Search
DBH-like monooxygenase protein 2 (MOXD2P, MOXD2)
Function:
- monooxygenase (putative)
Cofactor: binds 2 copper ions per subunit (putative)
Structure:
- belongs to the copper type 2 ascorbate-dependent monooxygenase family
- contains 1 DOMON domain
Genetics:
- could be the product of a pseudogene
- human MOXD2gene lacks the last 2 terminal exons, as well as the 3'-UTR & poly(A) signal found in all other mammalian sequences
- this deletion, which occured after the divergence of humans & chimpanzees, may interfere with proper mRNA processing &/or translation
General
evolutionary divergent human protein
glycoprotein
hydroxylase; monooxygenase
Properties
SIZE: entity length = 499 aa
MW = 56 kD
MOTIF: signal sequence {1-16}
DOMON {40-156}
tyrosine residue {Y209}
cysteine residue {C211}
MODIFICATION: cysteine residue {C261}
N-glycosylation site {N236}
copper [Cu]-binding site
SITE: 241-241
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 242-242
MOTIF: histidine residue (3)
cysteine residue {C248}
MODIFICATION: cysteine residue {C271}
active site
N-glycosylation site {N250}
cysteine residue {C261}
MODIFICATION: cysteine residue {C211}
cysteine residue {C271}
MODIFICATION: cysteine residue {C248}
copper [Cu]-binding site
SITE: 308-308
MOTIF: histidine residue (3)
cysteine residue {C365}
MODIFICATION: cysteine residue {C480}
histidine residue {H389}
copper [Cu]-binding site
SITE: 389-389
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 391-391
MOTIF: histidine residue (3)
N-glycosylation site {N404}
cysteine residue {C443}
MODIFICATION: cysteine residue {C465}
copper [Cu]-binding site
SITE: 464-464
MOTIF: histidine residue (3)
cysteine residue {C465}
MODIFICATION: cysteine residue {C443}
N-glycosylation site {N476}
cysteine residue {C480}
MODIFICATION: cysteine residue {C365}
Database Correlations
UniProt A6NHM9
PFAM correlations
References
UniProt :accession A6NHM9