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Database: UniProt
Entry: P80269
LinkDB: P80269
Original site: P80269 
ID   NDUS8_SOLTU             Reviewed;         229 AA.
AC   P80269; Q43849; Q43850;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   13-FEB-2019, entry version 124.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;
DE            EC=1.6.99.3;
DE            EC=7.1.1.2;
DE   AltName: Full=Complex I-28.5kD;
DE            Short=CI-28.5kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 28.5 kDa subunit;
DE   Flags: Precursor;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
OC   Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELES TYKY1 AND TYKY2).
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   PubMed=9037104; DOI=10.1007/s004380050342;
RA   Schmidt-Bleek K., Heiser V., Thieck O., Brennicke A., Grohmann L.;
RT   "The 28.5-kDa iron-sulfur protein of mitochondrial complex I is
RT   encoded in the nucleus in plants.";
RL   Mol. Gen. Genet. 253:448-454(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44;
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [3]
RP   PROTEIN SEQUENCE OF 42-65, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Bintje; TISSUE=Tuber;
RX   PubMed=8294484;
RA   Herz U., Schroeder W., Liddell A., Leaver C.J., Brennicke A.,
RA   Grohmann L.;
RT   "Purification of the NADH:ubiquinone oxidoreductase (complex I) of the
RT   respiratory chain from the inner mitochondrial membrane of Solanum
RT   tuberosum.";
RL   J. Biol. Chem. 269:2263-2269(1994).
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). May donate electrons to ubiquinone.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4
CC         H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565,
CC         Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389,
CC         ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=7.1.1.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + H(+) + NADH = AH2 + NAD(+); Xref=Rhea:RHEA:11356,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.99.3;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Complex I is composed of about 45 different subunits.
CC       This is a component of the iron-sulfur (IP) fragment of the enzyme
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:8294484}; Peripheral membrane protein
CC       {ECO:0000305}; Matrix side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Lowest expression found in storage tissues of
CC       tubers. Higher expression in older leaves than younger ones.
CC       Highest expression found in flowers.
CC   -!- POLYMORPHISM: There are two alleles; TYKY1 (shown here) and TYKY2.
CC       {ECO:0000305|PubMed:9037104}.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally reported that TYKY1 and TYKY2 were two
CC       different genes. {ECO:0000305|PubMed:9037104}.
DR   EMBL; X84319; CAA59062.1; -; mRNA.
DR   EMBL; X84320; CAA59063.1; -; mRNA.
DR   PIR; S52385; S52385.
DR   PIR; S52386; S52386.
DR   RefSeq; NP_001275214.1; NM_001288285.1.
DR   UniGene; Stu.18061; -.
DR   UniGene; Stu.18573; -.
DR   ProteinModelPortal; P80269; -.
DR   SMR; P80269; -.
DR   STRING; 4113.PGSC0003DMT400084285; -.
DR   EnsemblPlants; PGSC0003DMT400084285; PGSC0003DMT400084285; PGSC0003DMG400033912.
DR   GeneID; 102589342; -.
DR   Gramene; PGSC0003DMT400084285; PGSC0003DMT400084285; PGSC0003DMG400033912.
DR   KEGG; sot:102589342; -.
DR   eggNOG; KOG3256; Eukaryota.
DR   eggNOG; COG1143; LUCA.
DR   InParanoid; P80269; -.
DR   KO; K03941; -.
DR   OMA; NNGDQWE; -.
DR   OrthoDB; 1283957at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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:0003954; F:NADH dehydrogenase activity; IEA:UniProtKB-EC.
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   4Fe-4S; Complete proteome; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW   Polymorphism; Reference proteome; Repeat; Respiratory chain;
KW   Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT       1     41       Mitochondrion.
FT                                {ECO:0000269|PubMed:8294484}.
FT   CHAIN        42    229       NADH dehydrogenase [ubiquinone] iron-
FT                                sulfur protein 8, mitochondrial.
FT                                /FTId=PRO_0000020017.
FT   DOMAIN      121    150       4Fe-4S ferredoxin-type 1.
FT   DOMAIN      160    189       4Fe-4S ferredoxin-type 2.
FT   METAL       130    130       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       133    133       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       136    136       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       140    140       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       169    169       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       172    172       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       175    175       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       179    179       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   VARIANT      23     26       HTIE -> QAWQ (in allele TYKY2).
FT   VARIANT      30     33       GYNR -> TPNG (in allele TYKY2).
FT   VARIANT      57     57       E -> R (in strain: cv. Bintje).
FT   VARIANT      62     62       E -> K (in strain: cv. Bintje).
FT   VARIANT      65     65       K -> T (in strain: cv. Bintje).
FT   VARIANT     121    121       R -> H (in allele TYKY2).
FT   VARIANT     216    216       T -> I (in allele TYKY2).
SQ   SEQUENCE   229 AA;  26378 MW;  D995415DBE064A93 CRC64;
     MAAILARKSL SALRSRQLVL AGHTIEGTNG YNRTLLGTRS FATKHSFSTD KDDEEREQLA
     KELSKDWNSV FERSINTLFL TEMVRGLMLT LKYFFEKKVT INYPFEKGPL SPRFRGEHAL
     RRYATGEERC IACKLCEAIC PAQAITIEAE EREDGSRRTT RYDIDMTKCI YCGFCQEACP
     VDAIVEGPNF EFATETHEEL LYDKEKLLEN GDRWETEIAE NLRSESLYR
//
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