Reviewed, UniProtKB/Swiss-Prot Q0MQI2 (NDUS8_GORGO)

Names and origin

Protein names

Recommended name:
    NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
    EC=1.6.5.3
    EC=1.6.99.3
Alternative name(s):
    NADH-ubiquinone oxidoreductase 23 kDa subunit
    Complex I-23kD
      Short name=CI-23kD

Gene names

Name:

NDUFS8

Organism

Gorilla gorilla gorilla (Lowland gorilla)

Taxonomic identifier

9595 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Gorilla

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 2 4Fe-4S clusters per subunit By similarity.
Subunit structure	Complex I is composed of 45 different subunits This is a component of the iron-sulfur (IP) fragment of the enzyme By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the complex I 23 kDa subunit family. Contains 2 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Mitochondrion
Domain	Repeat Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial respiratory chain complex I assembly Inferred from sequence or structural similarity. Source: UniProtKB response to oxidative stress Inferred from sequence or structural similarity. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial respiratory chain complex I Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro 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 – 34	34	Mitochondrion By similarity
	Chain	35 – 210	176	NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial		PRO_0000251874
Regions
	Domain	102 – 131	30	4Fe-4S ferredoxin-type 1
	Domain	141 – 170	30	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	111	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	114	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	117	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	121	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	150	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	153	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	156	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	160	1	Iron-sulfur 1 (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0MQI2-1 [UniParc]. Last modified September 19, 2006. Version 1. Checksum: 663FA09AF05D1CA9	FASTA	210	23,703
	10 20 30 40 50 60 MRCLTTPVLL RALAQAARAG PPGGRSLHSS AVAATYKYVN MQDPEMDMKS VTDRAARTLL 70 80 90 100 110 120 WTELFRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAI 130 140 150 160 170 180 CPAQAITIEA EPRADGSRRT TRYDIDMTKC IYCGFCQEAC PVDAIVEGPN FEFSTETHEE 190 200 210 LLYNKEKLLN NGDKWEAEIT ANIQADYLYR

References

[1]	"Adaptive selection of mitochondrial complex I subunits during primate radiation." Mishmar D., Ruiz-Pesini E., Mondragon-Palomino M., Procaccio V., Gaut B., Wallace D.C. Gene 378:11-18(2006) [PubMed: 16828987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ885652 mRNA. Translation: ABH12161.1.
3D structure databases
SMR	Q0MQI2. Positions 84-201.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q0MQI2.
OMA	IFKEPAT.
Enzyme and pathway databases
BRENDA	1.6.5.3. 299462. 1.6.99.3. 299462.
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR009051. Helical_ferredxn. IPR010226. NADH_quinone_OxRdtase_chainI. [Graphical view]
TIGRFAMs	TIGR01971. NuoI. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NDUS8_GORGO

Accession

Primary (citable) accession number: Q0MQI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	September 19, 2006
Last modified:	February 9, 2010
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)