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Q91VD9

- NDUS1_MOUSE

UniProt

Q91VD9 - NDUS1_MOUSE

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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

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
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

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
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.1 Publication

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.
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.
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:
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 Q91VD9.
KOi K03934.
OMAi FQGNDVA.
OrthoDBi EOG783MTP.
TreeFami TF105756.

Miscellaneous databases

NextBioi 378510.
PROi Q91VD9.
SOURCEi Search...

Gene expression databases

Bgeei Q91VD9.
CleanExi MM_NDUFS1.
ExpressionAtlasi Q91VD9. baseline and differential.
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

« 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: October 29, 2014
This is version 119 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