Reviewed, UniProtKB/Swiss-Prot Q91YT0 (NDUV1_MOUSE)

Names and origin

Protein names

Recommended name:
    NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    EC=1.6.5.3
    EC=1.6.99.3
Alternative name(s):
    NADH-ubiquinone oxidoreductase 51 kDa subunit
    Complex I-51kD
      Short name=CI-51kD

Gene names

Name:

Ndufv1

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	464 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.
Catalytic activity	NADH + ubiquinone = NAD+ + ubiquinol. NADH + acceptor = NAD+ + reduced acceptor.
Cofactor	Binds 1 FMN Potential. Binds 1 4Fe-4S cluster Potential.
Subunit structure	Complex I is composed of 45 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme By similarity.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.
Sequence similarities	Belongs to the complex I 51 kDa subunit family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FMN binding Inferred from electronic annotation. Source: InterPro NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 20	20	Mitochondrion Ref.3
	Chain	21 – 464	444	NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial		PRO_0000019978
Regions
	Nucleotide binding	87 – 96	10	NAD(H) By similarity
	Nucleotide binding	199 – 247	49	FMN By similarity
Sites
	Metal binding	379	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	382	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	385	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	425	1	Iron-sulfur (4Fe-4S) Potential
Amino acid modifications
	Modified residue	81	1	N6-acetyllysine Ref.5
	Modified residue	104	1	N6-acetyllysine Ref.5
	Modified residue	375	1	N6-acetyllysine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q91YT0-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 611EAB1546D2A630	FASTA	464	50,834
	10 20 30 40 50 60 MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG 70 80 90 100 110 120 DWYKTKEILL KGPDWILGEM KTSGLRGRGG AGFPTGLKWS FMNKPSDGRP KYLVVNADEG 130 140 150 160 170 180 EPGTCKDREI MRHDPHKLVE GCLVGGRAMG ARAAYIYIRG EFYNEASNLQ VAIREAYEAG 190 200 210 220 230 240 LIGKNACGSD YDFDVFVVRG AGAYICGEET ALIESIEGKQ GKPRLKPPFP ADVGVFGCPT 250 260 270 280 290 300 TVANVETVAV SPTICRRGGT WFAGFGRERN SGTKLFNISG HVNHPCTVEE EMSVPLKELI 310 320 330 340 350 360 EKHAGGVTGG WDNLLAVIPG GSSTPLIPKS VCETVLMDFD ALVQAQTGLG TAAVIVMDRS 370 380 390 400 410 420 TDIVKAIARL IEFYKHESCG QCTPCREGVD WMNKVMARFV KGDARPAEID SLWEISKQIE 430 440 450 460 GHTICALGDG AAWPVQGLIR HFRPELEDRM QRFAQQHRAW QAAS

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.
[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]. Strain: FVB/N. Tissue: Kidney.
[3]	"Proteome analysis of mouse brain: two-dimensional electrophoresis profiles of tissue proteins during the course of aging." Tsugita A., Kawakami T., Uchida T., Sakai T., Kamo M., Matsui T., Watanabe Y., Morimasa T., Hosokawa K., Toda T. Electrophoresis 21:1853-1871(2000) [PubMed: 10870971] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-29. Strain: C57BL/6. Tissue: Brain.
[4]	Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 29-48; 72-81; 89-126; 138-147; 153-219; 258-267; 275-297; 303-329; 370-375; 387-394 AND 402-449, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and 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-81; LYS-104 AND LYS-375, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK075692 mRNA. Translation: BAC35893.1. BC014818 mRNA. Translation: AAH14818.1. BC041682 mRNA. Translation: AAH41682.1.
IPI	IPI00130460.
PIR	PC7078.
RefSeq	NP_598427.1.
UniGene	Mm.29842
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q91YT0.
Proteomic databases
PRIDE	Q91YT0.
Genome annotation databases
Ensembl	ENSMUSG00000037916. Mus musculus. [Contig view]
GeneID	17995.
KEGG	mmu:17995.
NMPDR	fig|10090.3.peg.4389.
Organism-specific databases
MGI	MGI:107851. Ndufv1.
Phylogenomic databases
HOVERGEN	Q91YT0.
OMA	Q91YT0. PCNVEEE.
Enzyme and pathway databases
BRENDA	1.6.5.3. 244. 1.6.99.3. 244.
Gene expression databases
Bgee	Q91YT0.
CleanEx	MM_NDUFV1.
GermOnline	ENSMUSG00000037916. Mus musculus.
Family and domain databases
InterPro	IPR001949. NADH-UbQ_OxRdtase_51KDa_CS. IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd. IPR011537. NADH-UbQ_OxRdtase_suF. IPR011538. NADH_UbQ_OxRdtase_51KDa_su. IPR019554. Soluble_ligand_bd. [Graphical view]
Pfam	PF01512. Complex1_51K. 1 hit. PF10589. NADH_4Fe-4S. 1 hit. PF10531. SLBB. 1 hit. [Graphical view]
TIGRFAMs	TIGR01959. nuoF_fam. 1 hit.
PROSITE	PS00644. COMPLEX1_51K_1. 1 hit. PS00645. COMPLEX1_51K_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	292979.
SOURCE	Search...

Entry information

Entry name

NDUV1_MOUSE

Accession

Primary (citable) accession number: Q91YT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	December 1, 2001
Last modified:	July 7, 2009
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)