NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

Details

Name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
Synonyms
  • CI-18 kDa
  • CI-AQDQ
  • Complex I-18 kDa
  • Complex I-AQDQ
  • NADH-ubiquinone oxidoreductase 18 kDa subunit
Gene Name
NDUFS4
Organism
Humans
Amino acid sequence
>lcl|BSEQ0016111|NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
MAAVSMSVVLRQTLWRRRAVAVAALSVSRVPTRSLRTSTWRLAQDQTQDTQLITVDEKLD
ITTLTGVPEEHIKTRKVRIFVPARNNMQSGVNNTKKWKMEFDTRERWENPLMGWASTADP
LSNMVLTFSTKEDAVSFAEKNGWSYDIEERKVPKPKSKSYGANFSWNKRTRVSTK
Number of residues
175
Molecular Weight
20107.84
Theoretical pI
11.02
GO Classification
Functions
NADH dehydrogenase (ubiquinone) activity
Processes
brain development / cAMP-mediated signaling / cellular metabolic process / cellular respiration / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / positive regulation of fibroblast proliferation / reactive oxygen species metabolic process / regulation of protein phosphorylation / respiratory electron transport chain / response to cAMP / small molecule metabolic process
Components
mitochondrial inner membrane / mitochondrial respiratory chain complex I / mitochondrion
General Function
Nadh dehydrogenase (ubiquinone) activity
Specific Function
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Mitochondrion inner membrane
Gene sequence
>lcl|BSEQ0016112|NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial (NDUFS4)
ATGGCGGCGGTGTCAATGTCAGTGGTACTGAGGCAGACGTTGTGGCGGAGAAGGGCAGTG
GCTGTAGCTGCCCTTTCCGTTTCCAGGGTTCCGACCAGGTCGTTGAGGACTTCCACATGG
AGATTGGCACAGGACCAGACTCAAGACACACAACTCATAACAGTTGATGAAAAATTGGAT
ATCACTACTTTAACTGGAGTTCCAGAAGAGCATATAAAAACTAGAAAAGTCAGGATCTTT
GTTCCTGCTCGCAATAACATGCAGTCTGGAGTAAACAACACAAAGAAATGGAAGATGGAG
TTTGATACCAGAGAGCGATGGGAAAATCCTTTGATGGGTTGGGCATCAACGGCTGATCCC
TTATCCAACATGGTTCTAACCTTCAGTACTAAAGAAGATGCAGTTTCCTTTGCAGAAAAA
AATGGATGGAGCTATGACATTGAAGAGAGGAAGGTTCCAAAACCCAAGTCCAAGTCTTAT
GGTGCAAACTTTTCTTGGAACAAAAGAACAAGAGTATCCACAAAATAG
Chromosome Location
5
Locus
5q11.1
External Identifiers
ResourceLink
UniProtKB IDO43181
UniProtKB Entry NameNDUS4_HUMAN
GenBank Protein ID2655053
GenBank Gene IDAF020351
GenAtlas IDNDUFS4
HGNC IDHGNC:7711
General References
  1. van den Heuvel L, Ruitenbeek W, Smeets R, Gelman-Kohan Z, Elpeleg O, Loeffen J, Trijbels F, Mariman E, de Bruijn D, Smeitink J: Demonstration of a new pathogenic mutation in human complex I deficiency: a 5-bp duplication in the nuclear gene encoding the 18-kD (AQDQ) subunit. Am J Hum Genet. 1998 Feb;62(2):262-8. [Article]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  3. 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. [Article]
  4. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  5. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00157NADHapproved, nutraceuticalunknownDetails