NU3M_RAT
ID NU3M_RAT Reviewed; 115 AA.
AC P05506;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 3 {ECO:0000305};
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P03897};
DE AltName: Full=NADH dehydrogenase subunit 3;
GN Name=mt-Nd3 {ECO:0000312|RGD:620557}; Synonyms=Nd3;
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. Essential for the catalytic activity of complex I.
CC {ECO:0000250|UniProtKB:P03897}.
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:P03897};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits. Interacts with TMEM186.
CC Interacts with TMEM242 (By similarity). {ECO:0000250|UniProtKB:P03897}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P03898}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the complex I subunit 3 family. {ECO:0000305}.
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DR EMBL; J01435; AAD15021.1; -; Genomic_DNA.
DR EMBL; X14848; CAA32961.1; -; Genomic_DNA.
DR EMBL; AY172581; AAN77601.1; -; Genomic_DNA.
DR PIR; S04754; S04754.
DR RefSeq; AP_004899.1; AC_000022.2.
DR RefSeq; YP_665636.1; NC_001665.2.
DR AlphaFoldDB; P05506; -.
DR SMR; P05506; -.
DR STRING; 10116.ENSRNOP00000039725; -.
DR CarbonylDB; P05506; -.
DR PhosphoSitePlus; P05506; -.
DR PaxDb; P05506; -.
DR PRIDE; P05506; -.
DR Ensembl; ENSRNOT00000041241; ENSRNOP00000039725; ENSRNOG00000033615.
DR GeneID; 26199; -.
DR KEGG; rno:26199; -.
DR CTD; 4537; -.
DR RGD; 620557; mt-Nd3.
DR eggNOG; KOG4662; Eukaryota.
DR GeneTree; ENSGT00390000011605; -.
DR HOGENOM; CLU_119549_3_1_1; -.
DR InParanoid; P05506; -.
DR OMA; RFPVKYY; -.
DR OrthoDB; 1605459at2759; -.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR Reactome; R-RNO-6799198; Complex I biogenesis.
DR PRO; PR:P05506; -.
DR Proteomes; UP000002494; Mitochondrion.
DR Bgee; ENSRNOG00000033615; Expressed in cerebellum and 19 other tissues.
DR ExpressionAtlas; P05506; baseline and differential.
DR Genevisible; P05506; RN.
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:0071385; P:cellular response to glucocorticoid stimulus; IDA:RGD.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR GO; GO:0009725; P:response to hormone; IMP:RGD.
DR GO; GO:0009642; P:response to light intensity; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
DR Gene3D; 1.20.58.1610; -; 1.
DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR PANTHER; PTHR11058; PTHR11058; 1.
DR Pfam; PF00507; Oxidored_q4; 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..115
FT /note="NADH-ubiquinone oxidoreductase chain 3"
FT /id="PRO_0000117818"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 4
FT /note="L -> P (in Ref. 2; CAA32961 and 1; AAD15021)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="T -> A (in Ref. 1; AAD15021)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> S (in Ref. 2; CAA32961)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="S -> A (in Ref. 2; CAA32961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 115 AA; 13087 MW; A09BBBDAD3787119 CRC64;
MNLLIIITIN ITLSFILISI AFWLPQMNLY SEKANPYECG FDPTSSARLP FSMKFFLVAI
TFLLFDLEIA LLLPLPWAIQ TTNTTTMMAT AFILVTILAL GLSYEWTQKG LEWTE
