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 26-FEB-2020, entry version 131. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4L; DE EC=7.1.1.2; 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; 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=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 genes RT for the cytochrome oxidase subunits I, II and III, ATPase subunit 6, and RT 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., 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 [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., 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). 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:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the complex I subunit 4L family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PRIDE; 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; CLU_182394_0_0_1; -. DR InParanoid; P05507; -. DR KO; K03882; -. DR OMA; YRSHLMS; -. DR OrthoDB; 1538435at2759; -. DR PRO; PR:P05507; -. DR Proteomes; UP000002494; Mitochondrion. DR Bgee; ENSRNOG00000031053; Expressed in brain and 8 other tissues. DR ExpressionAtlas; P05507; baseline and differential. 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:0030964; C:NADH dehydrogenase complex; 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 InterPro; IPR039428; NUOK/Mnh_C1-like. DR PANTHER; PTHR11434; PTHR11434; 1. DR Pfam; PF00420; Oxidored_q2; 1. 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..98 FT /note="NADH-ubiquinone oxidoreductase chain 4L" FT /id="PRO_0000118483" FT TRANSMEM 2..22 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 26..46 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 59..79 FT /note="Helical" FT /evidence="ECO:0000255" FT CONFLICT 71 FT /note="A -> V (in Ref. 1; AAD15022)" FT /evidence="ECO:0000305" FT CONFLICT 85 FT /note="Y -> H (in Ref. 1; AAD15022)" FT /evidence="ECO:0000305" SQ SEQUENCE 98 AA; 10659 MW; A22AA1102426DF7E CRC64; MTSAFLNLTM AFTLSLLGTF MFRSHLMSTL LCLEGMMLSL FVMTSTSTLN SNSMISMTIP ITILVFAACE AAVGLALLVK ISNTYGTDYV QNLNLLQC //