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Showing Protein NmrA-like family domain-containing protein 1 (HMDBP12624)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP12624
Secondary Accession Numbers None
Name NmrA-like family domain-containing protein 1
Synonyms Not Available
Gene Name NMRAL1
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer.
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
urea cycle
Cellular Component
cytosol
perinuclear region of cytoplasm
nucleoplasm
Molecular Function
identical protein binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 299
Molecular Weight 33344.14
Theoretical pI 7.52
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q9HBL8
UniProtKB/Swiss-Prot Entry Name NMRL1_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
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  3. Zheng X, Dai X, Zhao Y, Chen Q, Lu F, Yao D, Yu Q, Liu X, Zhang C, Gu X, Luo M: Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein. Proc Natl Acad Sci U S A. 2007 May 22;104(21):8809-14. Epub 2007 May 11. [PubMed:17496144 ]
  4. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [PubMed:22814378 ]
  5. Zhao Y, Zhang J, Li H, Li Y, Ren J, Luo M, Zheng X: An NADPH sensor protein (HSCARG) down-regulates nitric oxide synthesis by association with argininosuccinate synthetase and is essential for epithelial cell viability. J Biol Chem. 2008 Apr 18;283(16):11004-13. doi: 10.1074/jbc.M708697200. Epub 2008 Feb 8. [PubMed:18263583 ]
  6. Dai X, Li Y, Meng G, Yao S, Zhao Y, Yu Q, Zhang J, Luo M, Zheng X: NADPH is an allosteric regulator of HSCARG. J Mol Biol. 2009 Apr 17;387(5):1277-85. doi: 10.1016/j.jmb.2009.02.049. Epub 2009 Feb 28. [PubMed:19254724 ]