NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

NameNADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
Synonyms
  • 1.6.5.3
  • NADH-ubiquinone oxidoreductase 24 kDa subunit
Gene NameNDUFV2
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010175|NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
MFFSAALRARAAGLTAHWGRHVRNLHKTVMQNGAGGALFVHRDTPENNPDTPFDFTPENY
KRIEAIVKNYPEGHKAAAVLPVLDLAQRQNGWLPISAMNKVAEVLQVPPMRVYEVATFYT
MYNRKPVGKYHIQVCTTTPCMLRNSDSILEAIQKKLGIKVGETTPDKLFTLIEVECLGAC
VNAPMVQINDNYYEDLTAKDIEEIIDELKAGKIPKPGPRSGRFSCEPAGGLTSLTEPPKG
PGFGVQAGL
Number of residues249
Molecular Weight27391.36
Theoretical pI8.21
GO Classification
Functions
  • NADH dehydrogenase (ubiquinone) activity
  • metal ion binding
  • electron carrier activity
  • 2 iron, 2 sulfur cluster binding
Processes
  • mitochondrial electron transport, NADH to ubiquinone
  • small molecule metabolic process
  • cellular metabolic process
  • respiratory electron transport chain
  • nervous system development
  • cardiac muscle tissue development
Components
  • mitochondrion
  • mitochondrial inner membrane
  • myelin sheath
  • mitochondrial respiratory chain complex I
General FunctionNadh dehydrogenase (ubiquinone) activity
Specific FunctionCore 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).
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID188852
UniProtKB IDP19404
UniProtKB Entry NameNDUV2_HUMAN
Cellular LocationMitochondrion inner membrane
Gene sequence
>lcl|BSEQ0010176|NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial (NDUFV2)
ATGTTCTTCTCCGCGGCGCTCCGGGCCCGGGCGGCTGGCCTCACCGCCCACTGGGGAAGA
CATGTAAGGAATTTGCATAAGACAGTTATGCAAAATGGAGCTGGAGGAGCTTTATTTGTG
CACAGAGATACTCCTGAGAATAACCCTGATACTCCATTTGATTTCACACCAGAAAACTAT
AAGAGGATAGAGGCAATTGTAAAAAACTATCCAGAAGGCCATAAAGCAGCAGCTGTTCTT
CCAGTCCTGGATTTAGCCCAAAGGCAGAATGGGTGGTTGCCCATCTCTGCTATGAACAAG
GTTGCAGAAGTTTTACAAGTACCTCCAATGAGAGTATATGAAGTAGCAACTTTTTATACA
ATGTATAATCGAAAGCCAGTTGGAAAGTATCACATTCAGGTCTGCACTACTACACCCTGC
ATGCTTCGAAACTCTGACAGCATACTGGAGGCCATTCAGAAAAAGCTTGGAATAAAGGTT
GGGGAGACTACACCTGACAAACTTTTCACTCTTATAGAAGTGGAATGTTTAGGGGCCTGT
GTGAACGCACCAATGGTTCAAATAAATGACAATTACTATGAGGATTTGACAGCTAAGGAT
ATTGAAGAAATTATTGATGAGCTCAAGGCTGGCAAAATCCCAAAACCAGGGCCAAGGAGT
GGACGCTTCTCTTGTGAGCCAGCTGGAGGTCTTACCTCTTTGACTGAACCACCCAAGGGA
CCTGGATTTGGTGTACAAGCAGGCCTTTAA
GenBank Gene IDM22538
GeneCard IDNot Available
GenAtlas IDNDUFV2
HGNC IDHGNC:7717
Chromosome Location18
Locus18p11.31-p11.2
References
  1. Pilkington SJ, Walker JE: Mitochondrial NADH-ubiquinone reductase: complementary DNA sequences of import precursors of the bovine and human 24-kDa subunit. Biochemistry. 1989 Apr 18;28(8):3257-64. 2500970
  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. 15489334
  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. 12611891
  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. 21269460
  5. Ogura M, Yamaki J, Homma MK, Homma Y: Mitochondrial c-Src regulates cell survival through phosphorylation of respiratory chain components. Biochem J. 2012 Oct 15;447(2):281-9. 22823520
  6. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
  7. 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. 25944712