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 16-JUN-2009, entry version 57. DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit; DE AltName: Full=Complex I-23kD; DE Short=CI-23kD; DE Flags: Precursor; GN Name=Ndufs8; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; 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 MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone = NAD(+) + ubiquinol. CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity). CC -!- SUBUNIT: Complex I is composed of 45 different subunits This is a CC component of the iron-sulfur (IP) fragment of the enzyme (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY096002; AAM34451.1; -; Genomic_DNA. DR IPI; IPI00170093; -. DR PIR; PC7079; PC7079. DR RefSeq; NP_659119.2; -. DR UniGene; Mm.44227; -. DR HSSP; P00198; 2FDN. DR PhosphoSite; Q8K3J1; -. DR REPRODUCTION-2DPAGE; Q8K3J1; -. DR PRIDE; Q8K3J1; -. DR Ensembl; ENSMUSG00000059734; Mus musculus. DR GeneID; 225887; -. DR KEGG; mmu:225887; -. DR NMPDR; fig|10090.3.peg.4372; -. DR MGI; MGI:2385079; Ndufs8. DR HOVERGEN; Q8K3J1; -. DR OMA; Q8K3J1; QADFLYR. DR BRENDA; 1.6.5.3; 244. DR BRENDA; 1.6.99.3; 244. DR NextBio; 377849; -. DR ArrayExpress; Q8K3J1; -. DR Bgee; Q8K3J1; -. DR CleanEx; MM_NDUFS8; -. DR GermOnline; ENSMUSG00000059734; Mus musculus. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:EC. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR001450; 4Fe4S_Fe_S_bd_subgr. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI. DR Pfam; PF00037; Fer4; 2. 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 4Fe-4S; Direct protein sequencing; Electron transport; Iron; KW Iron-sulfur; Metal-binding; Mitochondrion; NAD; Oxidoreductase; KW Repeat; Respiratory chain; Transit peptide; Transport; Ubiquinone. FT TRANSIT 1 34 Mitochondrion (By similarity). FT CHAIN 35 212 NADH dehydrogenase [ubiquinone] iron- FT sulfur protein 8, mitochondrial. FT /FTId=PRO_0000020014. FT DOMAIN 104 133 4Fe-4S ferredoxin-type 1. FT DOMAIN 143 172 4Fe-4S ferredoxin-type 2. FT METAL 113 113 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 116 116 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 119 119 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 123 123 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 152 152 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 155 155 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 158 158 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 162 162 Iron-sulfur 1 (4Fe-4S) (By similarity). 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 //