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NU6M_CAEEL
ID   NU6M_CAEEL              Reviewed;         144 AA.
AC   P24885;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 6;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 6;
GN   Name=nduo-6 {ECO:0000312|WormBase:MTCE.3};
GN   Synonyms=nd6 {ECO:0000312|WormBase:MTCE.3};
GN   ORFNames=MTCE.3 {ECO:0000312|WormBase:MTCE.3};
OS   Caenorhabditis elegans.
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=1551572; DOI=10.1093/genetics/130.3.471;
RA   Okimoto R., Macfarlane J.L., Clary D.O., Wolstenholme D.R.;
RT   "The mitochondrial genomes of two nematodes, Caenorhabditis elegans and
RT   Ascaris suum.";
RL   Genetics 130:471-498(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-144, AND VARIANTS ILE-39; SER-81
RP   AND PHE-90.
RC   STRAIN=AB1, AB2, Bristol N2, CB4852, CB4853, CB4854, CB4855, CB4856,
RC   CB4857, CB4858, KR314, PB303, PB306, RW7000, and TR403;
RX   PubMed=12644560; DOI=10.1093/molbev/msg044;
RA   Denver D.R., Morris K., Thomas W.K.;
RT   "Phylogenetics in Caenorhabditis elegans: an analysis of divergence and
RT   outcrossing.";
RL   Mol. Biol. Evol. 20:393-400(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX   PubMed=2235493; DOI=10.1093/nar/18.20.6113;
RA   Okimoto R., Macfarlane J.L., Wolstenholme D.R.;
RT   "Evidence for the frequent use of TTG as the translation initiation codon
RT   of mitochondrial protein genes in the nematodes, Ascaris suum and
RT   Caenorhabditis elegans.";
RL   Nucleic Acids Res. 18:6113-6118(1990).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) that is believed to belong to the
CC       minimal assembly required for catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The immediate
CC       electron acceptor for the enzyme is believed to be ubiquinone (By
CC       similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family. {ECO:0000305}.
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DR   EMBL; X54252; CAA38153.1; -; Genomic_DNA.
DR   EMBL; AY171133; AAO16385.1; -; Genomic_DNA.
DR   EMBL; AY171134; AAO16388.1; -; Genomic_DNA.
DR   EMBL; AY171135; AAO16391.1; -; Genomic_DNA.
DR   EMBL; AY171136; AAO16394.1; -; Genomic_DNA.
DR   EMBL; AY171137; AAO16397.1; -; Genomic_DNA.
DR   EMBL; AY171138; AAO16400.1; -; Genomic_DNA.
DR   EMBL; AY171139; AAO16403.1; -; Genomic_DNA.
DR   EMBL; AY171140; AAO16406.1; -; Genomic_DNA.
DR   EMBL; AY171141; AAO16409.1; -; Genomic_DNA.
DR   EMBL; AY171142; AAO16412.1; -; Genomic_DNA.
DR   EMBL; AY171143; AAO16415.1; -; Genomic_DNA.
DR   EMBL; AY171144; AAO16418.1; -; Genomic_DNA.
DR   EMBL; AY171145; AAO16421.1; -; Genomic_DNA.
DR   EMBL; AY171146; AAO16424.1; -; Genomic_DNA.
DR   EMBL; AY171147; AAO16427.1; -; Genomic_DNA.
DR   PIR; S26026; S26026.
DR   RefSeq; NP_006953.1; NC_001328.1.
DR   AlphaFoldDB; P24885; -.
DR   SMR; P24885; -.
DR   IntAct; P24885; 1.
DR   STRING; 6239.MTCE.3; -.
DR   PaxDb; P24885; -.
DR   EnsemblMetazoa; MTCE.3.1; MTCE.3.1; WBGene00010957.
DR   GeneID; 2565699; -.
DR   KEGG; cel:ND6; -.
DR   CTD; 4541; -.
DR   WormBase; MTCE.3; CE34072; WBGene00010957; nduo-6.
DR   HOGENOM; CLU_1798189_0_0_1; -.
DR   InParanoid; P24885; -.
DR   OMA; SIDMDYS; -.
DR   PRO; PR:P24885; -.
DR   Proteomes; UP000001940; Mitochondrion.
DR   Bgee; WBGene00010957; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; NAD; Reference proteome;
KW   Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..144
FT                   /note="NADH-ubiquinone oxidoreductase chain 6"
FT                   /id="PRO_0000118257"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VARIANT         39
FT                   /note="V -> I (in strain: AB1, AB2, CB4852, CB4853, CB4855,
FT                   CB4857, CB4858, KR314 and PB306)"
FT                   /evidence="ECO:0000269|PubMed:12644560"
FT   VARIANT         81
FT                   /note="A -> S (in strain: CB4854)"
FT                   /evidence="ECO:0000269|PubMed:12644560"
FT   VARIANT         90
FT                   /note="L -> F (in strain: AB1, AB2, CB4852, CB4853, CB4855,
FT                   CB4857, CB4858, KR314 and PB306)"
FT                   /evidence="ECO:0000269|PubMed:12644560"
SQ   SEQUENCE   144 AA;  16788 MW;  04F51D0E354B40F9 CRC64;
     MVKVFFVLAV LSSIISYINI DPMKSSFFLI FSLLFSMPVI SMSMHIWFSY FICLLFLSGI
     FVILVYFSSL SKINVVKSYM AVFLLLLSML YFSPTVLTYS SYLGLSGFYY SIYWFIFCFI
     LVCLLFFMNF SSYFLNFSGA LRKV
 
 
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