NDUA5_MOUSE
ID NDUA5_MOUSE Reviewed; 116 AA.
AC Q9CPP6; Q9CY90; Q9D2P2; Q9D703; Q9D739;
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 5;
DE AltName: Full=Complex I subunit B13;
DE AltName: Full=Complex I-13kD-B;
DE Short=CI-13kD-B;
DE AltName: Full=NADH-ubiquinone oxidoreductase 13 kDa-B subunit;
GN Name=Ndufa5;
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=Embryo, Hippocampus, Small intestine, and Tongue;
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 gland;
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 PROTEIN SEQUENCE OF 8-30; 47-60 AND 67-86, 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 [4]
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 [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-98, 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-36; LYS-46 AND LYS-98, 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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24154540; DOI=10.1093/hmg/ddt526;
RA Peralta S., Torraco A., Wenz T., Garcia S., Diaz F., Moraes C.T.;
RT "Partial complex I deficiency due to the CNS conditional ablation of Ndufa5
RT results in a mild chronic encephalopathy but no increase in oxidative
RT damage.";
RL Hum. Mol. Genet. 23:1399-1412(2014).
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. {ECO:0000269|PubMed:24154540}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC {ECO:0000250|UniProtKB:Q16718}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q16718}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q16718}; Matrix side
CC {ECO:0000250|UniProtKB:Q16718}.
CC -!- PTM: Acetylation of Lys-98 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- DISRUPTION PHENOTYPE: Lethality around embryonic day 9 (E9).
CC Conditional knockout in the central nervous system does not lead to any
CC visible phenotype until mice reach 10-11 months of age: then mice
CC become lethargic, lose motor control and have difficulty maintaining
CC balance. Defects cause loss of other complex I subunits and reduced
CC NADH dehydrogenase activity. {ECO:0000269|PubMed:24154540}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA5 subunit family.
CC {ECO:0000305}.
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DR EMBL; AK008156; BAB25499.1; -; mRNA.
DR EMBL; AK008286; BAB25577.1; -; mRNA.
DR EMBL; AK008414; BAB25655.1; -; mRNA.
DR EMBL; AK009338; BAB26226.1; -; mRNA.
DR EMBL; AK009396; BAB26263.1; -; mRNA.
DR EMBL; AK009461; BAB26302.1; -; mRNA.
DR EMBL; AK009493; BAB26323.1; -; mRNA.
DR EMBL; AK009608; BAB26389.1; -; mRNA.
DR EMBL; AK009642; BAB26409.1; -; mRNA.
DR EMBL; AK009652; BAB26416.1; -; mRNA.
DR EMBL; AK009775; BAB26496.1; -; mRNA.
DR EMBL; AK009840; BAB26535.1; -; mRNA.
DR EMBL; AK009985; BAB26627.1; -; mRNA.
DR EMBL; AK010024; BAB26649.1; -; mRNA.
DR EMBL; AK010090; BAB26695.1; -; mRNA.
DR EMBL; AK010092; BAB26696.1; -; mRNA.
DR EMBL; AK011579; BAB27713.1; -; mRNA.
DR EMBL; AK011947; BAB27932.1; -; mRNA.
DR EMBL; AK019084; BAB31537.1; -; mRNA.
DR EMBL; AK019201; BAB31598.1; -; mRNA.
DR EMBL; AK019207; BAB31601.1; -; mRNA.
DR EMBL; AK019215; BAB31606.1; -; mRNA.
DR EMBL; AK019242; BAB31622.1; -; mRNA.
DR EMBL; AK019245; BAB31624.1; -; mRNA.
DR EMBL; AK019291; BAB31650.1; -; mRNA.
DR EMBL; AK019301; BAB31656.1; -; mRNA.
DR EMBL; AK019324; BAB31667.1; -; mRNA.
DR EMBL; AK019354; BAB31675.1; -; mRNA.
DR EMBL; AK019359; BAB31678.1; -; mRNA.
DR EMBL; AK019364; BAB31681.1; -; mRNA.
DR EMBL; AK019368; BAB31682.1; -; mRNA.
DR EMBL; BC028633; AAH28633.1; -; mRNA.
DR CCDS; CCDS19942.1; -.
DR RefSeq; NP_080890.1; NM_026614.2.
DR PDB; 6G2J; EM; 3.30 A; V=1-116.
DR PDB; 6G72; EM; 3.90 A; V=1-116.
DR PDB; 6ZR2; EM; 3.10 A; V=1-116.
DR PDB; 6ZTQ; EM; 3.00 A; V=1-116.
DR PDB; 7AK5; EM; 3.17 A; V=1-116.
DR PDB; 7AK6; EM; 3.82 A; V=1-116.
DR PDB; 7B93; EM; 3.04 A; V=1-116.
DR PDB; 7PSA; EM; 3.40 A; V=1-116.
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; Q9CPP6; -.
DR SMR; Q9CPP6; -.
DR BioGRID; 212725; 64.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q9CPP6; -.
DR IntAct; Q9CPP6; 5.
DR STRING; 10090.ENSMUSP00000023851; -.
DR iPTMnet; Q9CPP6; -.
DR PhosphoSitePlus; Q9CPP6; -.
DR SwissPalm; Q9CPP6; -.
DR EPD; Q9CPP6; -.
DR jPOST; Q9CPP6; -.
DR MaxQB; Q9CPP6; -.
DR PaxDb; Q9CPP6; -.
DR PeptideAtlas; Q9CPP6; -.
DR PRIDE; Q9CPP6; -.
DR ProteomicsDB; 293639; -.
DR Antibodypedia; 31753; 197 antibodies from 29 providers.
DR DNASU; 68202; -.
DR Ensembl; ENSMUST00000023851; ENSMUSP00000023851; ENSMUSG00000023089.
DR GeneID; 68202; -.
DR KEGG; mmu:68202; -.
DR UCSC; uc009bbs.1; mouse.
DR CTD; 4698; -.
DR MGI; MGI:1915452; Ndufa5.
DR VEuPathDB; HostDB:ENSMUSG00000023089; -.
DR eggNOG; KOG3365; Eukaryota.
DR GeneTree; ENSGT00390000008099; -.
DR HOGENOM; CLU_099943_2_0_1; -.
DR InParanoid; Q9CPP6; -.
DR OMA; VNEHPHR; -.
DR OrthoDB; 1372253at2759; -.
DR PhylomeDB; Q9CPP6; -.
DR TreeFam; TF313785; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR BioGRID-ORCS; 68202; 18 hits in 72 CRISPR screens.
DR ChiTaRS; Ndufa5; mouse.
DR PRO; PR:Q9CPP6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CPP6; protein.
DR Bgee; ENSMUSG00000023089; Expressed in aortic valve and 268 other tissues.
DR ExpressionAtlas; Q9CPP6; baseline and differential.
DR Genevisible; Q9CPP6; MM.
DR GO; GO:0005743; C:mitochondrial inner 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:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045271; C:respiratory chain complex I; IMP:MGI.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
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:0022904; P:respiratory electron transport chain; IMP:MGI.
DR InterPro; IPR006806; NDUFA5.
DR PANTHER; PTHR12653; PTHR12653; 1.
DR Pfam; PF04716; ETC_C1_NDUFA5; 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; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23935"
FT CHAIN 2..116
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 5"
FT /id="PRO_0000118633"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P23935"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16718"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16718"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63362"
FT MOD_RES 98
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 98
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 93
FT /note="K -> E (in Ref. 1; BAB31682)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="K -> E (in Ref. 1; BAB26496)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="E -> A (in Ref. 1; BAB31622)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="K -> N (in Ref. 1; BAB26409)"
FT /evidence="ECO:0000305"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:6ZR2"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 43..61
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 77..97
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6G2J"
SQ SEQUENCE 116 AA; 13360 MW; E673FE583D07C7D5 CRC64;
MAGLLKKTTG LVGLAVCDTP HERLTILYTK TLDILKHFPK HAAYRKYTEQ ITNEKLDMVK
AEPDVKKLEA LLQGGEVEEV ILQAEKELSL ARKMLKWKPW EPLVEEPPAN QWKWPI
