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 02-OCT-2024, entry version 147. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4L; DE EC=7.1.1.2; DE AltName: Full=NADH dehydrogenase subunit 4L; GN Name=Mt-nd4l {ECO:0000312|RGD:620494}; Synonyms=Mtnd4l, 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) which catalyzes electron transfer from CC NADH through the respiratory chain, using ubiquinone as an electron CC acceptor. Part of the enzyme membrane arm which is embedded in the CC lipid bilayer and involved in proton translocation. CC {ECO:0000250|UniProtKB:P03901}. 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:P03901}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29092; CC Evidence={ECO:0000250|UniProtKB:P03901}; CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex CC I) which is composed of 45 different subunits. CC {ECO:0000250|UniProtKB:P03902}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P03902}; Multi-pass membrane protein CC {ECO:0000255}. 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 AlphaFoldDB; P05507; -. DR SMR; P05507; -. DR STRING; 10116.ENSRNOP00000042064; -. DR PaxDb; 10116-ENSRNOP00000042064; -. DR Ensembl; ENSRNOT00000044582.3; ENSRNOP00000042064.3; ENSRNOG00000031053.3. DR GeneID; 26200; -. DR KEGG; rno:26200; -. DR AGR; RGD:620494; -. DR CTD; 4539; -. DR RGD; 620494; Mt-nd4l. DR eggNOG; KOG4669; Eukaryota. DR GeneTree; ENSGT00390000004755; -. DR HOGENOM; CLU_182394_0_0_1; -. DR InParanoid; P05507; -. DR OMA; MYRSHLM; -. DR OrthoDB; 3030031at2759; -. DR PRO; PR:P05507; -. DR Proteomes; UP000002494; Mitochondrion. DR Bgee; ENSRNOG00000031053; Expressed in adult mammalian kidney and 18 other cell types or tissues. DR ExpressionAtlas; P05507; 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:0045271; C:respiratory chain complex I; ISS:UniProtKB. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR Gene3D; 1.10.287.3510; -; 1. DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K. DR InterPro; IPR039428; NUOK/Mnh_C1-like. DR PANTHER; PTHR11434:SF0; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4L; 1. DR PANTHER; PTHR11434; NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT ND4L; 1. DR Pfam; PF00420; Oxidored_q2; 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..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 //