NDUA6_ARATH
ID NDUA6_ARATH Reviewed; 133 AA.
AC Q9LHI0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;
GN OrderedLocusNames=At3g12260; ORFNames=F28J15.12, MQC3.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed to be not
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Complex I is composed of at least 49 different subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I LYR family. {ECO:0000305}.
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DR EMBL; AP002047; BAB03135.1; -; Genomic_DNA.
DR EMBL; AC069472; AAG51074.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75177.1; -; Genomic_DNA.
DR EMBL; AY054576; AAK96767.1; -; mRNA.
DR EMBL; AY064675; AAL47381.1; -; mRNA.
DR RefSeq; NP_566416.1; NM_112062.4.
DR PDB; 7A23; EM; 3.70 A; X=1-133.
DR PDB; 7A24; EM; 3.80 A; X=1-133.
DR PDB; 7AQR; EM; 2.91 A; W=1-133.
DR PDB; 7AR7; EM; 3.72 A; W=1-133.
DR PDB; 7AR8; EM; 3.53 A; W=1-133.
DR PDB; 7ARB; EM; 3.41 A; W=1-133.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQR; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; Q9LHI0; -.
DR SMR; Q9LHI0; -.
DR BioGRID; 5740; 1.
DR IntAct; Q9LHI0; 2.
DR STRING; 3702.AT3G12260.1; -.
DR TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; Q9LHI0; -.
DR PRIDE; Q9LHI0; -.
DR ProteomicsDB; 251102; -.
DR EnsemblPlants; AT3G12260.1; AT3G12260.1; AT3G12260.
DR GeneID; 820406; -.
DR Gramene; AT3G12260.1; AT3G12260.1; AT3G12260.
DR KEGG; ath:AT3G12260; -.
DR Araport; AT3G12260; -.
DR TAIR; locus:2082209; AT3G12260.
DR eggNOG; KOG3426; Eukaryota.
DR HOGENOM; CLU_111660_1_0_1; -.
DR InParanoid; Q9LHI0; -.
DR OMA; EICTLYA; -.
DR OrthoDB; 1518948at2759; -.
DR PhylomeDB; Q9LHI0; -.
DR BioCyc; ARA:AT3G12260-MON; -.
DR PRO; PR:Q9LHI0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHI0; baseline and differential.
DR Genevisible; Q9LHI0; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR CDD; cd20266; Complex1_LYR_NDUFA6_LYRM6; 1.
DR InterPro; IPR045299; Complex1_LYR_NDUFA6_LYRM6.
DR InterPro; IPR016488; NADH_Ub_cplx-1_asu_su-6.
DR PANTHER; PTHR12964; PTHR12964; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transport.
FT CHAIN 1..133
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 6"
FT /id="PRO_0000410929"
FT HELIX 19..35
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 72..90
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:7AQR"
SQ SEQUENCE 133 AA; 15082 MW; DA32DF850DED1819 CRC64;
MAAPFALRKI GVPPNSANLT EARRRVFDFF RAACRSIPTI MDIYNLQDVV APSQLRYAIS
AQIRNNAHIT DPKVIDLLIF KGMEELTDIV DHAKQRHHII GQYVVGEGLV QNTGNKDQGK
TDFLKNFYTS NYF