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Protein

Zinc metalloproteinase oxiagin

Gene
N/A
Organism
Naja oxiana (Central Asian cobra) (Oxus cobra)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Snake venom metalloproteinase that inhibits the classical complement pathway dose-dependently. It acts by binding to carbohydrates of IgG within the antibody-sensitized sheep erythrocytes (EA) complex, and thus prevents interaction of component C2 with immobilized C4b. Also induces cation-independent hemagglutination that can be prevented by D-galactose pretreatment.1 Publication

Miscellaneous

Does not show proteolytic activity on rabbit IgG, human C3 and C4 complement components, fibrinogen, beta-casein, hemoglobin, ferritin, myoglobin, chymotrypsinogen, and melittin.1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

GO - Molecular functioni

Keywordsi

Molecular functionCell adhesion impairing toxin, Complement system impairing toxin, Hydrolase, Metalloprotease, Protease, Toxin
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc metalloproteinase oxiagin (EC:3.4.24.-)
Alternative name(s):
Snake venom metalloprotease
Short name:
SVMP
OrganismiNaja oxiana (Central Asian cobra) (Oxus cobra)
Taxonomic identifieri8657 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004181941 – ›22Zinc metalloproteinase oxiaginAdd BLAST›22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi8 ↔ ?By similarity
Disulfide bondi14 ↔ ?By similarity

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterotrimer; disulfide-linked. The heterotrimer consists of 1 metalloproteinase chain and 2 lectin chains (Probable).1 Publication

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – ›22Peptidase M12BPROSITE-ProRule annotation›9

Sequence similaritiesi

Sequencei

Sequence statusi: Fragment.

P0DJJ4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20 
TNTPEQQCYL QAKCYIEFYV VV
Length:22
Mass (Da):2,640
Last modified:July 11, 2012 - v1
Checksum:i17B5542D28899940
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei221

Mass spectrometryi

Molecular mass is 49800 Da from positions 1 - ?. Determined by MALDI. 1 Publication

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiVM3_NAJOX
AccessioniPrimary (citable) accession number: P0DJJ4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: July 11, 2012
Last modified: November 22, 2017
This is version 15 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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