NDUA9_MOUSE
ID NDUA9_MOUSE Reviewed; 377 AA.
AC Q9DC69; Q6GTD3; Q99JP9;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;
DE AltName: Full=Complex I-39kD;
DE Short=CI-39kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 39 kDa subunit;
DE Flags: Precursor;
GN Name=Ndufa9;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 76-95; 118-132; 164-175; 193-209; 213-221; 238-286 AND
RP 304-316, AND IDENTIFICATION BY MASS 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-175, 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-189 AND LYS-370, AND
RP IDENTIFICATION 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).
RN [8]
RP INTERACTION WITH RAB5IF.
RX PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL IScience 19:1114-1132(2019).
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:Q16795}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Complex I is composed of 45 different subunits (By
CC similarity). This a component of the hydrophobic protein fraction (By
CC similarity). Interacts with BLOC1S1 (By similarity). Interacts with
CC SLC2A4 (By similarity). Interacts with CLOCK (By similarity). Interacts
CC with RAB5IF (PubMed:31536960). {ECO:0000250|UniProtKB:Q16795,
CC ECO:0000250|UniProtKB:Q5BK63, ECO:0000269|PubMed:31536960}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q16795}.
CC -!- PTM: Acetylated on lysine residues. BLOC1S1 is required for
CC acetylation. Acetylated by CLOCK in a circadian manner.
CC {ECO:0000250|UniProtKB:Q16795}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA9 subunit family.
CC {ECO:0000305}.
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DR EMBL; AK003137; BAB22596.1; -; mRNA.
DR EMBL; CH466523; EDK99844.1; -; Genomic_DNA.
DR EMBL; BC005760; AAH05760.1; -; mRNA.
DR EMBL; BC058378; AAH58378.1; -; mRNA.
DR CCDS; CCDS20557.1; -.
DR RefSeq; NP_079634.2; NM_025358.3.
DR PDB; 6G2J; EM; 3.30 A; P=1-377.
DR PDB; 6G72; EM; 3.90 A; P=1-377.
DR PDB; 6ZR2; EM; 3.10 A; P=1-377.
DR PDB; 6ZTQ; EM; 3.00 A; P=1-377.
DR PDB; 7AK5; EM; 3.17 A; P=1-377.
DR PDB; 7AK6; EM; 3.82 A; P=1-377.
DR PDB; 7B93; EM; 3.04 A; P=1-377.
DR PDB; 7PSA; EM; 3.40 A; P=1-377.
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; Q9DC69; -.
DR SMR; Q9DC69; -.
DR BioGRID; 211219; 33.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q9DC69; -.
DR IntAct; Q9DC69; 9.
DR MINT; Q9DC69; -.
DR STRING; 10090.ENSMUSP00000085523; -.
DR iPTMnet; Q9DC69; -.
DR PhosphoSitePlus; Q9DC69; -.
DR SwissPalm; Q9DC69; -.
DR EPD; Q9DC69; -.
DR jPOST; Q9DC69; -.
DR MaxQB; Q9DC69; -.
DR PaxDb; Q9DC69; -.
DR PeptideAtlas; Q9DC69; -.
DR PRIDE; Q9DC69; -.
DR ProteomicsDB; 253045; -.
DR TopDownProteomics; Q9DC69; -.
DR Antibodypedia; 22301; 261 antibodies from 29 providers.
DR DNASU; 66108; -.
DR Ensembl; ENSMUST00000205002; ENSMUSP00000144904; ENSMUSG00000000399.
DR GeneID; 66108; -.
DR KEGG; mmu:66108; -.
DR UCSC; uc009dve.2; mouse.
DR CTD; 4704; -.
DR MGI; MGI:1913358; Ndufa9.
DR VEuPathDB; HostDB:ENSMUSG00000000399; -.
DR eggNOG; KOG2865; Eukaryota.
DR GeneTree; ENSGT00390000006865; -.
DR HOGENOM; CLU_007383_6_4_1; -.
DR InParanoid; Q9DC69; -.
DR OMA; FFNRFAA; -.
DR OrthoDB; 721605at2759; -.
DR PhylomeDB; Q9DC69; -.
DR TreeFam; TF105961; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 66108; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Ndufa9; mouse.
DR PRO; PR:Q9DC69; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9DC69; protein.
DR Bgee; ENSMUSG00000000399; Expressed in interventricular septum and 273 other tissues.
DR ExpressionAtlas; Q9DC69; baseline and differential.
DR Genevisible; Q9DC69; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0003954; F:NADH dehydrogenase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
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 GO; GO:1901006; P:ubiquinone-6 biosynthetic process; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW FAD; Flavoprotein; Mitochondrion; Reference proteome; Respiratory chain;
KW Transit peptide; Transport.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 36..377
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 9, mitochondrial"
FT /id="PRO_0000019993"
FT MOD_RES 175
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 189
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 370
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 100
FT /note="L -> P (in Ref. 1; BAB22596)"
FT /evidence="ECO:0000305"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:7AK5"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:6G2J"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6G2J"
FT HELIX 179..194
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:7B93"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 295..306
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 377 AA; 42525 MW; 473FA5F2F018AC78 CRC64;
MAAAVRFRVV RALPMSRPAI TAAATSVFCG SSHRQLHHAV IPHGKGGRSS VSGVVATVFG
ATGFLGRYVV NHLGRMGSQV IIPYRCDVYD IMHLRLMGDL GQLTFLEWDA RDKDSIRKAV
QHSNVVINLI GREWETRNFD FEDVFVNIPR AIAQASKEAG VERFIHVSHL NASMKSSSKS
LRSKAVGEKE VRSVFPEAII IRPSDIFGRE DRFLNHFANY RWFLAVPLVS LGFKTVKQPV
YVADVSKGIV NATKDPDAVG KTFAFTGPNR YLLFHLVKYI FGMTHRTFIP YPLPLFVYSW
IGKLFGLSPF EPWTTKDKVE RIHISDVMPT DLPGLEDLGV QPTPLELKSI EVLRRHRTYR
WLSSEIEETK PAKTVNY
