ID NU4LM_RAT Reviewed; 98 AA.
AC P05507;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 3.
DT 15-MAR-2017, entry version 115.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4L;
DE EC=1.6.5.3;
DE AltName: Full=NADH dehydrogenase subunit 4L;
GN Name=Mtnd4l; Synonyms=mt-Nd4l, Nd4l;
OS Rattus norvegicus (Rat).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=24185961; DOI=10.1007/BF00365694;
RA Grosskopf R., Feldmann H.;
RT "Analysis of a DNA segment from rat liver mitochondria containing the
RT genes for the cytochrome oxidase subunits I, II and III, ATPase
RT subunit 6, and several tRNA genes.";
RL Curr. Genet. 4:151-158(1981).
RN [2]
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.,
RA Saccone C.;
RT "The complete nucleotide sequence of the Rattus norvegicus
RT mitochondrial genome: cryptic signals revealed by comparative analysis
RT between vertebrates.";
RL J. Mol. Evol. 28:497-516(1989).
RN [3]
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.,
RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA 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.,
RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA 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.,
RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into
RT mammalian evolution.";
RL Nature 428:493-521(2004).
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: NADH + ubiquinone + 5 H(+)(In) = NAD(+) +
CC ubiquinol + 4 H(+)(Out).
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4L family.
CC {ECO:0000305}.
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DR EMBL; J01435; AAD15022.1; -; Genomic_DNA.
DR EMBL; X14848; CAA32962.1; -; Genomic_DNA.
DR EMBL; AY172581; AAN77602.1; -; Genomic_DNA.
DR PIR; S04755; S04755.
DR RefSeq; AP_004900.1; AC_000022.2.
DR RefSeq; YP_665637.1; NC_001665.2.
DR SMR; P05507; -.
DR STRING; 10116.ENSRNOP00000042064; -.
DR PaxDb; P05507; -.
DR Ensembl; ENSRNOT00000044582; ENSRNOP00000042064; ENSRNOG00000031053.
DR GeneID; 26200; -.
DR KEGG; rno:26200; -.
DR CTD; 4539; -.
DR RGD; 620494; mt-Nd4l.
DR eggNOG; KOG4669; Eukaryota.
DR eggNOG; COG0713; LUCA.
DR GeneTree; ENSGT00390000004755; -.
DR HOGENOM; HOG000113880; -.
DR HOVERGEN; HBG071122; -.
DR InParanoid; P05507; -.
DR KO; K03882; -.
DR OMA; MMLSLFI; -.
DR OrthoDB; EOG091G0ZRL; -.
DR PRO; PR:P05507; -.
DR Proteomes; UP000002494; Mitochondrion.
DR ExpressionAtlas; P05507; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K.
DR PANTHER; PTHR11434; PTHR11434; 1.
PE 3: Inferred from homology;
KW Complete proteome; Electron transport; Membrane; Mitochondrion; NAD;
KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1 98 NADH-ubiquinone oxidoreductase chain 4L.
FT /FTId=PRO_0000118483.
FT TRANSMEM 2 22 Helical. {ECO:0000255}.
FT TRANSMEM 26 46 Helical. {ECO:0000255}.
FT TRANSMEM 59 79 Helical. {ECO:0000255}.
FT CONFLICT 71 71 A -> V (in Ref. 1; AAD15022).
FT {ECO:0000305}.
FT CONFLICT 85 85 Y -> H (in Ref. 1; AAD15022).
FT {ECO:0000305}.
SQ SEQUENCE 98 AA; 10659 MW; A22AA1102426DF7E CRC64;
MTSAFLNLTM AFTLSLLGTF MFRSHLMSTL LCLEGMMLSL FVMTSTSTLN SNSMISMTIP
ITILVFAACE AAVGLALLVK ISNTYGTDYV QNLNLLQC
//