NDUS6_ARATH
ID NDUS6_ARATH Reviewed; 110 AA.
AC Q9M9M6; Q41901;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;
DE Flags: Precursor;
GN OrderedLocusNames=At3g03070; ORFNames=T17B22_24;
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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RA Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-22.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Complex I is composed of at least 49 different subunits. This
CC is a component of the iron-sulfur (IP) fragment of the enzyme.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250,
CC ECO:0000305|PubMed:25732537}; Peripheral membrane protein
CC {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I NDUFS6 subunit family.
CC {ECO:0000305}.
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DR EMBL; AC012328; AAF26117.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73898.1; -; Genomic_DNA.
DR EMBL; Z17587; CAA79002.1; -; mRNA.
DR EMBL; AF325039; AAG40391.1; -; mRNA.
DR EMBL; BT004574; AAO42820.1; -; mRNA.
DR EMBL; AK227975; BAE99941.1; -; mRNA.
DR EMBL; AY087471; AAM65015.1; -; mRNA.
DR RefSeq; NP_566191.1; NM_111177.4.
DR PDB; 7A23; EM; 3.70 A; P=1-110.
DR PDB; 7A24; EM; 3.80 A; P=1-110.
DR PDB; 7AQR; EM; 2.91 A; R=1-110.
DR PDB; 7AR7; EM; 3.72 A; R=48-109.
DR PDB; 7AR8; EM; 3.53 A; R=1-110.
DR PDB; 7ARB; EM; 3.41 A; R=1-110.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQR; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; Q9M9M6; -.
DR SMR; Q9M9M6; -.
DR BioGRID; 6466; 1.
DR STRING; 3702.AT3G03070.1; -.
DR TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; Q9M9M6; -.
DR PRIDE; Q9M9M6; -.
DR ProteomicsDB; 238791; -.
DR EnsemblPlants; AT3G03070.1; AT3G03070.1; AT3G03070.
DR GeneID; 821133; -.
DR Gramene; AT3G03070.1; AT3G03070.1; AT3G03070.
DR KEGG; ath:AT3G03070; -.
DR Araport; AT3G03070; -.
DR TAIR; locus:2097810; AT3G03070.
DR eggNOG; KOG3456; Eukaryota.
DR HOGENOM; CLU_083053_2_1_1; -.
DR InParanoid; Q9M9M6; -.
DR OMA; NEPAICK; -.
DR OrthoDB; 1641902at2759; -.
DR PhylomeDB; Q9M9M6; -.
DR PRO; PR:Q9M9M6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M9M6; baseline and differential.
DR Genevisible; Q9M9M6; AT.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR InterPro; IPR016668; NDUFS6.
DR InterPro; IPR019401; Znf_CHCC.
DR Pfam; PF10276; zf-CHCC; 1.
DR PIRSF; PIRSF016564; CI-13KD-A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transit peptide; Transport.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 23..110
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 6, mitochondrial"
FT /id="PRO_0000410794"
FT CONFLICT 64
FT /note="K -> R (in Ref. 3; CAA79002)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="E -> A (in Ref. 3; CAA79002)"
FT /evidence="ECO:0000305"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:7AQR"
SQ SEQUENCE 110 AA; 12234 MW; 8E81416C52B9C437 CRC64;
MASNLLKALI RSQILPSSRR NFSVATTQLG IPTDDLVGNH TAKWMQDRSK KSPMELISEV
PPIKVDGRIV ACEGDTNPAL GHPIEFICLD LNEPAICKYC GLRYVQDHHH
