Reviewed, UniProtKB/Swiss-Prot Q91VD9 (NDUS1_MOUSE)

Names and origin

Protein names

Recommended name:
    NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
    EC=1.6.5.3
    EC=1.6.99.3
Alternative name(s):
    Complex I-75kD
      Short name=CI-75kD

Gene names

Name:

Ndufs1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	727 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized By similarity.
Catalytic activity	NADH + ubiquinone = NAD(+) + ubiquinol. NADH + acceptor = NAD(+) + reduced acceptor.
Cofactor	Binds 1 2Fe-2S cluster per subunit By similarity. Binds 2 4Fe-4S clusters per subunit By similarity.
Subunit structure	Complex I is composed of 45 different subunits By similarity.
Subcellular location	Mitochondrion inner membraneBy similarity. Note= Matrix and cytoplasmic side of the mitochondrial inner membrane By similarity.
Post-translational modification	Acetylation of Lys-84 is observed in liver mitochondria from fasted mice but not from fed mice.
Sequence similarities	Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	ATP metabolic process Inferred from sequence or structural similarity. Source: UniProtKB ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro apoptosis Inferred from sequence or structural similarity. Source: UniProtKB cellular respiration Inferred from sequence or structural similarity. Source: UniProtKB oxygen and reactive oxygen species metabolic process Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitochondrial membrane potential Inferred from sequence or structural similarity. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial intermembrane space Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial respiratory chain complex I Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 23	23	Mitochondrion By similarity
	Chain	24 – 727	704	NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial		PRO_0000019969
Regions
	Domain	30 – 108	79	2Fe-2S ferredoxin-type
Sites
	Metal binding	64	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	75	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	78	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	92	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	124	1	Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
	Metal binding	128	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	131	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	137	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	176	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	179	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	182	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	226	1	Iron-sulfur 3 (4Fe-4S) By similarity
Amino acid modifications
	Modified residue	84	1	N6-acetyllysine
Experimental info
	Sequence conflict	491	1	A → V in BAC29641. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q91VD9-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 10FD90BB715AEDEA	FASTA	727	79,749
	10 20 30 40 50 60 MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI 70 80 90 100 110 120 PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL 130 140 150 160 170 180 LANHPLDCPI CDQGGECDLQ DQSMMFGSDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT 190 200 210 220 230 240 RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NVIDICPVGA LTSKPYAFTA 250 260 270 280 290 300 RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ 310 320 330 340 350 360 RLTEPMVRNE KGLLTYTSWE DALSRVAGML QNFEGNAVAA IAGGLVDAEA LVALKDLLNK 370 380 390 400 410 420 VDSDNLCTEE IFPTEGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK 430 440 450 460 470 480 SWLHNDLKVA LIGSPVDLTY RYDHLGDSPK ILQDIASGRH SFCEVLKDAK KPMVVLGSSA 490 500 510 520 530 540 LQRDDGAAIL AAVSNMVQKI RVTTGVAAEW KVMNILHRIA SQVAALDLGY KPGVEAIRKN 550 560 570 580 590 600 PPKMLFLLGA DGGCITRQDL PKDCFIVYQG HHGDVGAPMA DVILPGAAYT EKSATYVNTE 610 620 630 640 650 660 GRAQQTKVAV TPPGLAREDW KIIRALSEIA GITLPYDTLD QVRNRLEEVS PNLVRYDDIE 670 680 690 700 710 720 ETNYFQQASE LAKLVNQEVL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA VEEPSIC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Vagina.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[3]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 77-84; 88-108; 185-212; 247-266; 277-289; 292-299; 312-325; 361-382; 409-417; 421-441; 451-467; 471-483; 502-511; 519-539; 544-557; 608-617; 625-643; 646-655; 674-702 AND 713-727, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[4]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 185-200, MASS SPECTROMETRY. Tissue: Hippocampus.
[5]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK036926 mRNA. Translation: BAC29641.1. BC006660 mRNA. Translation: AAH06660.1. BC015300 mRNA. Translation: AAH15300.1.
RefSeq	NP_663493.1.
UniGene	Mm.290791 Mm.392955
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q91VD9.
2-D gel databases
REPRODUCTION-2DPAGE	Q91VD9.
Genome annotation databases
Ensembl	ENSMUSG00000025968. Mus musculus. [Contig view]
GeneID	227197.
KEGG	mmu:227197.
Organism-specific databases
MGI	MGI:2443241. Ndufs1.
Phylogenomic databases
HOVERGEN	Q91VD9.
Gene expression databases
ArrayExpress	Q91VD9.
CleanEx	MM_NDUFS1.
GermOnline	ENSMUSG00000025968. Mus musculus.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR001041. Ferredoxin. IPR006656. Mopterin_OxRdtase. IPR000283. NADH_DHase_75KDa_su_CS. IPR010228. NADH_quinone_OxRdtase_G. IPR015405. NuoG_C. [Graphical view]
Pfam	PF09326. DUF1982. 1 hit. PF00111. Fer2. 1 hit. PF00384. Molybdopterin. 1 hit. [Graphical view]
TIGRFAMs	TIGR01973. NuoG. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS00641. COMPLEX1_75K_1. 1 hit. PS00642. COMPLEX1_75K_2. 1 hit. PS00643. COMPLEX1_75K_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	378510.
SOURCE	Search...

Entry information

Entry name

NDUS1_MOUSE

Accession

Primary (citable) accession number: Q91VD9
Secondary accession number(s): Q8BM16

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	December 1, 2001
Last modified:	November 25, 2008
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)