ID   NDUS8_BOVIN             Reviewed;         212 AA.
AC   P42028; Q32KV7;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-NOV-2008, entry version 64.
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   AltName: Full=TYKY subunit;
DE   Flags: Precursor;
GN   Name=NDUFS8;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 37-59.
RC   TISSUE=Heart;
RX   MEDLINE=91175743; PubMed=1901022; DOI=10.1021/bi00225a032;
RA   Dupuis A., Skehel J.M., Walker J.E.;
RT   "A homologue of a nuclear-coded iron-sulfur protein subunit of bovine
RT   mitochondrial complex I is encoded in chloroplast genomes.";
RL   Biochemistry 30:2954-2960(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC   -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
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DR   EMBL; M58717; AAA30664.1; -; mRNA.
DR   EMBL; BC109906; AAI09907.1; -; mRNA.
DR   PIR; A38409; A38409.
DR   RefSeq; NP_777243.2; -.
DR   UniGene; Bt.5483; -.
DR   HSSP; P00198; 2FDN.
DR   Ensembl; ENSBTAG00000012072; Bos taurus.
DR   GeneID; 287027; -.
DR   KEGG; bta:287027; -.
DR   HOVERGEN; P42028; -.
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:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001450; 4Fe4S_Fe_S_bd.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_I.
DR   Pfam; PF00037; Fer4; 2.
DR   PRINTS; PR00353; 4FE4SFRDOXIN.
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     36       Mitochondrion.
FT   CHAIN        37    212       NADH dehydrogenase [ubiquinone] iron-
FT                                sulfur protein 8, mitochondrial.
FT                                /FTId=PRO_0000020011.
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).
FT   CONFLICT    129    129       T -> I (in Ref. 2; AAI09907).
SQ   SEQUENCE   212 AA;  23896 MW;  4D5F95E4C918FEF8 CRC64;
     MRCLTMPMLL RALAQAQAAR AGHASVRGLH SSAVAATYKY VNLREPSMDM KSVTDRAAQT
     LLWTELIRGL GMTLSYLFRE PATINYPFEK GPLSPRFRGE HALRRYPSGE ERCIACKLCE
     AVCPAQAITI EAEPRADGSR RTTRYDIDMT KCIYCGFCQE ACPVDAIVEG PNFEFSTETH
     EELLYNKEKL LNNGDKWEAE IAANIQADYL YR
//