NU3M_ARATH
ID NU3M_ARATH Reviewed; 119 AA.
AC P92533; A7KNH1; Q2V2T5; Q8S878;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 3;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 3;
GN Name=ND3; Synonyms=NAD3; OrderedLocusNames=AtMg00990;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Mitochondrion.
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. C24;
RX PubMed=8988169; DOI=10.1038/ng0197-57;
RA Unseld M., Marienfeld J.R., Brandt P., Brennicke A.;
RT "The mitochondrial genome of Arabidopsis thaliana contains 57 genes in
RT 366,924 nucleotides.";
RL Nat. Genet. 15:57-61(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT2G07751).
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-108, AND RNA EDITING.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta; TISSUE=Rosette leaf;
RX PubMed=17565941; DOI=10.1534/genetics.107.073585;
RA Bentolila S., Elliott L.E., Hanson M.R.;
RT "Genetic architecture of mitochondrial editing in Arabidopsis thaliana.";
RL Genetics 178:1693-1708(2008).
RN [4]
RP RNA EDITING.
RX PubMed=10611383; DOI=10.1073/pnas.96.26.15324;
RA Giege P., Brennicke A.;
RT "RNA editing in Arabidopsis mitochondria effects 441 C to U changes in
RT ORFs.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15324-15329(1999).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) that is believed to belong to the
CC minimal assembly required for catalysis. Complex I functions in the
CC transfer of electrons from NADH to the respiratory chain. The immediate
CC electron acceptor for the enzyme is believed to be ubiquinone (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC -!- SUBUNIT: Complex I is composed of at least 49 different subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=3 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 9 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 28 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 50 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 71 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 84 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 85 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 116 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 118 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941};
CC -!- MISCELLANEOUS: A stretch of 270 kb of the mitochondrial genome is
CC duplicated within the centromere of chromosome 2 resulting in the
CC duplication of the gene. The expression of this duplicated gene
CC (At2g07751) is not demonstrated. It is also probably not RNA edited and
CC therefore differs in all the positions known to be edited.
CC -!- SIMILARITY: Belongs to the complex I subunit 3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM15514.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y08501; CAA69839.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007730; AAM15514.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EF488914; ABS50626.1; -; mRNA.
DR EMBL; EF488915; ABS50627.1; -; mRNA.
DR RefSeq; NP_085553.2; NC_001284.2.
DR PDB; 7A23; EM; 3.70 A; J=1-119.
DR PDB; 7A24; EM; 3.80 A; J=1-119.
DR PDB; 7AQQ; EM; 3.06 A; A=1-119.
DR PDB; 7AR7; EM; 3.72 A; A=1-119.
DR PDB; 7AR8; EM; 3.53 A; A=1-119.
DR PDB; 7ARB; EM; 3.41 A; A=1-119.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQQ; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; P92533; -.
DR SMR; P92533; -.
DR STRING; 3702.ATMG00990.1; -.
DR PeptideAtlas; P92533; -.
DR PRIDE; P92533; -.
DR Araport; ATMG00990; -.
DR eggNOG; KOG4662; Eukaryota.
DR InParanoid; P92533; -.
DR OrthoDB; 1605459at2759; -.
DR BioCyc; ARA:ATMG00990-MON; -.
DR PRO; PR:P92533; -.
DR Proteomes; UP000006548; Mitochondrion (cv. C24).
DR ExpressionAtlas; P92533; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR Gene3D; 1.20.58.1610; -; 1.
DR HAMAP; MF_01394; NDH1_NuoA; 1.
DR InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid.
DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR PANTHER; PTHR11058; PTHR11058; 1.
DR Pfam; PF00507; Oxidored_q4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion; NAD;
KW Reference proteome; Respiratory chain; RNA editing; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..119
FT /note="NADH-ubiquinone oxidoreductase chain 3"
FT /id="PRO_0000117707"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:7ARB"
FT HELIX 6..28
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 60..83
FT /evidence="ECO:0007829|PDB:7AQQ"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 92..112
FT /evidence="ECO:0007829|PDB:7AQQ"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:7AQQ"
SQ SEQUENCE 119 AA; 13935 MW; 0BD4C8F07C94B8F8 CRC64;
MMLEFAPIFI YLVISLLVSL ILLGVPFLFA SNSSTYPEKL SAYECGFDPF GDARSRFDIR
FYLVSILFLI FDLEVTFFFP WAVSLNKIDL FGFWSMMAFL FILTIGFLYE WKRGALDWE
