cloning and characterization of a metalloproteinase from
RT Naja atra venom.";
RL Toxicon 56:1459-1469(2010).
RN [2]
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 the classical and
CC alternative pathways of complement by cleaving factor B, C6, C7, and
CC C8. Also slowly and selectively degrades alpha-chain of fibrinogen
CC (FGA), and shows edema-inducing activity.
CC {ECO:0000269|PubMed:20837040}.
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: Inhibited by EDTA, EGTA, 1,10-phenanthroline and
CC DTT. Not inhibited by PMSF and SBTI. {ECO:0000269|PubMed:20837040}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=49400; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20837040};
CC -!- MISCELLANEOUS: Does not degrade beta- and gamma-chains of fibrinogen.
CC Does not hydrolyze fibrin, azocasein and BAEE. Does not show
CC hemorrhagic activity (PubMed:20837040). {ECO:0000305|PubMed:20837040}.
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; GU902978; ADD14036.1; -; mRNA.
DR EMBL; GU985447; ADG02948.1; -; mRNA.
DR AlphaFoldDB; D6PXE8; -.
DR SMR; D6PXE8; -.
DR MEROPS; M12.236; -.
DR PRIDE; D6PXE8; -.
DR TopDownProteomics; D6PXE8; -.
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; -; 2.
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; PF01562; Pep_M12B_propep; 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; Complement system impairing toxin; Direct protein sequencing;
KW Disulfide bond; Fibrinogenolytic toxin; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Signal; Toxin; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000269|PubMed:20837040"
FT /id="PRO_0000418031"
FT CHAIN 192..593
FT /note="Zinc metalloproteinase-disintegrin-like atrase-B"
FT /id="PRO_0000418032"
FT DOMAIN 205..400
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 408..477
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 455..457
FT /note="D/ECD-tripeptide"
FT ACT_SITE 342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 395
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="1"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 316..395
FT /evidence="ECO:0000250"
FT DISULFID 356..379
FT /evidence="ECO:0000250"
FT DISULFID 358..363
FT /evidence="ECO:0000250"
FT DISULFID 422..435
FT /evidence="ECO:0000250"
FT DISULFID 424..430
FT /evidence="ECO:0000250"
FT DISULFID 434..440
FT /evidence="ECO:0000250"
FT DISULFID 449..469
FT /evidence="ECO:0000250"
FT DISULFID 456..488
FT /evidence="ECO:0000250"
FT DISULFID 481..493
FT /evidence="ECO:0000250"
FT DISULFID 500..550
FT /evidence="ECO:0000250"
FT DISULFID 515..558
FT /evidence="ECO:0000250"
FT DISULFID 528..538
FT /evidence="ECO:0000250"
FT DISULFID 545..581
FT /evidence="ECO:0000250"
FT DISULFID 575..586
FT /evidence="ECO:0000250"
SQ SEQUENCE 593 AA; 66246 MW; FA9BD3873780BE92 CRC64;
MIQALLVIIC LAVFPHQGSS IILESGNVND YEVVYPQKVP ALLKGGVQNP QPETKYEDTM
RYEFQVNGEP VVLHLERNKG LFSEDYTETH YAPDGREITT SPPVQDHCYY HGYIQNEADS
SAVISACDGL KGHFEHQGET YFIEPLKISN SEAHAIYKDE NVENEDETPE ICGVTETTWE
SDESIEKTSQ LTNTPEQDRY LQDKKYIEFY VIVDNRMYRY YNNDKPAIKI RVYEMINAVN
TKFRPLKIHI ALIGLEIWSN KDKFEVKPAA SVTLKSFGEW RETVLLPRKR NDNAQLLTGI
DFNGNTVGRA YIGSLCKTNE SVAIVQDYNR RISLVASTMT HELGHNLGIH HDKASCICIP
GPCIMLKKRT APAFQFSSCS IREYREYLLR DRPQCILNKP LSTDIVSPPI CGNYFVEVGE
ECDCGSPQAC QSACCNAATC QFKGAETECR VAKDDCDLPE LCTGQSAECP TDSLQRNGHP
CQNNQGYCYN RTCPTLTNQC ITLLGPHFTV SPKGCFDLNM RGDDGSFCGM EDGTKIPCAA
KDVKCGRLYC TEKNTMSCLI PPNPDGIMAE PGTKCGDGMV CSKGQCVDVQ TAY
