Q9DCT2 (NDUS3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
EC=1.6.5.3
EC=1.6.99.3

Alternative name(s):
Complex I-30kD
Short name=CI-30kD
NADH-ubiquinone oxidoreductase 30 kDa subunit

Gene names

Name:

Ndufs3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	263 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.
Subunit structure	Complex I is composed of 45 different subunits By similarity. Interacts with NDUFAF3 By similarity.
Subcellular location	Mitochondrion inner membrane By similarity. Note: Matrix and cytoplasmic side of the mitochondrial inner membrane By similarity.
Sequence similarities	Belongs to the complex I 30 kDa subunit family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	NAD Ubiquinone
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB reactive oxygen species metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrial respiratory chain complex I Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC NADH dehydrogenase activity 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 – 35	35	Mitochondrion By similarity
	Chain	36 – 263	228	NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial		PRO_0000019999
Experimental info
	Sequence conflict	20	1	G → D in BAB22149. Ref.1
	Sequence conflict	23	1	A → P in AAH27270. Ref.3
	Sequence conflict	49	1	R → W in AAH27270. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9DCT2 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 482F6C4D5E991B7F	FASTA	263	30,149
	10 20 30 40 50 60 MAAAAARVWC RGLLGAASVG RGAGRPSVLW QHVRRESAAA DKRPTVRPRS DVTHKQLSAF 70 80 90 100 110 120 GEYVAEILPK YVQQVQVSCL DELEICIHPD GVIPTLTFLR DHTNAQFKSL ADLTAVDVPT 130 140 150 160 170 180 RQNRFEIVYN LLSLRFNSRI RVKTYADELT PIDSIVSVHI AANWYEREVW DMFGVFFFNH 190 200 210 220 230 240 PDLRRILTDY GFEGHPFRKD FPLTGYVELR YDDEVKRVVA EPVELAQEFR KFDLNSPWEA 250 260 FPAYRQPPES LKLEAGDKKP ETK

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Kidney and Thymus.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 109-121; 125-135; 186-198; 200-210 AND 218-245, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK002501 mRNA. Translation: BAB22149.1. AK088337 mRNA. Translation: BAC40291.1. AL672241 Genomic DNA. Translation: CAM15313.1. BC027270 mRNA. Translation: AAH27270.1. BC119267 mRNA. Translation: AAI19268.1. BC119269 mRNA. Translation: AAI19270.1.
IPI	IPI00121309.
RefSeq	NP_080964.1. NM_026688.2.
UniGene	Mm.30113.
3D structure databases
ProteinModelPortal	Q9DCT2.
SMR	Q9DCT2. Positions 47-203.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32378N.
IntAct	Q9DCT2. 3 interactions.
PTM databases
PhosphoSite	Q9DCT2.
2D gel databases
World-2DPAGE	0004:Q9DCT2.
Proteomic databases
PaxDb	Q9DCT2.
PRIDE	Q9DCT2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005647; ENSMUSP00000005647; ENSMUSG00000005510.
GeneID	68349.
KEGG	mmu:68349.
UCSC	uc008ktr.1. mouse.
Organism-specific databases
CTD	4722.
MGI	MGI:1915599. Ndufs3.
Phylogenomic databases
eggNOG	COG0852.
GeneTree	ENSGT00390000017480.
HOGENOM	HOG000009797.
HOVERGEN	HBG000450.
InParanoid	Q9DCT2.
KO	K03936.
OMA	QQVQVTC.
OrthoDB	EOG4VMFGB.
Gene expression databases
Bgee	Q9DCT2.
CleanEx	MM_NDUFS3.
Genevestigator	Q9DCT2.
GermOnline	ENSMUSG00000005510. Mus musculus.
Family and domain databases
InterPro	IPR010218. NADH_DH_suC. IPR001268. NADH_UbQ_OxRdtase_30kDa_su. IPR020396. NADH_UbQ_OxRdtase_CS. [Graphical view]
Pfam	PF00329. Complex1_30kDa. 1 hit. [Graphical view]
ProDom	PD001581. NADH_UbQ_OxRdtase_30kDa_su. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01961. NuoC_fam. 1 hit.
PROSITE	PS00542. COMPLEX1_30K. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	327045.
SOURCE	Search...

Entry information

Entry name

NDUS3_MOUSE

Accession

Primary (citable) accession number: Q9DCT2
Secondary accession number(s): Q8BTZ3, Q8R073

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program