| Identification |
|---|
| HMDB Protein ID
| HMDBP00182 |
| Secondary Accession Numbers
| |
| Name
| NADH-ubiquinone oxidoreductase chain 3 |
| Synonyms
|
- NADH dehydrogenase subunit 3
|
| Gene Name
| MT-ND3 |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Involved in NADH dehydrogenase (ubiquinone) activity |
| Specific Function
| Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
|
| Pathways
|
- Oxidative phosphorylation
- Parkinson disease
|
| Reactions
|
| NADH + Coenzyme Q10 → NAD + QH(2) |
details
|
| QH2 + Acceptor → Ubiquinone-2 + Reduced acceptor |
details
|
|
| GO Classification
|
| Biological Process |
| small molecule metabolic process |
| response to oxidative stress |
| mitochondrial electron transport, NADH to ubiquinone |
| response to hormone stimulus |
| response to light intensity |
| Cellular Component |
| integral to membrane |
| mitochondrial respiratory chain complex I |
| Function |
| catalytic activity |
| oxidoreductase activity |
| oxidoreductase activity, acting on nadh or nadph |
| nadh dehydrogenase activity |
| nadh dehydrogenase (quinone) activity |
| nadh dehydrogenase (ubiquinone) activity |
| Molecular Function |
| NADH dehydrogenase (ubiquinone) activity |
| Process |
| metabolic process |
| oxidation reduction |
|
| Cellular Location
|
- Mitochondrion membrane
- Multi-pass membrane protein
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| MT-ND3 |
| Gene Sequence
|
>346 bp
ATAAACTTCGCCTTAATTTTAATAATCAACACCCTCCTAGCCTTACTACTAATAATTATT
ACATTTTGACTACCACAACTCAACGGCTACATAGAAAAATCCACCCCTTACGAGTGCGGC
TTCGACCCTATATCCCCCGCCCGCGTCCCTTTCTCCATAAAATTCTTCTTAGTAGCTATT
ACCTTCTTATTATTTGATCTAGAAATTGCCCTCCTTTTACCCCTACCATGAGCCCTACAA
ACAACTAACCTGCCACTAATAGTTATGTCATCCCTCTTATTAATCATCATCCTAGCCCTA
AGTCTGGCCTATGAGTGACTACAAAAAGGATTAGACTGAACCGAAT
|
| Protein Properties |
|---|
| Number of Residues
| 115 |
| Molecular Weight
| 13185.87 |
| Theoretical pI
| 4.41 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
>NADH-ubiquinone oxidoreductase chain 3
MNFALILMINTLLALLLMIITFWLPQLNGYMEKSTPYECGFDPMSPARVPFSMKFFLVAI
TFLLFDLEIALLLPLPWALQTTNLPLMVMSSLLLIIILALSLAYEWLQKGLDWTE
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P03897 |
| UniProtKB/Swiss-Prot Entry Name
| NU3M_HUMAN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| J01415 |
| GeneCard ID
| MT-ND3 |
| GenAtlas ID
| MT-ND3 |
| HGNC ID
| HGNC:7458 |
| References |
|---|
| General References
| - Murray J, Zhang B, Taylor SW, Oglesbee D, Fahy E, Marusich MF, Ghosh SS, Capaldi RA: The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification. J Biol Chem. 2003 Apr 18;278(16):13619-22. Epub 2003 Feb 28. [PubMed:12611891 ]
- Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed:7219534 ]
- Moilanen JS, Finnila S, Majamaa K: Lineage-specific selection in human mtDNA: lack of polymorphisms in a segment of MTND5 gene in haplogroup J. Mol Biol Evol. 2003 Dec;20(12):2132-42. Epub 2003 Aug 29. [PubMed:12949126 ]
- Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed:11130070 ]
- Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed:12840039 ]
- Coble MD, Just RS, O'Callaghan JE, Letmanyi IH, Peterson CT, Irwin JA, Parsons TJ: Single nucleotide polymorphisms over the entire mtDNA genome that increase the power of forensic testing in Caucasians. Int J Legal Med. 2004 Jun;118(3):137-46. Epub 2004 Feb 4. [PubMed:14760490 ]
- Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed:3921850 ]
- Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed:1757091 ]
- Oliver NA, Greenberg BD, Wallace DC: Assignment of a polymorphic polypeptide to the human mitochondrial DNA unidentified reading frame 3 gene by a new peptide mapping strategy. J Biol Chem. 1983 May 10;258(9):5834-9. [PubMed:6343397 ]
- Taylor RW, Singh-Kler R, Hayes CM, Smith PE, Turnbull DM: Progressive mitochondrial disease resulting from a novel missense mutation in the mitochondrial DNA ND3 gene. Ann Neurol. 2001 Jul;50(1):104-7. [PubMed:11456298 ]
- Sarzi E, Brown MD, Lebon S, Chretien D, Munnich A, Rotig A, Procaccio V: A novel recurrent mitochondrial DNA mutation in ND3 gene is associated with isolated complex I deficiency causing Leigh syndrome and dystonia. Am J Med Genet A. 2007 Jan 1;143A(1):33-41. [PubMed:17152068 ]
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