NDUA8_MOUSE
ID NDUA8_MOUSE Reviewed; 172 AA.
AC Q9DCJ5; A2AL45;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;
DE AltName: Full=Complex I-19kD;
DE Short=CI-19kD;
DE AltName: Full=Complex I-PGIV;
DE Short=CI-PGIV;
DE AltName: Full=NADH-ubiquinone oxidoreductase 19 kDa subunit;
GN Name=Ndufa8;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 2-19; 42-47; 62-72; 115-127; 131-145 AND 146-162, AND
RP 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).
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:P51970}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC {ECO:0000250|UniProtKB:P51970}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P51970}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P51970}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:P51970}. Mitochondrion
CC {ECO:0000250|UniProtKB:P51970}.
CC -!- DOMAIN: Contains four C-X9-C motifs that are predicted to form a helix-
CC coil-helix structure, permitting the formation of intramolecular
CC disulfide bonds. {ECO:0000250|UniProtKB:P51970}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA8 subunit family.
CC {ECO:0000305}.
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DR EMBL; AK002744; BAB22322.1; -; mRNA.
DR EMBL; AL773525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012416; AAH12416.1; -; mRNA.
DR EMBL; BC024673; AAH24673.1; -; mRNA.
DR CCDS; CCDS15967.1; -.
DR RefSeq; NP_080979.1; NM_026703.2.
DR PDB; 6G2J; EM; 3.30 A; X=1-172.
DR PDB; 6G72; EM; 3.90 A; X=1-172.
DR PDB; 6ZR2; EM; 3.10 A; X=1-172.
DR PDB; 6ZTQ; EM; 3.00 A; X=1-172.
DR PDB; 7AK5; EM; 3.17 A; X=1-172.
DR PDB; 7AK6; EM; 3.82 A; X=1-172.
DR PDB; 7B93; EM; 3.04 A; X=1-172.
DR PDB; 7PSA; EM; 3.40 A; X=1-172.
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; Q9DCJ5; -.
DR SMR; Q9DCJ5; -.
DR BioGRID; 212827; 69.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q9DCJ5; -.
DR IntAct; Q9DCJ5; 7.
DR MINT; Q9DCJ5; -.
DR STRING; 10090.ENSMUSP00000065352; -.
DR iPTMnet; Q9DCJ5; -.
DR PhosphoSitePlus; Q9DCJ5; -.
DR SwissPalm; Q9DCJ5; -.
DR EPD; Q9DCJ5; -.
DR jPOST; Q9DCJ5; -.
DR MaxQB; Q9DCJ5; -.
DR PaxDb; Q9DCJ5; -.
DR PeptideAtlas; Q9DCJ5; -.
DR PRIDE; Q9DCJ5; -.
DR ProteomicsDB; 293641; -.
DR Antibodypedia; 30251; 227 antibodies from 30 providers.
DR DNASU; 68375; -.
DR Ensembl; ENSMUST00000070112; ENSMUSP00000065352; ENSMUSG00000026895.
DR GeneID; 68375; -.
DR KEGG; mmu:68375; -.
DR UCSC; uc008jlb.1; mouse.
DR CTD; 4702; -.
DR MGI; MGI:1915625; Ndufa8.
DR VEuPathDB; HostDB:ENSMUSG00000026895; -.
DR eggNOG; KOG3458; Eukaryota.
DR GeneTree; ENSGT00390000008938; -.
DR HOGENOM; CLU_081931_2_1_1; -.
DR InParanoid; Q9DCJ5; -.
DR OMA; DRPNKEF; -.
DR OrthoDB; 1526152at2759; -.
DR PhylomeDB; Q9DCJ5; -.
DR TreeFam; TF105633; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 68375; 18 hits in 72 CRISPR screens.
DR ChiTaRS; Ndufa8; mouse.
DR PRO; PR:Q9DCJ5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DCJ5; protein.
DR Bgee; ENSMUSG00000026895; Expressed in digastric muscle group and 256 other tissues.
DR Genevisible; Q9DCJ5; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; 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:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
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; IPR010625; CHCH.
DR InterPro; IPR016680; NDUFA8.
DR PANTHER; PTHR13344; PTHR13344; 1.
DR Pfam; PF06747; CHCH; 1.
DR PIRSF; PIRSF017016; NDUA8; 1.
DR PROSITE; PS51808; CHCH; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P42029"
FT CHAIN 2..172
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 8"
FT /id="PRO_0000118735"
FT DOMAIN 33..74
FT /note="CHCH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DOMAIN 75..118
FT /note="CHCH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 36..46
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 56..66
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 78..88
FT /note="Cx9C motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 100..110
FT /note="Cx9C motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 36..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 46..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 78..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 88..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:7B93"
FT HELIX 58..76
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6ZR2"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:7AK5"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 172 AA; 19992 MW; 7DF62AB86B5BF684 CRC64;
MPGIVELPTL EELKVEEVKV SSAVLKAAAH HYGAQCDKTN KEFMLCRWEE KDPRRCLKEG
KLVNGCALNF FRQIKSHCAE PFTEYWTCLD YSNMQLFRHC RQQQAKFDQC VLDKLGWVRP
DLGQLSKVTK VKTDRPLPEN PYHSRARPEP NPVIEGDLKP AKHGTRFFFW TV
