NDUS8_MOUSE
ID NDUS8_MOUSE Reviewed; 212 AA.
AC Q8K3J1;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:O00217};
DE AltName: Full=Complex I-23kD;
DE Short=CI-23kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit;
DE Flags: Precursor;
GN Name=Ndufs8;
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 [GENOMIC DNA].
RA Lucas-Teixeira V.A., Marques S., Belo J.A.;
RT "Genomic organization of the mouse NDUFS8 gene encoding the NADH
RT dehydrogenase:ubiquinone Fe-S protein 8.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 19-37; 60-90 AND 118-135, 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 [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [5]
RP INTERACTION WITH RAB5IF.
RX PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL IScience 19:1114-1132(2019).
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 (By similarity). Essential for the catalytic activity and
CC assembly of complex I (By similarity). {ECO:0000250|UniProtKB:O00217}.
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:O00217};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q56224};
CC Note=Binds 2 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q56224};
CC -!- SUBUNIT: Complex I is composed of 45 different subunits (By
CC similarity). This is a component of the iron-sulfur (IP) fragment of
CC the enzyme (By similarity). Interacts with RAB5IF (PubMed:31536960).
CC {ECO:0000250|UniProtKB:P42028, ECO:0000269|PubMed:31536960}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P42028}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P42028}; Matrix side
CC {ECO:0000250|UniProtKB:P42028}.
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AY096002; AAM34451.1; -; Genomic_DNA.
DR CCDS; CCDS29402.1; -.
DR PIR; PC7079; PC7079.
DR RefSeq; NP_001258372.1; NM_001271443.1.
DR RefSeq; NP_001258373.1; NM_001271444.1.
DR RefSeq; NP_659119.2; NM_144870.5.
DR PDB; 6G2J; EM; 3.30 A; I=1-212.
DR PDB; 6G72; EM; 3.90 A; I=1-212.
DR PDB; 6ZR2; EM; 3.10 A; I=1-212.
DR PDB; 6ZTQ; EM; 3.00 A; I=1-212.
DR PDB; 7AK5; EM; 3.17 A; I=1-212.
DR PDB; 7AK6; EM; 3.82 A; I=1-212.
DR PDB; 7B93; EM; 3.04 A; I=1-212.
DR PDB; 7PSA; EM; 3.40 A; I=1-212.
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; Q8K3J1; -.
DR SMR; Q8K3J1; -.
DR BioGRID; 230440; 3.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q8K3J1; -.
DR IntAct; Q8K3J1; 4.
DR STRING; 10090.ENSMUSP00000074600; -.
DR iPTMnet; Q8K3J1; -.
DR PhosphoSitePlus; Q8K3J1; -.
DR SwissPalm; Q8K3J1; -.
DR REPRODUCTION-2DPAGE; Q8K3J1; -.
DR EPD; Q8K3J1; -.
DR jPOST; Q8K3J1; -.
DR MaxQB; Q8K3J1; -.
DR PaxDb; Q8K3J1; -.
DR PRIDE; Q8K3J1; -.
DR ProteomicsDB; 293648; -.
DR Antibodypedia; 1263; 269 antibodies from 34 providers.
DR DNASU; 225887; -.
DR Ensembl; ENSMUST00000075092; ENSMUSP00000074600; ENSMUSG00000059734.
DR Ensembl; ENSMUST00000235847; ENSMUSP00000158029; ENSMUSG00000059734.
DR Ensembl; ENSMUST00000236801; ENSMUSP00000158541; ENSMUSG00000059734.
DR Ensembl; ENSMUST00000237341; ENSMUSP00000158327; ENSMUSG00000059734.
DR GeneID; 225887; -.
DR KEGG; mmu:225887; -.
DR UCSC; uc008fxn.2; mouse.
DR CTD; 4728; -.
DR MGI; MGI:2385079; Ndufs8.
DR VEuPathDB; HostDB:ENSMUSG00000059734; -.
DR eggNOG; KOG3256; Eukaryota.
DR GeneTree; ENSGT00390000003049; -.
DR HOGENOM; CLU_067218_5_1_1; -.
DR InParanoid; Q8K3J1; -.
DR OMA; TIMYPYE; -.
DR OrthoDB; 1283957at2759; -.
DR PhylomeDB; Q8K3J1; -.
DR TreeFam; TF105610; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 225887; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Ndufs8; mouse.
DR PRO; PR:Q8K3J1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K3J1; protein.
DR Bgee; ENSMUSG00000059734; Expressed in interventricular septum and 242 other tissues.
DR ExpressionAtlas; Q8K3J1; baseline and differential.
DR Genevisible; Q8K3J1; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA: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:0009060; P:aerobic respiration; 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 GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR HAMAP; MF_01351; NDH1_NuoI; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR PANTHER; PTHR10849; PTHR10849; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR TIGRFAMs; TIGR01971; NuoI; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
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; Reference proteome;
KW Repeat; Respiratory chain; Transit peptide; Translocase; Transport;
KW Ubiquinone.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..212
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 8, mitochondrial"
FT /id="PRO_0000020014"
FT DOMAIN 104..133
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 143..172
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 116
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 155
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6G2J"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:7AK5"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 187..208
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 212 AA; 24038 MW; 1E06E024EA7829CD CRC64;
MYRLSSSMLP RALAQAMRTG HLNGQSLHSS AVAATYKYVN KKEQESEVDM KSATDNAARI
LMWTELIRGL GMTLSYLFRE PATINYPFEK GPLSPRFRGE HALRRYPSGE ERCIACKLCE
AICPAQAITI EAEPRADGSR RTTRYDIDMT KCIYCGFCQE ACPVDAIVEG PNFEFSTETH
EELLYNKEKL LNNGDKWEAE IAANIQADYL YR
