Reviewed, UniProtKB/Swiss-Prot Q91WD5 (NDUS2_MOUSE)

Names and origin

Protein names

Recommended name:
    NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
    EC=1.6.5.3
    EC=1.6.99.3
Alternative name(s):
    NADH-ubiquinone oxidoreductase 49 kDa subunit
    Complex I-49kD
      Short name=CI-49kD

Gene names

Name:

Ndufs2

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	463 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 4Fe-4S cluster.
Subunit structure	Complex I is composed of 45 different subunits. Component of the iron-sulfur (IP) 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 49 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 Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW 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 NAD or NADH binding Inferred from electronic annotation. Source: InterPro 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 quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 33	33	Mitochondrion By similarity
	Chain	34 – 463	430	NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial		PRO_0000019982
Sites
	Metal binding	326	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	332	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	347	1	Iron-sulfur (4Fe-4S) Potential
Experimental info
	Sequence conflict	1	1	M → V in AAH03898. Ref.2
	Sequence conflict	2	1	A → R in BAE30656. Ref.1
	Sequence conflict	2	1	A → R in BAE31936. Ref.1
	Sequence conflict	81	1	T → A in BAE27028. Ref.1
	Sequence conflict	186	1	A → S in BAE27028. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q91WD5-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 989934D73F5C8D27	FASTA	463	52,626
	10 20 30 40 50 60 MAALRALRCL RGVGAPVLRP GSGIRLPSQP SRGARQWQPD IEWAEQFSGA VMYPSKETAH 70 80 90 100 110 120 WKPPPWNDVD ILKEKAVTNM TLNFGPQHPA AHGVLRLVLE LSGEMVRKCD PHIGLLHRGT 130 140 150 160 170 180 EKLIEYKTYL QALPYFDRLD YVSMMCNEQA YSIAVEKLLN IQPPPRAQWI RVLFGEITRI 190 200 210 220 230 240 LNHIMAVTTH ALDIGAMTPF FWMFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL 250 260 270 280 290 300 LDDIYEFSKN FSLRIDEVEE MLTNNRIWRN RTVDIGVVTA EDALNYGFSG VMLRGSGIQW 310 320 330 340 350 360 DLRKTQPYDV YDQVEFDVPI GSRGDCYDRY LCRVEEMRQS LRIIEQCLNK MPPGEIKVDD 370 380 390 400 410 420 AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI EAPKGEFGVY LVSDGSSRPY 430 440 450 460 RCKIKAPGFA HLAGLDKMSK GHMLADVVAI IGTQDIVFGE IDR

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: BALB/c and C57BL/6J. Tissue: Bone marrow.
[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: Mammary tumor and Salivary gland.
[3]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 57-73; 76-108; 128-138; 158-166; 172-179; 210-216; 255-266; 272-323; 373-421; 424-437 AND 441-463, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK078474 mRNA. Translation: BAC37293.1. AK146269 mRNA. Translation: BAE27028.1. AK150431 mRNA. Translation: BAE29554.1. AK151746 mRNA. Translation: BAE30656.1. AK153364 mRNA. Translation: BAE31936.1. AK165426 mRNA. Translation: BAE38181.1. BC003898 mRNA. Translation: AAH03898.1. Different initiation. BC016097 mRNA. Translation: AAH16097.1.
IPI	IPI00128023.
RefSeq	NP_694704.1.
UniGene	Mm.21669
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q91WD5.
Proteomic databases
PRIDE	Q91WD5.
Genome annotation databases
Ensembl	ENSMUSG00000013593. Mus musculus. [Contig view]
GeneID	226646.
KEGG	mmu:226646.
NMPDR	fig|10090.3.peg.1471.
Organism-specific databases
MGI	MGI:2385112. Ndufs2.
Phylogenomic databases
HOVERGEN	Q91WD5.
OMA	Q91WD5. MYEAVSG.
Enzyme and pathway databases
BRENDA	1.6.5.3. 244. 1.6.99.3. 244.
Gene expression databases
ArrayExpress	Q91WD5.
Bgee	Q91WD5.
CleanEx	MM_NDUFS2.
GermOnline	ENSMUSG00000013593. Mus musculus.
Family and domain databases
InterPro	IPR010219. NADH_DH_1_dsu. IPR001135. NADH_Q_OxRdtase_suD. IPR014029. NADH_UbQ_OxRdtase_su-49kDa_CS. [Graphical view]
Pfam	PF00346. Complex1_49kDa. 1 hit. [Graphical view]
TIGRFAMs	TIGR01962. NuoD. 1 hit.
PROSITE	PS00535. COMPLEX1_49K. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	378279.
SOURCE	Search...

Entry information

Entry name

NDUS2_MOUSE

Accession

Primary (citable) accession number: Q91WD5
Secondary accession number(s): Q3TNA8 , Q3U5Y9, Q3UJX7, Q99L23

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)