NDUS7_MOUSE
ID NDUS7_MOUSE Reviewed; 224 AA.
AC Q9DC70;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:O75251};
DE AltName: Full=Complex I-20kD;
DE Short=CI-20kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 20 kDa subunit;
DE Flags: Precursor;
GN Name=Ndufs7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 78-86; 127-140 AND 157-179, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-41, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC NADH through the respiratory chain, using ubiquinone as an electron
CC acceptor. Essential for the catalytic activity of complex I.
CC {ECO:0000250|UniProtKB:O75251}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC Evidence={ECO:0000250|UniProtKB:O75251};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits (By similarity). This is
CC a component of the iron-sulfur (IP) fragment of the enzyme (By
CC similarity). {ECO:0000250|UniProtKB:P42026}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P42026}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P42026}; Matrix side
CC {ECO:0000250|UniProtKB:P42026}.
CC -!- PTM: Hydroxylated ar Arg-111 by NDUFAF5 early in the pathway of
CC assembly of complex I, before the formation of the juncture between
CC peripheral and membrane arms. {ECO:0000250|UniProtKB:O75251}.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AK003132; BAB22592.1; -; mRNA.
DR EMBL; BC013503; AAH13503.1; -; mRNA.
DR CCDS; CCDS24015.1; -.
DR RefSeq; NP_083548.1; NM_029272.3.
DR PDB; 6G2J; EM; 3.30 A; B=1-224.
DR PDB; 6G72; EM; 3.90 A; B=1-224.
DR PDB; 6ZR2; EM; 3.10 A; B=1-224.
DR PDB; 6ZTQ; EM; 3.00 A; B=1-224.
DR PDB; 7AK5; EM; 3.17 A; B=1-224.
DR PDB; 7AK6; EM; 3.82 A; B=1-224.
DR PDB; 7B93; EM; 3.04 A; B=1-224.
DR PDB; 7PSA; EM; 3.40 A; B=1-224.
DR PDBsum; 6G2J; -.
DR PDBsum; 6G72; -.
DR PDBsum; 6ZR2; -.
DR PDBsum; 6ZTQ; -.
DR PDBsum; 7AK5; -.
DR PDBsum; 7AK6; -.
DR PDBsum; 7B93; -.
DR PDBsum; 7PSA; -.
DR AlphaFoldDB; Q9DC70; -.
DR SMR; Q9DC70; -.
DR BioGRID; 217459; 75.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q9DC70; -.
DR IntAct; Q9DC70; 3.
DR STRING; 10090.ENSMUSP00000101003; -.
DR iPTMnet; Q9DC70; -.
DR PhosphoSitePlus; Q9DC70; -.
DR SwissPalm; Q9DC70; -.
DR EPD; Q9DC70; -.
DR jPOST; Q9DC70; -.
DR MaxQB; Q9DC70; -.
DR PaxDb; Q9DC70; -.
DR PeptideAtlas; Q9DC70; -.
DR PRIDE; Q9DC70; -.
DR ProteomicsDB; 287470; -.
DR Antibodypedia; 22663; 167 antibodies from 31 providers.
DR DNASU; 75406; -.
DR Ensembl; ENSMUST00000020361; ENSMUSP00000020361; ENSMUSG00000020153.
DR Ensembl; ENSMUST00000105364; ENSMUSP00000101003; ENSMUSG00000020153.
DR GeneID; 75406; -.
DR KEGG; mmu:75406; -.
DR UCSC; uc007gci.1; mouse.
DR CTD; 374291; -.
DR MGI; MGI:1922656; Ndufs7.
DR VEuPathDB; HostDB:ENSMUSG00000020153; -.
DR eggNOG; KOG1687; Eukaryota.
DR GeneTree; ENSGT00390000006565; -.
DR HOGENOM; CLU_055737_1_2_1; -.
DR InParanoid; Q9DC70; -.
DR OMA; AGWVRKS; -.
DR OrthoDB; 1278656at2759; -.
DR PhylomeDB; Q9DC70; -.
DR TreeFam; TF312859; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 75406; 16 hits in 71 CRISPR screens.
DR ChiTaRS; Ndufs7; mouse.
DR PRO; PR:Q9DC70; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9DC70; protein.
DR Bgee; ENSMUSG00000020153; Expressed in interventricular septum and 258 other tissues.
DR Genevisible; Q9DC70; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR GO; GO:0003954; F:NADH dehydrogenase activity; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR Pfam; PF01058; Oxidored_q6; 1.
DR TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR PROSITE; PS01150; COMPLEX1_20K; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transit peptide; Translocase;
KW Transport; Ubiquinone.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P42026"
FT CHAIN 36..224
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 7, mitochondrial"
FT /id="PRO_0000020028"
FT REGION 28..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT HELIX 71..88
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:7AK5"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6ZR2"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6ZR2"
FT HELIX 198..213
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 224 AA; 24683 MW; 234F3FF0ABC36A92 CRC64;
MAALAAPGLL SVRILGLRTA QVQLRRVHQS VATEGPSPSP SPSLSSTQSA VSKAGAGAVV
PKLSHLPRSR AEYVVTKLDD LINWARRSSL WPMTFGLACC AVEMMHMAAP RYDMDRFGVV
FRASPRQADV MIVAGTLTNK MAPALRKVYD QMPEPRYVVS MGSCANGGGY YHYSYSVVRG
CDRIVPVDIY VPGCPPTAEA LLYGILQLQR KIKREQKLKI WYRR
