CPLM-017263

Genbank Nucleotide ID

NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

Protein Synonyms/Alias

Complex I-23kD; CI-23kD; NADH-ubiquinone oxidoreductase 23 kDa subunit

Mus musculus (Mouse)

Position	Peptide	Type	References
41	ATYKYVNKKEQESEV	acetylation	[1, 2, 3]
42	TYKYVNKKEQESEVD	acetylation	[3, 4]
51	QESEVDMKSATDNAA	acetylation	[3, 5]

[1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
[2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
[3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
[5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]

Functional Description

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).

DOMAIN 104 133 4Fe-4S ferredoxin-type 1.
DOMAIN 143 172 4Fe-4S ferredoxin-type 2.
METAL 113 113 Iron-sulfur 1 (4Fe-4S) (By similarity).
METAL 116 116 Iron-sulfur 1 (4Fe-4S) (By similarity).
METAL 119 119 Iron-sulfur 1 (4Fe-4S) (By similarity).
METAL 123 123 Iron-sulfur 2 (4Fe-4S) (By similarity).
METAL 152 152 Iron-sulfur 2 (4Fe-4S) (By similarity).
METAL 155 155 Iron-sulfur 2 (4Fe-4S) (By similarity).
METAL 158 158 Iron-sulfur 2 (4Fe-4S) (By similarity).
METAL 162 162 Iron-sulfur 1 (4Fe-4S) (By similarity).

4Fe-4S; Complete proteome; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Reference proteome; Repeat; Respiratory chain; Transit peptide; Transport; Ubiquinone.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005747; C:mitochondrial respiratory chain complex I; IEA:Compara.
GO:0005739; C:mitochondrion; IDA:MGI.
GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO:0009055; F:electron carrier activity; IEA:InterPro.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:EC.
GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
GO:0032981; P:mitochondrial respiratory chain complex I assembly; IEA:Compara.
GO:0006979; P:response to oxidative stress; IEA:Compara.

IPR001450; 4Fe4S-bd_dom.
IPR017896; 4Fe4S_Fe-S-bd.
IPR017900; 4Fe4S_Fe_S_CS.
IPR012285; Fum_reductase_C.
IPR010226; NADH_quinone_OxRdtase_chainI.

PS00198; 4FE4S_FER_1
PS51379; 4FE4S_FER_2