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Protein

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

Gene

Ndufs1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized (By similarity).By similarity

Catalytic activityi

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).
NADH + acceptor = NAD+ + reduced acceptor.

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster per subunit.By similarity
  • [4Fe-4S] clusterBy similarityNote: Binds 2 [4Fe-4S] clusters per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi75 – 751Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi78 – 781Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi92 – 921Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi124 – 1241Iron-sulfur 2 (4Fe-4S); via pros nitrogenBy similarity
Metal bindingi128 – 1281Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi131 – 1311Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi137 – 1371Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi176 – 1761Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi179 – 1791Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi182 – 1821Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi226 – 2261Iron-sulfur 3 (4Fe-4S)By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD, Ubiquinone

Enzyme and pathway databases

ReactomeiREACT_278797. Respiratory electron transport.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
Alternative name(s):
Complex I-75kD
Short name:
CI-75kD
Gene namesi
Name:Ndufs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2443241. Ndufs1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial intermembrane space Source: UniProtKB
  • mitochondrial respiratory chain complex I Source: UniProtKB
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323MitochondrionBy similarityAdd
BLAST
Chaini24 – 727704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrialPRO_0000019969Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841N6-acetyllysine1 Publication
Modified residuei467 – 4671N6-acetyllysine1 Publication
Modified residuei499 – 4991N6-acetyllysine1 Publication
Modified residuei709 – 7091N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation of Lys-84 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ91VD9.
PaxDbiQ91VD9.
PRIDEiQ91VD9.

2D gel databases

REPRODUCTION-2DPAGEIPI00308882.
Q91VD9.

PTM databases

PhosphoSiteiQ91VD9.

Expressioni

Gene expression databases

BgeeiQ91VD9.
CleanExiMM_NDUFS1.
ExpressionAtlasiQ91VD9. baseline and differential.
GenevisibleiQ91VD9. MM.

Interactioni

Subunit structurei

Complex I is composed of 45 different subunits.By similarity

Protein-protein interaction databases

BioGridi230599. 3 interactions.
IntActiQ91VD9. 6 interactions.
MINTiMINT-1860504.
STRINGi10090.ENSMUSP00000027111.

Structurei

3D structure databases

ProteinModelPortaliQ91VD9.
SMRiQ91VD9. Positions 31-636.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 108792Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini245 – 301574Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the complex I 75 kDa subunit family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1034.
GeneTreeiENSGT00390000018768.
HOGENOMiHOG000031442.
HOVERGENiHBG003482.
InParanoidiQ91VD9.
KOiK03934.
OMAiFQGNDVA.
OrthoDBiEOG783MTP.
TreeFamiTF105756.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
IPR015405. NuoG_C.
[Graphical view]
PfamiPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTiSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR01973. NuoG. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00641. COMPLEX1_75K_1. 1 hit.
PS00642. COMPLEX1_75K_2. 1 hit.
PS00643. COMPLEX1_75K_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91VD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL
60 70 80 90 100
QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW
110 120 130 140 150
NILTNSEKSK KAREGVMEFL LANHPLDCPI CDQGGECDLQ DQSMMFGSDR
160 170 180 190 200
SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT RCIRFASEIA GVDDLGTTGR
210 220 230 240 250
GNDMQVGTYI EKMFMSELSG NVIDICPVGA LTSKPYAFTA RPWETRKTES
260 270 280 290 300
IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ
310 320 330 340 350
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QNFEGNAVAA IAGGLVDAEA
360 370 380 390 400
LVALKDLLNK VDSDNLCTEE IFPTEGAGTD LRSNYLLNTT IAGVEEADVV
410 420 430 440 450
LLVGTNPRFE APLFNARIRK SWLHNDLKVA LIGSPVDLTY RYDHLGDSPK
460 470 480 490 500
ILQDIASGRH SFCEVLKDAK KPMVVLGSSA LQRDDGAAIL VAVSNMVQKI
510 520 530 540 550
RVTTGVAAEW KVMNILHRIA SQVAALDLGY KPGVEAIRKN PPKMLFLLGA
560 570 580 590 600
DGGCITRQDL PKDCFIVYQG HHGDVGAPMA DVILPGAAYT EKSATYVNTE
610 620 630 640 650
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GITLPYDTLD QVRNRLEEVS
660 670 680 690 700
PNLVRYDDIE ETNYFQQASE LAKLVNQEVL ADPLVPPQLT IKDFYMTDSI
710 720
SRASQTMAKC VKAVTEGAQA VEEPSIC
Length:727
Mass (Da):79,777
Last modified:July 27, 2011 - v2
Checksum:i4A4B4BD6C330BB4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti491 – 4911V → A in AAH06660 (PubMed:15489334).Curated
Sequence conflicti491 – 4911V → A in AAH15300 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034597 mRNA. Translation: BAE20494.1.
AK036926 mRNA. Translation: BAC29641.1.
AK142711 mRNA. Translation: BAE25170.1.
AL645950 Genomic DNA. Translation: CAI24120.1.
CH466548 Genomic DNA. Translation: EDL00180.1.
CH466548 Genomic DNA. Translation: EDL00181.1.
CH466548 Genomic DNA. Translation: EDL00182.1.
CH466548 Genomic DNA. Translation: EDL00184.1.
BC006660 mRNA. Translation: AAH06660.1.
BC015300 mRNA. Translation: AAH15300.1.
CCDSiCCDS14996.1.
RefSeqiNP_001153510.1. NM_001160038.1.
NP_001153511.1. NM_001160039.1.
NP_001153512.1. NM_001160040.1.
NP_663493.2. NM_145518.2.
XP_006496015.1. XM_006495952.2.
UniGeneiMm.290791.

Genome annotation databases

EnsembliENSMUST00000027111; ENSMUSP00000027111; ENSMUSG00000025968.
ENSMUST00000168099; ENSMUSP00000126621; ENSMUSG00000025968.
GeneIDi227197.
KEGGimmu:227197.
UCSCiuc007bfu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034597 mRNA. Translation: BAE20494.1.
AK036926 mRNA. Translation: BAC29641.1.
AK142711 mRNA. Translation: BAE25170.1.
AL645950 Genomic DNA. Translation: CAI24120.1.
CH466548 Genomic DNA. Translation: EDL00180.1.
CH466548 Genomic DNA. Translation: EDL00181.1.
CH466548 Genomic DNA. Translation: EDL00182.1.
CH466548 Genomic DNA. Translation: EDL00184.1.
BC006660 mRNA. Translation: AAH06660.1.
BC015300 mRNA. Translation: AAH15300.1.
CCDSiCCDS14996.1.
RefSeqiNP_001153510.1. NM_001160038.1.
NP_001153511.1. NM_001160039.1.
NP_001153512.1. NM_001160040.1.
NP_663493.2. NM_145518.2.
XP_006496015.1. XM_006495952.2.
UniGeneiMm.290791.

3D structure databases

ProteinModelPortaliQ91VD9.
SMRiQ91VD9. Positions 31-636.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230599. 3 interactions.
IntActiQ91VD9. 6 interactions.
MINTiMINT-1860504.
STRINGi10090.ENSMUSP00000027111.

PTM databases

PhosphoSiteiQ91VD9.

2D gel databases

REPRODUCTION-2DPAGEIPI00308882.
Q91VD9.

Proteomic databases

MaxQBiQ91VD9.
PaxDbiQ91VD9.
PRIDEiQ91VD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027111; ENSMUSP00000027111; ENSMUSG00000025968.
ENSMUST00000168099; ENSMUSP00000126621; ENSMUSG00000025968.
GeneIDi227197.
KEGGimmu:227197.
UCSCiuc007bfu.2. mouse.

Organism-specific databases

CTDi4719.
MGIiMGI:2443241. Ndufs1.

Phylogenomic databases

eggNOGiCOG1034.
GeneTreeiENSGT00390000018768.
HOGENOMiHOG000031442.
HOVERGENiHBG003482.
InParanoidiQ91VD9.
KOiK03934.
OMAiFQGNDVA.
OrthoDBiEOG783MTP.
TreeFamiTF105756.

Enzyme and pathway databases

ReactomeiREACT_278797. Respiratory electron transport.

Miscellaneous databases

NextBioi378510.
PROiQ91VD9.
SOURCEiSearch...

Gene expression databases

BgeeiQ91VD9.
CleanExiMM_NDUFS1.
ExpressionAtlasiQ91VD9. baseline and differential.
GenevisibleiQ91VD9. MM.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
IPR015405. NuoG_C.
[Graphical view]
PfamiPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTiSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR01973. NuoG. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00641. COMPLEX1_75K_1. 1 hit.
PS00642. COMPLEX1_75K_2. 1 hit.
PS00643. COMPLEX1_75K_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    Tissue: Embryonic breast, Heart and Vagina.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Kidney.
  5. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 77-84; 88-108; 185-212; 247-266; 277-289; 292-299; 312-325; 361-382; 409-417; 421-441; 451-467; 471-483; 502-511; 519-539; 544-557; 608-617; 625-643; 646-655; 674-702 AND 713-727, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-467; LYS-499 AND LYS-709, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNDUS1_MOUSE
AccessioniPrimary (citable) accession number: Q91VD9
Secondary accession number(s): Q3UQ73, Q8BM16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.