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NU6M_RAT
ID   NU6M_RAT                Reviewed;         172 AA.
AC   P03926; Q9ZZM7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 4.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 6;
DE            EC=7.1.1.2 {ECO:0000250|UniProtKB:P03923};
DE   AltName: Full=NADH dehydrogenase subunit 6;
GN   Name=Mtnd6; Synonyms=mt-Nd6, Nd6;
OS   Rattus norvegicus (Rat).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Wistar;
RX   PubMed=2504926; DOI=10.1007/bf02602930;
RA   Gadaleta G., Pepe G., de Candia G., Quagliariello C., Sbisa E., Saccone C.;
RT   "The complete nucleotide sequence of the Rattus norvegicus mitochondrial
RT   genome: cryptic signals revealed by comparative analysis between
RT   vertebrates.";
RL   J. Mol. Evol. 28:497-516(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
RX   PubMed=6299885; DOI=10.1016/0378-1119(82)90036-1;
RA   Koike K., Kobayashi M., Yaginuma K., Taira M., Yoshida E., Imai M.;
RT   "Nucleotide sequence and evolution of the rat mitochondrial cytochrome b
RT   gene containing the ochre termination codon.";
RL   Gene 20:177-185(1982).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-172.
RX   PubMed=1383760; DOI=10.1016/0921-8734(92)90022-h;
RA   Gadaleta M.N., Rainaldi G., Lezza A.M., Milella F., Fracasso F.,
RA   Cantatore P.;
RT   "Mitochondrial DNA copy number and mitochondrial DNA deletion in adult and
RT   senescent rats.";
RL   Mutat. Res. 275:181-193(1992).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC       NADH through the respiratory chain, using ubiquinone as an electron
CC       acceptor. Essential for the catalytic activity and assembly of complex
CC       I. {ECO:0000250|UniProtKB:P03923}.
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         Evidence={ECO:0000250|UniProtKB:P03923};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits.
CC       {ECO:0000250|UniProtKB:P03924}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P03924}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family. {ECO:0000305}.
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DR   EMBL; X14848; CAA32965.1; -; Genomic_DNA.
DR   EMBL; AY172581; AAN77605.1; -; Genomic_DNA.
DR   EMBL; S46798; AAB23820.2; -; Genomic_DNA.
DR   PIR; S04758; DERTN6.
DR   RefSeq; AP_004903.1; AC_000022.2.
DR   RefSeq; YP_665640.1; NC_001665.2.
DR   AlphaFoldDB; P03926; -.
DR   SMR; P03926; -.
DR   STRING; 10116.ENSRNOP00000045645; -.
DR   PaxDb; P03926; -.
DR   Ensembl; ENSRNOT00000051268; ENSRNOP00000045645; ENSRNOG00000029042.
DR   GeneID; 26203; -.
DR   KEGG; rno:26203; -.
DR   CTD; 4541; -.
DR   RGD; 620561; mt-Nd6.
DR   eggNOG; ENOG502S2Q2; Eukaryota.
DR   GeneTree; ENSGT00390000003988; -.
DR   HOGENOM; CLU_129718_0_0_1; -.
DR   InParanoid; P03926; -.
DR   OMA; YLGGMMV; -.
DR   OrthoDB; 1438416at2759; -.
DR   Reactome; R-RNO-611105; Respiratory electron transport.
DR   Reactome; R-RNO-6799198; Complex I biogenesis.
DR   PRO; PR:P03926; -.
DR   Proteomes; UP000002494; Mitochondrion.
DR   Bgee; ENSRNOG00000029042; Expressed in cerebellum and 19 other tissues.
DR   ExpressionAtlas; P03926; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISO:RGD.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR   Gene3D; 1.20.120.1200; -; 1.
DR   InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR   InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR   Pfam; PF00499; Oxidored_q3; 1.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..172
FT                   /note="NADH-ubiquinone oxidoreductase chain 6"
FT                   /id="PRO_0000118326"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        30
FT                   /note="L -> F (in Ref. 1; CAA32965)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="L -> M (in Ref. 4; AAB23820)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   172 AA;  18923 MW;  BC0ACC4533BC285C CRC64;
     MTNYMFILSL LFLTGCLGLA LKPSPIYGGL GLIVSGCIGC LMVLGFGGSF LGLMVFLIYL
     GGMLVVFGYT TAMATEEYPE TWGSNWFIFS FFVLGLFMEL VVFYLFSLNN KVELVDFDSL
     GDWLMYEIDD VGVMLEGGIG VAAIYSCATW MMVVAGWSLF AGIFIIIEIT RD
 
 
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