Reviewed, UniProtKB/Swiss-Prot Q5R4J8 (NDUS7_PONAB)

Names and origin

Protein names

Recommended name:
    NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
    EC=1.6.5.3
    EC=1.6.99.3
Alternative name(s):
    NADH-ubiquinone oxidoreductase 20 kDa subunit
    Complex I-20kD
      Short name=CI-20kD

Gene names

Name:

NDUFS7

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	213 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 1 4Fe-4S cluster Potential.
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	MitochondrionBy similarity.
Sequence similarities	Belongs to the complex I 20 kDa subunit family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	mitochondrial electron transport, NADH to ubiquinone Inferred from electronic annotation. Source: InterPro mitochondrial respiratory chain complex I assembly 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: InterPro NADH dehydrogenase (ubiquinone) 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 – 38	38	Mitochondrion By similarity
	Chain	39 – 213	175	NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial		PRO_0000020029
Sites
	Metal binding	88	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	89	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	153	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	183	1	Iron-sulfur (4Fe-4S) Potential
Experimental info
	Sequence conflict	10	1	R → C in ABH12165. Ref.1
	Sequence conflict	11 – 13	3	GFR → SFW in CAH93318. Ref.2
	Sequence conflict	28	1	R → Q in CAH93318. Ref.2
	Sequence conflict	71	1	V → I in CAH93318. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q5R4J8-1 [UniParc]. Last modified October 3, 2006. Version 2. Checksum: 68E416C908C54BCD	FASTA	213	23,539
	10 20 30 40 50 60 MAALSAPGLR GFRILGLRSS VGTAVQARGV HQSVATDGPS STQPALPKAR AVAPKPSSRG 70 80 90 100 110 120 EYVVAKLDDL VNWARRSSLW PMTFGLACCA VEMMHMAAPR YDMDRFGVVF RASPRQSDVM 130 140 150 160 170 180 IVAGTLTNKM APALRKVYDQ MPEPRYVVSM GSCANGGGYY HYSYSVVRGC DRIVPVDIYI 190 200 210 PGCPPTAEAL LYGILQLQRK IKRERRLQIW YRR

References

	« Hide 'large scale' referencesShow 'large scale' 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].
[2]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ885656 mRNA. Translation: ABH12165.1. CR861249 mRNA. Translation: CAH93318.1.
RefSeq	NP_001126953.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	100173971.
Phylogenomic databases
HOVERGEN	Q5R4J8.
Family and domain databases
InterPro	IPR006138. NADH_DHase_20kDa_su. IPR014406. NiFe_hyd_3_ssu/Q_oxred_NuoB. IPR006137. OxRdtase_q6. [Graphical view]
PANTHER	PTHR11995:SF2. NADH_DH_20kDa. 1 hit. PTHR11995. NiFe_hyd_3_ssu/Q_oxred_NuoB. 1 hit.
Pfam	PF01058. Oxidored_q6. 1 hit. [Graphical view]
TIGRFAMs	TIGR01957. nuoB_fam. 1 hit.
PROSITE	PS01150. COMPLEX1_20K. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NDUS7_PONAB

Accession

Primary (citable) accession number: Q5R4J8
Secondary accession number(s): Q0MQH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	October 3, 2006
Last modified:	November 25, 2008
This is version 26 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)