Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M407486200 on August 26, 2004

J. Biol. Chem., Vol. 279, Issue 46, 48159-48167, November 12, 2004
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
279/46/48159    most recent
M407486200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Xin, X.
Right arrow Articles by Eipper, B. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Xin, X.
Right arrow Articles by Eipper, B. A.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Monooxygenase X, a Member of the Copper-dependent Monooxygenase Family Localized to the Endoplasmic Reticulum*

Xiaonan Xin, Richard E. Mains, and Betty A. Eipper{ddagger}

From the Department of Neuroscience, University of Connecticut Health Center, Farmington, Connecticut 06030-3401

Based on sequence comparisons, MOX (monooxygenase X), is a member of the copper monooxygenase family that includes dopamine {beta}-monooxygenase (DBM) and peptidylglycine {alpha}-hydroxylating monooxygenase (PHM). MOX has all of the residues expected to be critical for copper binding, and its cysteine residues can yield the intramolecular disulfide bond pattern observed in DBM. Although DBM and PHM function within the lumen of the secretory pathway, the published sequence for human MOX lacks a signal sequence, suggesting that it does not enter this compartment. We identified an upstream exon that encodes the signal sequence of human MOX. A retained intron yields minor amounts of transcript encoding MOX without a signal sequence. MOX transcripts are widely expressed, with the highest levels in the salivary gland and ovary and moderate levels in brain, pituitary, and heart. Despite the presence of a signal sequence, exogenous MOX is not secreted, and it localizes throughout the endoplasmic reticulum in both endocrine or nonendocrine cells. Neither appending green fluorescent protein to its C terminus nor deleting the hydrophobic domain near its C terminus facilitates secretion of MOX. MOX is N-glycosylated, is tightly membrane-associated, and forms oligomers that are not disulfide-linked. Based on its sequence and localization, MOX is predicted to hydroxylate a hydrophobic substrate in the endoplasmic reticulum.


Received for publication, July 6, 2004 , and in revised form, August 24, 2004.

* This work was supported by National Institutes of Health Grant DK-32949. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} To whom correspondence should be addressed: Dept. of Neuroscience, University of Connecticut Health Center, 263 Farmington Ave., Farmington, CT 06030-3401. Tel.: 860-679-8898; Fax: 860-679-1885; E-mail: eipper{at}uchc.edu.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Mol Biol EvolHome page
Y. Hahn, S. Jeong, and B. Lee
Inactivation of MOXD2 and S100A15A by Exon Deletion during Human Evolution
Mol. Biol. Evol., October 1, 2007; 24(10): 2203 - 2212.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. De, J. Bell, N. J. Blackburn, R. E. Mains, and B. A. Eipper
Role for an Essential Tyrosine in Peptide Amidation
J. Biol. Chem., July 28, 2006; 281(30): 20873 - 20882.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement