NDUA2_MOUSE
ID NDUA2_MOUSE Reviewed; 99 AA.
AC Q9CQ75; Q9WUB2;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;
DE AltName: Full=Complex I-B8;
DE Short=CI-B8;
DE AltName: Full=NADH-ubiquinone oxidoreductase B8 subunit;
GN Name=Ndufa2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RX PubMed=10318868; DOI=10.1074/jbc.274.20.14429;
RA Murdock D.G., Boone B.E., Esposito L.A., Wallace D.C.;
RT "Up-regulation of nuclear and mitochondrial genes in the skeletal muscle of
RT mice lacking the heart/muscle isoform of the adenine nucleotide
RT translocator.";
RL J. Biol. Chem. 274:14429-14433(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 47-56 AND 76-98, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64 AND LYS-75, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed not to be
CC involved in catalysis. Complex I functions in the transfer of electrons
CC from NADH to the respiratory chain. The immediate electron acceptor for
CC the enzyme is believed to be ubiquinone.
CC {ECO:0000250|UniProtKB:O43678}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC {ECO:0000250|UniProtKB:O43678}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O43678}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43678}; Matrix side
CC {ECO:0000250|UniProtKB:O43678}.
CC -!- PTM: Acetylation of Lys-64 and Lys-75 is observed in liver mitochondria
CC from fasted mice but not from fed mice.
CC -!- SIMILARITY: Belongs to the complex I NDUFA2 subunit family.
CC {ECO:0000305}.
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DR EMBL; AF124786; AAD30475.1; -; mRNA.
DR EMBL; AK003608; BAB22887.1; -; mRNA.
DR EMBL; AK018732; BAB31375.1; -; mRNA.
DR EMBL; BC006815; AAH06815.1; -; mRNA.
DR CCDS; CCDS29161.1; -.
DR RefSeq; NP_035015.2; NM_010885.5.
DR PDB; 6G2J; EM; 3.30 A; S=1-99.
DR PDB; 6G72; EM; 3.90 A; S=1-99.
DR PDB; 6ZR2; EM; 3.10 A; S=1-99.
DR PDB; 6ZTQ; EM; 3.00 A; S=1-99.
DR PDB; 7AK5; EM; 3.17 A; S=1-99.
DR PDB; 7AK6; EM; 3.82 A; S=1-99.
DR PDB; 7B93; EM; 3.04 A; S=1-99.
DR PDB; 7PSA; EM; 3.40 A; S=1-99.
DR PDBsum; 6G2J; -.
DR PDBsum; 6G72; -.
DR PDBsum; 6ZR2; -.
DR PDBsum; 6ZTQ; -.
DR PDBsum; 7AK5; -.
DR PDBsum; 7AK6; -.
DR PDBsum; 7B93; -.
DR PDBsum; 7PSA; -.
DR AlphaFoldDB; Q9CQ75; -.
DR SMR; Q9CQ75; -.
DR BioGRID; 201716; 39.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q9CQ75; -.
DR IntAct; Q9CQ75; 6.
DR STRING; 10090.ENSMUSP00000014438; -.
DR iPTMnet; Q9CQ75; -.
DR PhosphoSitePlus; Q9CQ75; -.
DR EPD; Q9CQ75; -.
DR jPOST; Q9CQ75; -.
DR MaxQB; Q9CQ75; -.
DR PaxDb; Q9CQ75; -.
DR PeptideAtlas; Q9CQ75; -.
DR PRIDE; Q9CQ75; -.
DR ProteomicsDB; 286164; -.
DR Antibodypedia; 15357; 134 antibodies from 25 providers.
DR DNASU; 17991; -.
DR Ensembl; ENSMUST00000014438; ENSMUSP00000014438; ENSMUSG00000014294.
DR GeneID; 17991; -.
DR KEGG; mmu:17991; -.
DR UCSC; uc008eoj.2; mouse.
DR CTD; 4695; -.
DR MGI; MGI:1343103; Ndufa2.
DR VEuPathDB; HostDB:ENSMUSG00000014294; -.
DR eggNOG; KOG3446; Eukaryota.
DR GeneTree; ENSGT00390000006178; -.
DR HOGENOM; CLU_110897_0_0_1; -.
DR InParanoid; Q9CQ75; -.
DR OMA; FIEQQYV; -.
DR OrthoDB; 1633416at2759; -.
DR PhylomeDB; Q9CQ75; -.
DR TreeFam; TF300229; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 17991; 25 hits in 76 CRISPR screens.
DR ChiTaRS; Ndufa2; mouse.
DR PRO; PR:Q9CQ75; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9CQ75; protein.
DR Bgee; ENSMUSG00000014294; Expressed in aortic valve and 263 other tissues.
DR Genevisible; Q9CQ75; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; TAS:MGI.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR InterPro; IPR016464; NADH_Ub_cplx-1_asu_su-2.
DR InterPro; IPR007741; Ribosome/NADH_DH.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12878; PTHR12878; 1.
DR Pfam; PF05047; L51_S25_CI-B8; 1.
DR PIRSF; PIRSF005822; NDUA2; 1.
DR SMART; SM00916; L51_S25_CI-B8; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disulfide bond;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43678"
FT CHAIN 2..99
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 2"
FT /id="PRO_0000118790"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43678"
FT MOD_RES 64
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 64
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT DISULFID 24..58
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 12
FT /note="A -> T (in Ref. 1; AAD30475)"
FT /evidence="ECO:0000305"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 33..47
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 99 AA; 10916 MW; BB06EFCADD6E30EC CRC64;
MAAAAASRAV GAKLGLREIR VHLCQRSPGS QGVRDFIVQR YVELKKAHPN LPILIRECSE
VQPKLWARYA FGQEKTVSLN NLSADEVTRA MQNVLSGKA
