NDUA4_MOUSE
ID NDUA4_MOUSE Reviewed; 82 AA.
AC Q62425; Q9CQP6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cytochrome c oxidase subunit NDUFA4;
GN Name=Ndufa4;
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=Cerebellum, and Small intestine;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-82, AND PROTEIN SEQUENCE OF 61-68.
RC STRAIN=C57BL/6J;
RX PubMed=9064319; DOI=10.1084/jem.184.3.1017;
RA Tallquist M.D., Yun T.J., Pease L.R.;
RT "A single T cell receptor recognizes structurally distinct MHC/peptide
RT complexes with high specificity.";
RL J. Exp. Med. 184:1017-1026(1996).
RN [4]
RP PROTEIN SEQUENCE OF 36-74, 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;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [7]
RP IDENTIFICATION AS CYTOCHROME C OXIDASE SUBUNIT.
RX PubMed=22902835; DOI=10.1016/j.cmet.2012.07.015;
RA Balsa E., Marco R., Perales-Clemente E., Szklarczyk R., Calvo E.,
RA Landazuri M.O., Enriquez J.A.;
RT "NDUFA4 is a subunit of complex IV of the mammalian electron transport
RT chain.";
RL Cell Metab. 16:378-386(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10, AND IDENTIFICATION BY MASS
RP 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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 61-68 IN COMPLEX WITH THE MAJOR
RP HISTOCOMPATIBILITY COMPLEX.
RX PubMed=11994422; DOI=10.1084/jem.20011644;
RA Luz J.G., Huang M., Garcia K.C., Rudolph M.G., Apostolopoulos V.,
RA Teyton L., Wilson I.A.;
RT "Structural comparison of allogeneic and syngeneic T cell receptor-peptide-
RT major histocompatibility complex complexes: a buried alloreactive mutation
RT subtly alters peptide presentation substantially increasing V(beta)
RT interactions.";
RL J. Exp. Med. 195:1175-1186(2002).
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules unsing 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. NDUFA4 is required for complex
CC IV maintenance. {ECO:0000250|UniProtKB:O00483}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A,
CC COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC are encoded in the nuclear genome. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (By similarity).
CC Interacts with RAB5IF (By similarity). {ECO:0000250|UniProtKB:O00483}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O00483}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O00483}.
CC -!- SIMILARITY: Belongs to the complex IV NDUFA4 subunit family.
CC {ECO:0000305}.
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DR EMBL; AK005084; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK008357; BAB25627.1; -; mRNA.
DR EMBL; AK008506; BAB25706.1; -; mRNA.
DR EMBL; AK076036; BAC36137.1; -; mRNA.
DR EMBL; BC011114; AAH11114.1; -; mRNA.
DR EMBL; U59509; AAB03395.1; -; mRNA.
DR CCDS; CCDS39427.1; -.
DR RefSeq; NP_035016.1; NM_010886.2.
DR PDB; 1LEG; X-ray; 1.75 A; P=61-68.
DR PDB; 1LEK; X-ray; 2.15 A; P=61-68.
DR PDB; 1MWA; X-ray; 2.40 A; P/Q=61-68.
DR PDB; 2CKB; X-ray; 3.00 A; P/Q=61-68.
DR PDBsum; 1LEG; -.
DR PDBsum; 1LEK; -.
DR PDBsum; 1MWA; -.
DR PDBsum; 2CKB; -.
DR AlphaFoldDB; Q62425; -.
DR SMR; Q62425; -.
DR BioGRID; 201717; 67.
DR CORUM; Q62425; -.
DR IntAct; Q62425; 9.
DR MINT; Q62425; -.
DR STRING; 10090.ENSMUSP00000031637; -.
DR iPTMnet; Q62425; -.
DR PhosphoSitePlus; Q62425; -.
DR EPD; Q62425; -.
DR jPOST; Q62425; -.
DR MaxQB; Q62425; -.
DR PaxDb; Q62425; -.
DR PeptideAtlas; Q62425; -.
DR PRIDE; Q62425; -.
DR ProteomicsDB; 286165; -.
DR TopDownProteomics; Q62425; -.
DR Antibodypedia; 56007; 150 antibodies from 27 providers.
DR DNASU; 17992; -.
DR Ensembl; ENSMUST00000204714; ENSMUSP00000145413; ENSMUSG00000029632.
DR Ensembl; ENSMUST00000204978; ENSMUSP00000144932; ENSMUSG00000029632.
DR GeneID; 17992; -.
DR KEGG; mmu:17992; -.
DR UCSC; uc009ayd.1; mouse.
DR CTD; 4697; -.
DR MGI; MGI:107686; Ndufa4.
DR VEuPathDB; HostDB:ENSMUSG00000029632; -.
DR eggNOG; ENOG502S65P; Eukaryota.
DR GeneTree; ENSGT00940000154268; -.
DR HOGENOM; CLU_181002_0_0_1; -.
DR InParanoid; Q62425; -.
DR OMA; QHKFYSP; -.
DR OrthoDB; 1552648at2759; -.
DR PhylomeDB; Q62425; -.
DR TreeFam; TF106383; -.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 17992; 6 hits in 70 CRISPR screens.
DR ChiTaRS; Ndufa4; mouse.
DR EvolutionaryTrace; Q62425; -.
DR PRO; PR:Q62425; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q62425; protein.
DR Bgee; ENSMUSG00000029632; Expressed in right kidney and 279 other tissues.
DR ExpressionAtlas; Q62425; baseline and differential.
DR Genevisible; Q62425; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA: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:0005751; C:mitochondrial respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:1904960; P:positive regulation of cytochrome-c oxidase activity; ISS:UniProtKB.
DR InterPro; IPR010530; B12D.
DR PANTHER; PTHR14256; PTHR14256; 1.
DR Pfam; PF06522; B12D; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..82
FT /note="Cytochrome c oxidase subunit NDUFA4"
FT /id="PRO_0000118822"
FT TOPO_DOM 1..14
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:O00483"
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00483"
FT TOPO_DOM 38..82
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:O00483"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 82 AA; 9327 MW; 6E29865845807C7B CRC64;
MLRQILGQAK KHPSLIPLFV FIGAGGTGAA LYVMRLALFN PDVSWDRKNN PEPWNKLGPN
EQYKFYSVNV DYSKLKKEGP DF
