NU2M_RAT
ID NU2M_RAT Reviewed; 346 AA.
AC P11662;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000305};
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P03891};
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=mt-Nd2 {ECO:0000312|RGD:620556}; Synonyms=Nd2;
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 SEQUENCE REVISION.
RA Saccone C.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 321-346.
RC STRAIN=Donryu; TISSUE=Liver;
RX PubMed=6300770; DOI=10.1093/nar/11.6.1635;
RA Taira M., Yoshida E., Kobayashi M., Yaginuma K., Koike K.;
RT "Tumor-associated mutations of rat mitochondrial transfer RNA genes.";
RL Nucleic Acids Res. 11:1635-1643(1983).
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:P03891}.
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:P03891};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits. Interacts with TMEM242
CC (By similarity). {ECO:0000250|UniProtKB:P03891,
CC ECO:0000250|UniProtKB:P03892}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P03892}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR EMBL; X14848; CAA32955.1; -; Genomic_DNA.
DR EMBL; AY172581; AAN77595.1; -; Genomic_DNA.
DR EMBL; V00676; CAA24047.1; -; Genomic_DNA.
DR EMBL; V00677; CAA24049.1; -; Genomic_DNA.
DR EMBL; V00678; CAA24051.1; -; Genomic_DNA.
DR EMBL; V00679; CAA24053.1; -; Genomic_DNA.
DR PIR; S04748; S04748.
DR RefSeq; AP_004893.1; AC_000022.2.
DR RefSeq; YP_665630.1; NC_001665.2.
DR AlphaFoldDB; P11662; -.
DR SMR; P11662; -.
DR STRING; 10116.ENSRNOP00000043885; -.
DR PaxDb; P11662; -.
DR PRIDE; P11662; -.
DR Ensembl; ENSRNOT00000040993; ENSRNOP00000043885; ENSRNOG00000031033.
DR GeneID; 26194; -.
DR KEGG; rno:26194; -.
DR CTD; 4536; -.
DR RGD; 620556; mt-Nd2.
DR eggNOG; KOG4668; Eukaryota.
DR GeneTree; ENSGT00730000111348; -.
DR HOGENOM; CLU_007100_1_3_1; -.
DR InParanoid; P11662; -.
DR OMA; HFWVPEV; -.
DR OrthoDB; 1153818at2759; -.
DR PhylomeDB; P11662; -.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR Reactome; R-RNO-6799198; Complex I biogenesis.
DR PRO; PR:P11662; -.
DR Proteomes; UP000002494; Mitochondrion.
DR Bgee; ENSRNOG00000031033; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; P11662; baseline and differential.
DR Genevisible; P11662; 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:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
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:0072593; P:reactive oxygen species metabolic process; ISO:RGD.
DR InterPro; IPR010933; NADH_DH_su2_C.
DR InterPro; IPR003917; NADH_UbQ_OxRdtase_chain2.
DR InterPro; IPR001750; ND/Mrp_mem.
DR Pfam; PF06444; NADH_dehy_S2_C; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01436; NADHDHGNASE2.
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..346
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117633"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 7..28
FT /note="IIIYFTILMGPVITMSSSNLLL -> TIIYLTTFKGRLITTLSTNLPP (in
FT Ref. 1; CAA32955)"
FT /evidence="ECO:0000305"
FT CONFLICT 217..219
FT /note="ITL -> NYI (in Ref. 1; CAA32955)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="T -> A (in Ref. 1; CAA32955)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="M -> T (in Ref. 1; CAA32955)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="Missing (in Ref. 1; CAA32955)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 38653 MW; 2DD0FB68269A49D0 CRC64;
MNPITLIIIY FTILMGPVIT MSSSNLLLMW VGLEMSLLAI IPLLANKKSP RSTEAATKYF
LTQATASMII LLVIILNYKQ SGMWTLQQQT NNMLLNMMLI SLAMKLGLAP FHYWLPEVTQ
GIPLHIGLIL LTWQKIAPLS ILYQFYQLLN PTITTILAIS SVFVGAWGGL NQTQTRKIMA
YSSIAHMGWM TAILPYNPNL TLLNLTIYIL LTVPMFITLM TNSATTINTL SLAWNKTPMI
LTMTSIILLS LGGLPPLTGF LPKWAIISEL LKNNCSTLST LMAIMALLSL FFYTRLIYSM
SLTMFPTNNN SKMISHHHQN PKHNFILPTL TVLSTLTLPL SSQLIT
