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   27-MAR-2024, entry version 160.
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,
RC   Pancreas, 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   PDB; 8OLT; EM; 2.84 A; B=1-224.
DR   PDB; 8OM1; EM; 2.39 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   PDBsum; 8OLT; -.
DR   PDBsum; 8OM1; -.
DR   AlphaFoldDB; Q9DC70; -.
DR   EMDB; EMD-16962; -.
DR   EMDB; EMD-16965; -.
DR   SMR; Q9DC70; -.
DR   BioGRID; 217459; 77.
DR   ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR   CORUM; Q9DC70; -.
DR   IntAct; Q9DC70; 3.
DR   STRING; 10090.ENSMUSP00000101003; -.
DR   GlyGen; Q9DC70; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9DC70; -.
DR   PhosphoSitePlus; Q9DC70; -.
DR   SwissPalm; Q9DC70; -.
DR   EPD; Q9DC70; -.
DR   jPOST; Q9DC70; -.
DR   MaxQB; Q9DC70; -.
DR   PaxDb; 10090-ENSMUSP00000101003; -.
DR   PeptideAtlas; Q9DC70; -.
DR   ProteomicsDB; 287470; -.
DR   Pumba; Q9DC70; -.
DR   Antibodypedia; 22663; 183 antibodies from 31 providers.
DR   DNASU; 75406; -.
DR   Ensembl; ENSMUST00000020361.7; ENSMUSP00000020361.7; ENSMUSG00000020153.15.
DR   Ensembl; ENSMUST00000105364.8; ENSMUSP00000101003.2; ENSMUSG00000020153.15.
DR   GeneID; 75406; -.
DR   KEGG; mmu:75406; -.
DR   UCSC; uc007gci.1; mouse.
DR   AGR; MGI:1922656; -.
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; GPYWQHG; -.
DR   OrthoDB; 33762at2759; -.
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 76 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 260 other cell types or tissues.
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: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: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; NAS:ComplexPortal.
DR   Gene3D; 3.40.50.12280; -; 1.
DR   HAMAP; MF_01356; NDH1_NuoB; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR   NCBIfam; TIGR01957; nuoB_fam; 1.
DR   PANTHER; PTHR11995; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR11995:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   SUPFAM; SSF56770; HydA/Nqo6-like; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
DR   Genevisible; Q9DC70; MM.
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           70..88
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:7AK5"
FT   HELIX           99..108
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           114..117
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            139..141
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           142..150
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           162..167
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           181..183
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          188..191
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           198..213
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           217..222
FT                   /evidence="ECO:0007829|PDB:8OM1"
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
//