NDUAC_ARATH
ID NDUAC_ARATH Reviewed; 159 AA.
AC Q9M9M9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;
GN OrderedLocusNames=At3g03100; ORFNames=T17B22.21;
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;
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 33-43.
RC TISSUE=Leaf, and Stem;
RX PubMed=11743114; DOI=10.1104/pp.010474;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M9M9-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the complex I NDUFA12 subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC012328; AAF26114.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73901.1; -; Genomic_DNA.
DR EMBL; AF370349; AAK44164.1; -; mRNA.
DR EMBL; AY062979; AAL34153.1; -; mRNA.
DR EMBL; AY087701; AAM65238.1; -; mRNA.
DR RefSeq; NP_566192.1; NM_111180.5. [Q9M9M9-1]
DR PDB; 7A23; EM; 3.70 A; U=1-159.
DR PDB; 7A24; EM; 3.80 A; U=1-159.
DR PDB; 7AQR; EM; 2.91 A; q=1-159.
DR PDB; 7AR7; EM; 3.72 A; q=48-110.
DR PDB; 7AR8; EM; 3.53 A; q=1-159.
DR PDB; 7ARB; EM; 3.41 A; q=1-159.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQR; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; Q9M9M9; -.
DR SMR; Q9M9M9; -.
DR BioGRID; 6437; 11.
DR IntAct; Q9M9M9; 2.
DR STRING; 3702.AT3G03100.1; -.
DR TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR SwissPalm; Q9M9M9; -.
DR PaxDb; Q9M9M9; -.
DR PRIDE; Q9M9M9; -.
DR ProteomicsDB; 251132; -. [Q9M9M9-1]
DR DNASU; 821104; -.
DR EnsemblPlants; AT3G03100.1; AT3G03100.1; AT3G03100. [Q9M9M9-1]
DR GeneID; 821104; -.
DR Gramene; AT3G03100.1; AT3G03100.1; AT3G03100. [Q9M9M9-1]
DR KEGG; ath:AT3G03100; -.
DR Araport; AT3G03100; -.
DR TAIR; locus:2097765; AT3G03100.
DR eggNOG; KOG3382; Eukaryota.
DR HOGENOM; CLU_110455_0_0_1; -.
DR InParanoid; Q9M9M9; -.
DR PhylomeDB; Q9M9M9; -.
DR BioCyc; ARA:AT3G03100-MON; -.
DR BioCyc; MetaCyc:AT3G03100-MON; -.
DR PRO; PR:Q9M9M9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M9M9; baseline and differential.
DR Genevisible; Q9M9M9; 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; HDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR InterPro; IPR007763; NDUFA12.
DR PANTHER; PTHR12910; PTHR12910; 1.
DR Pfam; PF05071; NDUFA12; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transport.
FT CHAIN 1..159
FT /note="Probable NADH dehydrogenase [ubiquinone] 1 alpha
FT subcomplex subunit 12"
FT /id="PRO_0000118848"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:7ARB"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:7AQR"
SQ SEQUENCE 159 AA; 18317 MW; 29780059E9AA82DD CRC64;
MALTVAKSAL EAIREKGLGG FMRMIREEGF MRCLPDGNLL QTKIHNIGAT LVGVDKFGNK
YYQKLGDTQY GRHRWVEYAS KDRYNASQVP AEWHGWLHFI TDHTGDELLS LKPKRYGLEH
KENFSGEGDA YIYHSKGHTL NPGQKNWTRY QSWVPTKTQ