NU4M_ARATH
ID NU4M_ARATH Reviewed; 495 AA.
AC P93313;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 4;
GN Name=ND4; Synonyms=NAD4; OrderedLocusNames=AtMg00580;
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 [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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT2G07717).
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).
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=10 {ECO:0000269|PubMed:10611383}, 25
CC {ECO:0000269|PubMed:10611383}, 36 {ECO:0000269|PubMed:10611383}, 53
CC {ECO:0000269|PubMed:10611383}, 55 {ECO:0000269|PubMed:10611383}, 56
CC {ECO:0000269|PubMed:10611383}, 66 {ECO:0000269|PubMed:10611383}, 106
CC {ECO:0000269|PubMed:10611383}, 121 {ECO:0000269|PubMed:10611383}, 126
CC {ECO:0000269|PubMed:10611383}, 135 {ECO:0000269|PubMed:10611383}, 150
CC {ECO:0000269|PubMed:10611383}, 203 {ECO:0000269|PubMed:10611383}, 220
CC {ECO:0000269|PubMed:10611383}, 256 {ECO:0000269|PubMed:10611383}, 262
CC {ECO:0000269|PubMed:10611383}, 279 {ECO:0000269|PubMed:10611383}, 299
CC {ECO:0000269|PubMed:10611383}, 337 {ECO:0000269|PubMed:10611383}, 345
CC {ECO:0000269|PubMed:10611383}, 377 {ECO:0000269|PubMed:10611383}, 391
CC {ECO:0000269|PubMed:10611383}, 452 {ECO:0000269|PubMed:10611383}, 458
CC {ECO:0000269|PubMed:10611383}, 469 {ECO:0000269|PubMed:10611383}, 473
CC {ECO:0000269|PubMed:10611383}, 478 {ECO:0000269|PubMed:10611383};
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 the duplicated gene
CC (At2g07717) 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 4 family. {ECO:0000305}.
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DR EMBL; Y08501; CAA69742.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_085518.1; NC_001284.2.
DR PDB; 7A23; EM; 3.70 A; M=1-495.
DR PDB; 7AR7; EM; 3.72 A; M=9-495.
DR PDBsum; 7A23; -.
DR PDBsum; 7AR7; -.
DR AlphaFoldDB; P93313; -.
DR SMR; P93313; -.
DR IntAct; P93313; 1.
DR STRING; 3702.ATMG00580.1; -.
DR PeptideAtlas; P93313; -.
DR PRIDE; P93313; -.
DR Araport; ATMG00580; -.
DR eggNOG; KOG4845; Eukaryota.
DR InParanoid; P93313; -.
DR OrthoDB; 996580at2759; -.
DR BioCyc; ARA:ATMG00580-MON; -.
DR PRO; PR:P93313; -.
DR Proteomes; UP000006548; Mitochondrion (cv. C24).
DR ExpressionAtlas; P93313; 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:0048039; F:ubiquinone binding; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507; PTHR43507; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
DR TIGRFAMs; TIGR01972; NDH_I_M; 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..495
FT /note="NADH-ubiquinone oxidoreductase chain 4"
FT /id="PRO_0000117889"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 495 AA; 55830 MW; 246135C86467F445 CRC64;
MLEHFCECYF NLSGLILCPV LGSIILLFIP NSRIRLIRLI GLCASLITFL YSLVLWIQFD
SSTAKFQFVE SLRWLPYENI NFYLGIDGIS LFFVILTTFL IPICILVGWS GMRSYGKEYI
IAFLICEFLM IAVFCMLDLL LFYVFPESVL IPMFIIIGVW GSRQRKIKAA YQFFLYTLLG
SLFMLLAILL ILFQTGTTDL QILLTTEFSE RRQIFLWIAF FASFAVKVPM VPVHIWLPEA
HVEAPTAGSV ILAGILLKFG TYGFLRFSIP MFPEATLCFT PFIYTLSAIA IIYTSLTTLR
QIDLKKIIAY SSVAHMNLVT IGMFSPNIQG IGGSILLMLS HGLVSSALFL CVGVLYDRHK
TRLVRYYGGL VSTMPNFSTI FFSFTLANMS LPGTSSFIGE FLILVGAFQR NSLVATLAAL
GMILGAAYSL WLYNRVVSGN LKPDFLHKFS DLNGREVFIF IPFLVGLVWM GVYPKVFLDC
MHTSVSNLVQ HGKFH
