O75489 (NDUS3_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	264 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	Mammalian complex I is composed of 45 different subunits. Interacts with NDUFAF3. Ref.9 Ref.10
Subcellular location	Mitochondrion inner membrane.
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
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	NAD Ubiquinone
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	induction of apoptosis Inferred from mutant phenotype PubMed 16826196. Source: UniProtKB mitochondrial electron transport, NADH to ubiquinone Non-traceable author statement Ref.1PubMed 9878551. Source: UniProtKB negative regulation of cell growth Inferred from mutant phenotype PubMed 16826196. Source: UniProtKB reactive oxygen species metabolic process Inferred from mutant phenotype PubMed 16826196. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	mitochondrial respiratory chain complex I Inferred from direct assay Ref.9PubMed 17209039. Source: UniProtKB
Molecular_function	NADH dehydrogenase (ubiquinone) activity Non-traceable author statement Ref.1PubMed 9878551. Source: UniProtKB electron carrier activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NDUFS2	O75306	5	EBI-1224896,EBI-1224806

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 36	36	Mitochondrion Ref.7
	Chain	37 – 264	228	NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial		PRO_0000019998
Natural variations
	Natural variant	249	1	P → Q. Corresponds to variant rs9600 [ dbSNP | Ensembl ].		VAR_012036
Experimental info
	Sequence conflict	1 – 7	7	MAAAAVA → MAAGRY Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O75489 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: C058D62779BEF17B	FASTA	264	30,242
	10 20 30 40 50 60 MAAAAVARLW WRGILGASAL TRGTGRPSVL LLPVRRESAG ADTRPTVRPR NDVAHKQLSA 70 80 90 100 110 120 FGEYVAEILP KYVQQVQVSC FNELEVCIHP DGVIPVLTFL RDHTNAQFKS LVDLTAVDVP 130 140 150 160 170 180 TRQNRFEIVY NLLSLRFNSR IRVKTYTDEL TPIESAVSVF KAANWYEREI WDMFGVFFAN 190 200 210 220 230 240 HPDLRRILTD YGFEGHPFRK DFPLSGYVEL RYDDEVKRVV AEPVELAQEF RKFDLNSPWE 250 260 AFPVYRQPPE SLKLEAGDKK PDAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed." Loeffen J., van den Heuvel L., Smeets R., Triepels R., Sengers R., Trijbels F., Smeitink J. Biochem. Biophys. Res. Commun. 247:751-758(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Human NDUFS3 gene coding for the 30-kDa subunit of mitochondrial Complex I: genomic organization and expression." Procaccio V., Lescuyer P., Bourges I., Beugnot R., Duborjal H., Depetris D., Mousson B., Montfort M.F., Smeets H., De Coo R., Issartel J.P. Mamm. Genome 11:808-810(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Skin.
[7]	"Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini." Xu G., Shin S.B., Jaffrey S.R. Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 37-51. Tissue: Leukemic T-cell.
[8]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 126-136 AND 187-199, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[9]	"The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification." Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F., Ghosh S.S., Capaldi R.A. J. Biol. Chem. 278:13619-13622(2003) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY, IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
[10]	"Mutations in NDUFAF3 (C3ORF60), encoding an NDUFAF4 (C6ORF66)-interacting complex I assembly protein, cause fatal neonatal mitochondrial disease." Saada A., Vogel R.O., Hoefs S.J., van den Brand M.A., Wessels H.J., Willems P.H., Venselaar H., Shaag A., Barghuti F., Reish O., Shohat M., Huynen M.A., Smeitink J.A.M., van den Heuvel L.P., Nijtmans L.G. Am. J. Hum. Genet. 84:718-727(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NDUFAF3.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF067139 mRNA. Translation: AAC27451.1. AF200954 Genomic DNA. Translation: AAG17541.1. AF100743 mRNA. Translation: AAD40386.1. AK313802 mRNA. Translation: BAG36538.1. CH471064 Genomic DNA. Translation: EAW67895.1. BC000617 mRNA. Translation: AAH00617.1.
IPI	IPI00025796.
PIR	JE0195.
RefSeq	NP_004542.1. NM_004551.2.
UniGene	Hs.502528.
3D structure databases
ProteinModelPortal	O75489.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75489. 18 interactions.
STRING	9606.ENSP00000263774.
PTM databases
PhosphoSite	O75489.
2D gel databases
REPRODUCTION-2DPAGE	IPI00025796. O75489.
Proteomic databases
PaxDb	O75489.
PeptideAtlas	O75489.
PRIDE	O75489.
Protocols and materials databases
DNASU	4722.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263774; ENSP00000263774; ENSG00000213619.
GeneID	4722.
KEGG	hsa:4722.
UCSC	uc001nft.3. human.
Organism-specific databases
CTD	4722.
GeneCards	GC11P047587.
HGNC	HGNC:7710. NDUFS3.
HPA	HPA004484.
MIM	603846. gene.
neXtProt	NX_O75489.
Orphanet	2609. Isolated NADH-CoQ reductase deficiency. 255241. Leigh syndrome with leukodystrophy.
PharmGKB	PA31520.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0852.
HOGENOM	HOG000009797.
HOVERGEN	HBG000450.
InParanoid	O75489.
KO	K03936.
OMA	QQVQVTC.
OrthoDB	EOG4VMFGB.
PhylomeDB	O75489.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	O75489.
Bgee	O75489.
CleanEx	HS_NDUFS3.
Genevestigator	O75489.
GermOnline	ENSG00000110536. Homo sapiens.
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
ChiTaRS	NDUFS3. human.
DrugBank	DB00157. NADH.
GenomeRNAi	4722.
NextBio	18210.
SOURCE	Search...

Entry information

Entry name

NDUS3_HUMAN

Accession

Primary (citable) accession number: O75489
Secondary accession number(s): B2R9J1, Q9UNQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.