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Q91VD9

- NDUS1_MOUSE

UniProt

Q91VD9 - NDUS1_MOUSE

Protein

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

Gene

Ndufs1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    Binds 1 2Fe-2S cluster per subunit.By similarity
    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

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
    2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    3. electron carrier activity Source: InterPro
    4. metal ion binding Source: UniProtKB-KW
    5. NADH dehydrogenase (ubiquinone) activity Source: RefGenome

    GO - Biological processi

    1. apoptotic mitochondrial changes Source: UniProtKB
    2. ATP metabolic process Source: UniProtKB
    3. ATP synthesis coupled electron transport Source: InterPro
    4. cellular respiration Source: UniProtKB
    5. reactive oxygen species metabolic process Source: UniProtKB
    6. regulation of mitochondrial membrane potential Source: UniProtKB

    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

    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: Chromosome 1

    Organism-specific databases

    MGIiMGI:2443241. Ndufs1.

    Subcellular locationi

    Mitochondrion inner membrane By similarity
    Note: Matrix and cytoplasmic side of the mitochondrial inner membrane.By similarity

    GO - Cellular componenti

    1. mitochondrial intermembrane space Source: UniProtKB
    2. mitochondrial respiratory chain complex I Source: UniProtKB
    3. mitochondrion Source: MGI

    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.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ91VD9.
    PaxDbiQ91VD9.
    PRIDEiQ91VD9.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00308882.
    Q91VD9.

    PTM databases

    PhosphoSiteiQ91VD9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ91VD9.
    BgeeiQ91VD9.
    CleanExiMM_NDUFS1.
    GenevestigatoriQ91VD9.

    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.
    InParanoidiQ3UQ73.
    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

    MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL    50
    QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW 100
    NILTNSEKSK KAREGVMEFL LANHPLDCPI CDQGGECDLQ DQSMMFGSDR 150
    SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT RCIRFASEIA GVDDLGTTGR 200
    GNDMQVGTYI EKMFMSELSG NVIDICPVGA LTSKPYAFTA RPWETRKTES 250
    IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ 300
    RLTEPMVRNE KGLLTYTSWE DALSRVAGML QNFEGNAVAA IAGGLVDAEA 350
    LVALKDLLNK VDSDNLCTEE IFPTEGAGTD LRSNYLLNTT IAGVEEADVV 400
    LLVGTNPRFE APLFNARIRK SWLHNDLKVA LIGSPVDLTY RYDHLGDSPK 450
    ILQDIASGRH SFCEVLKDAK KPMVVLGSSA LQRDDGAAIL VAVSNMVQKI 500
    RVTTGVAAEW KVMNILHRIA SQVAALDLGY KPGVEAIRKN PPKMLFLLGA 550
    DGGCITRQDL PKDCFIVYQG HHGDVGAPMA DVILPGAAYT EKSATYVNTE 600
    GRAQQTKVAV TPPGLAREDW KIIRALSEIA GITLPYDTLD QVRNRLEEVS 650
    PNLVRYDDIE ETNYFQQASE LAKLVNQEVL ADPLVPPQLT IKDFYMTDSI 700
    SRASQTMAKC VKAVTEGAQA VEEPSIC 727
    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:
    EMBL
    GenBank
    DDBJ
    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_006496014.1. XM_006495951.1.
    XP_006496015.1. XM_006495952.1.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14996.1.
    RefSeqi NP_001153510.1. NM_001160038.1.
    NP_001153511.1. NM_001160039.1.
    NP_001153512.1. NM_001160040.1.
    NP_663493.2. NM_145518.2.
    XP_006496014.1. XM_006495951.1.
    XP_006496015.1. XM_006495952.1.
    UniGenei Mm.290791.

    3D structure databases

    ProteinModelPortali Q91VD9.
    SMRi Q91VD9. Positions 31-636.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230599. 3 interactions.
    IntActi Q91VD9. 6 interactions.
    MINTi MINT-1860504.
    STRINGi 10090.ENSMUSP00000027111.

    PTM databases

    PhosphoSitei Q91VD9.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00308882.
    Q91VD9.

    Proteomic databases

    MaxQBi Q91VD9.
    PaxDbi Q91VD9.
    PRIDEi Q91VD9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027111 ; ENSMUSP00000027111 ; ENSMUSG00000025968 .
    ENSMUST00000168099 ; ENSMUSP00000126621 ; ENSMUSG00000025968 .
    GeneIDi 227197.
    KEGGi mmu:227197.
    UCSCi uc007bfu.2. mouse.

    Organism-specific databases

    CTDi 4719.
    MGIi MGI:2443241. Ndufs1.

    Phylogenomic databases

    eggNOGi COG1034.
    GeneTreei ENSGT00390000018768.
    HOGENOMi HOG000031442.
    HOVERGENi HBG003482.
    InParanoidi Q3UQ73.
    KOi K03934.
    OMAi FQGNDVA.
    OrthoDBi EOG783MTP.
    TreeFami TF105756.

    Miscellaneous databases

    NextBioi 378510.
    PROi Q91VD9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q91VD9.
    Bgeei Q91VD9.
    CleanExi MM_NDUFS1.
    Genevestigatori Q91VD9.

    Family and domain databases

    Gene3Di 3.10.20.30. 1 hit.
    InterProi IPR001041. 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 ]
    Pfami PF09326. DUF1982. 1 hit.
    PF00384. Molybdopterin. 1 hit.
    PF10588. NADH-G_4Fe-4S_3. 1 hit.
    [Graphical view ]
    SMARTi SM00929. NADH-G_4Fe-4S_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54292. SSF54292. 1 hit.
    TIGRFAMsi TIGR01973. NuoG. 1 hit.
    PROSITEi PS51085. 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 ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 118 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