ID   VM3_NAJOX               Reviewed;          22 AA.
AC   P0DJJ4;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Zinc metalloproteinase oxiagin;
DE            EC=3.4.24.-;
DE   AltName: Full=Snake venom metalloprotease;
DE            Short=SVMP;
DE   Flags: Fragment;
OS   Naja oxiana (Central Asian cobra) (Oxus cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8657;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=15829304; DOI=10.1016/j.molimm.2004.11.009;
RA   Shoibonov B.B., Osipov A.V., Kryukova E.V., Zinchenko A.A., Lakhtin V.M.,
RA   Tsetlin V.I., Utkin Y.N.;
RT   "Oxiagin from the Naja oxiana cobra venom is the first reprolysin
RT   inhibiting the classical pathway of complement.";
RL   Mol. Immunol. 42:1141-1153(2005).
CC   -!- FUNCTION: Snake venom metalloproteinase that inhibits the classical
CC       complement pathway dose-dependently. It acts by binding to
CC       carbohydrates of IgG within the antibody-sensitized sheep erythrocytes
CC       (EA) complex, and thus prevents interaction of component C2 with
CC       immobilized C4b. Also induces cation-independent hemagglutination that
CC       can be prevented by D-galactose pretreatment.
CC       {ECO:0000269|PubMed:15829304}.
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: Heterotrimer; disulfide-linked. The heterotrimer consists of 1
CC       metalloproteinase chain and 2 lectin chains (Probable).
CC       {ECO:0000305|PubMed:15829304}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: N-glycosylated.
CC   -!- MASS SPECTROMETRY: Mass=49800; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15829304};
CC   -!- MISCELLANEOUS: Does not show proteolytic activity on rabbit IgG, human
CC       C3 and C4 complement components, fibrinogen, beta-casein, hemoglobin,
CC       ferritin, myoglobin, chymotrypsinogen, and melittin.
CC       {ECO:0000305|PubMed:15829304}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIId sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DJJ4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cell adhesion impairing toxin; Complement system impairing toxin;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT   CHAIN           1..>22
FT                   /note="Zinc metalloproteinase oxiagin"
FT                   /id="PRO_0000418194"
FT   DOMAIN          14..>22
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        8..?
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..?
FT                   /evidence="ECO:0000250"
FT   NON_TER         22
SQ   SEQUENCE   22 AA;  2640 MW;  17B5542D28899940 CRC64;
     TNTPEQQCYL QAKCYIEFYV VV