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Database: UniProt
Entry: Q22619
LinkDB: Q22619
Original site: Q22619 
ID   NDUS8_CAEEL             Reviewed;         212 AA.
AC   Q22619;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JAN-2019, entry version 150.
DE   RecName: Full=Probable 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-23kD;
DE            Short=CI-23kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit;
DE   Flags: Precursor;
GN   ORFNames=T20H4.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=10446229; DOI=10.1093/nar/27.17.3424;
RA   Hough R.F., Lingam A.T., Bass B.L.;
RT   "Caenorhabditis elegans mRNAs that encode a protein similar to ADARs
RT   derive from an operon containing six genes.";
RL   Nucleic Acids Res. 27:3424-3432(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
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). {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 45 different subunits This is a
CC       component of the iron-sulfur (IP) fragment of the enzyme.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC       {ECO:0000305}.
DR   EMBL; AF140272; AAD34863.1; -; mRNA.
DR   EMBL; FO081693; CCD73352.1; -; Genomic_DNA.
DR   PIR; T16914; T16914.
DR   RefSeq; NP_498595.1; NM_066194.4.
DR   UniGene; Cel.34232; -.
DR   ProteinModelPortal; Q22619; -.
DR   SMR; Q22619; -.
DR   BioGrid; 41235; 5.
DR   DIP; DIP-24953N; -.
DR   STRING; 6239.T20H4.5; -.
DR   EPD; Q22619; -.
DR   PaxDb; Q22619; -.
DR   PeptideAtlas; Q22619; -.
DR   PRIDE; Q22619; -.
DR   EnsemblMetazoa; T20H4.5; T20H4.5; WBGene00020636.
DR   GeneID; 176023; -.
DR   KEGG; cel:CELE_T20H4.5; -.
DR   UCSC; T20H4.5; c. elegans.
DR   CTD; 176023; -.
DR   WormBase; T20H4.5; CE00832; WBGene00020636; -.
DR   eggNOG; KOG3256; Eukaryota.
DR   eggNOG; COG1143; LUCA.
DR   GeneTree; ENSGT00390000003049; -.
DR   HOGENOM; HOG000228289; -.
DR   InParanoid; Q22619; -.
DR   KO; K03941; -.
DR   OMA; LCGLCIE; -.
DR   OrthoDB; 1283957at2759; -.
DR   PhylomeDB; Q22619; -.
DR   Reactome; R-CEL-6799198; Complex I biogenesis.
DR   PRO; PR:Q22619; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00020636; Expressed in 5 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:WormBase.
DR   GO; GO:0005739; C:mitochondrion; IDA:WormBase.
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   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:WormBase.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IBA:GO_Central.
DR   GO; GO:0042493; P:response to drug; IMP:WormBase.
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   2: Evidence at transcript level;
KW   4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW   Repeat; Respiratory chain; Transit peptide; Translocase; Transport;
KW   Ubiquinone.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000250}.
FT   CHAIN         ?    212       Probable NADH dehydrogenase [ubiquinone]
FT                                iron-sulfur protein 8, mitochondrial.
FT                                /FTId=PRO_0000020015.
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). {ECO:0000250}.
FT   METAL       116    116       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       119    119       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       123    123       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       152    152       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       155    155       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       158    158       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       162    162       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   212 AA;  23870 MW;  F50C413D89E80AB7 CRC64;
     MAMKSVAVLT KGMFGRIPAQ LAVSSVPSNT IQKRSNYKFV GMPNETDGTL AGDLNYGLHN
     VFFTELFRGF GVMLGHVFME PATINYPFEK GPLSSRFRGE HALRRYPSGE ERCIACKLCE
     AICPAQAITI EAETRPDGSR RTTRYDIDMT KCIYCGLCQE ACPVDAIVEG PNFEYSTETH
     EELLYNKEKL LLNGDRWEPE LASNLQAEYL YR
//
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