NU2M_ARATH
ID NU2M_ARATH Reviewed; 499 AA.
AC O05000; O04988; Q95621;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=ND2; Synonyms=NAD2; OrderedLocusNames=AtMg00285/AtMg01320;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=8737990; DOI=10.1515/bchm3.1996.377.4.251;
RA Lippok B., Brennicke A., Unseld M.;
RT "The rps4-gene is encoded upstream of the nad2-gene in Arabidopsis
RT mitochondria.";
RL Biol. Chem. Hoppe-Seyler 377:251-257(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT2G07733 AND AT2G07689).
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 [5]
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).
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 inner membrane; Multi-pass membrane
CC protein.
CC -!- RNA EDITING: Modified_positions=20 {ECO:0000269|PubMed:10611383}, 30
CC {ECO:0000269|PubMed:10611383}, 114 {ECO:0000269|PubMed:10611383}, 115
CC {ECO:0000269|PubMed:10611383}, 130 {ECO:0000269|PubMed:10611383}, 132
CC {ECO:0000269|PubMed:10611383}, 134 {ECO:0000269|PubMed:10611383}, 143
CC {ECO:0000269|PubMed:10611383}, 154 {ECO:0000269|PubMed:10611383}, 177
CC {ECO:0000269|PubMed:10611383}, 232 {ECO:0000269|PubMed:10611383}, 274
CC {ECO:0000269|PubMed:10611383}, 281 {ECO:0000269|PubMed:10611383}, 318
CC {ECO:0000269|PubMed:10611383}, 321 {ECO:0000269|PubMed:10611383}, 331
CC {ECO:0000269|PubMed:10611383}, 332 {ECO:0000269|PubMed:10611383}, 364
CC {ECO:0000269|PubMed:10611383}, 387 {ECO:0000269|PubMed:10611383}, 427
CC {ECO:0000269|PubMed:10611383}, 437 {ECO:0000269|PubMed:10611383}, 478
CC {ECO:0000269|PubMed:10611383}, 479 {ECO:0000269|PubMed:10611383}, 497
CC {ECO:0000269|PubMed:10611383};
CC -!- MISCELLANEOUS: Exons a and b (AtMg00285) and c, d and e (AtMg01320) are
CC cis-spliced, while a trans-splicing reaction is required to link exons
CC b and c.
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 (At2g07733 and At2g07689) is not demonstrated. It is also probably not
CC RNA edited and therefore differs in all the positions known to be
CC edited.
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; X96535; CAA65381.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X96536; CAA65381.1; JOINED; Genomic_DNA.
DR EMBL; Y08501; CAA69771.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S71136; S71136.
DR RefSeq; NP_085584.1; NC_001284.2.
DR PDB; 7A23; EM; 3.70 A; I=1-499.
DR PDB; 7A24; EM; 3.80 A; I=1-499.
DR PDB; 7AQQ; EM; 3.06 A; N=1-499.
DR PDB; 7AR7; EM; 3.72 A; N=12-499.
DR PDB; 7AR8; EM; 3.53 A; N=1-499.
DR PDB; 7ARB; EM; 3.41 A; N=1-499.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQQ; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; O05000; -.
DR SMR; O05000; -.
DR IntAct; O05000; 1.
DR STRING; 3702.ATMG00285.1; -.
DR PaxDb; O05000; -.
DR PeptideAtlas; O05000; -.
DR PRIDE; O05000; -.
DR Araport; ATMG00285; -.
DR Araport; ATMG01320; -.
DR eggNOG; KOG4668; Eukaryota.
DR InParanoid; O05000; -.
DR OrthoDB; 1153818at2759; -.
DR BioCyc; ARA:ATMG00285-MON; -.
DR BioCyc; ARA:ATMG01320-MON; -.
DR PRO; PR:O05000; -.
DR Proteomes; UP000006548; Chromosome 2.
DR Proteomes; UP000006548; Mitochondrion (cv. C24).
DR ExpressionAtlas; O05000; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IEA:UniProt.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR InterPro; IPR001750; ND/Mrp_mem.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Reference proteome; Respiratory chain;
KW RNA editing; Translocase; Transmembrane; Transmembrane helix; Transport;
KW Ubiquinone.
FT CHAIN 1..499
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117551"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 13..18
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 20..40
FT /evidence="ECO:0007829|PDB:7AQQ"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 51..71
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:7AQQ"
FT TURN 78..86
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 91..110
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 145..163
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 170..201
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 224..241
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 259..265
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 268..284
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 289..309
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 315..335
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 339..366
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 406..419
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 423..448
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 463..477
FT /evidence="ECO:0007829|PDB:7AQQ"
FT TURN 478..481
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 484..496
FT /evidence="ECO:0007829|PDB:7AQQ"
SQ SEQUENCE 499 AA; 55450 MW; FA5626F0930069BB CRC64;
MKAEFVRILP HMFNLFLAVF PEIFIINATF ILLIHGVVFS TSKKYDYPPL ASNVGWLGLL
SVLITLLLLA AGAPLLTIAH LFWNNLFRRD NFTYFCQIFL LLSTAGTISM CFDFFDQERF
DAFEFIVLIL LSTCGMLFMI SAYDLIAMYL AIELQSLCFY VIAASKRKSE FSTEAGLKYL
ILGAFSSGIL LFGCSMIYGS TGATHFDQLA KILTGYEITG ARSSGIFMGI LFIAVGFLFK
ITAVPFHMWA PDIYEGSPTP VTAFLSIAPK ISIFANILRV FIYGSYGATL QQIFFFCSIA
SMILGALAAM AQTKVKRLLA YSSIGHVGYI CIGFSCGTIE GIQSLLIGIF IYALMTMDAF
AIVLALRQTR VKYIADLGAL AKTNPILAIT FSITMFSYAG IPPLAGFCSK FYLFFAALGC
GAYFLALVGV VTSVIGCFYY IRLVKRMFFD TPRTWILYEP MDRNKSLLLA MTSFFITLFL
LYPSPLFSVT HQMALSLYL
