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NU4LM_ARATH
ID   NU4LM_ARATH             Reviewed;         100 AA.
AC   Q04614; A7KNH4;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 4L;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 4L;
GN   Name=ND4L; Synonyms=NAD4L; OrderedLocusNames=AtMg00650;
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].
RX   PubMed=1494348; DOI=10.1007/bf00279640;
RA   Brandt P., Sunkel S., Unseld M., Brennicke A., Knoop V.;
RT   "The nad4L gene is encoded between exon c of nad5 and orf25 in the
RT   Arabidopsis mitochondrial genome.";
RL   Mol. Gen. Genet. 236:33-38(1992).
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 [MRNA] OF 18-90, 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).
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=14 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 19 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 29 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 32 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 34 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 37 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 53 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 63 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941}, 66 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:17565941};
CC   -!- SIMILARITY: Belongs to the complex I subunit 4L family. {ECO:0000305}.
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DR   EMBL; X67105; CAA47479.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; Y08501; CAA69749.3; ALT_SEQ; Genomic_DNA.
DR   EMBL; EF488917; ABS50629.1; -; mRNA.
DR   EMBL; EF488919; ABS50631.1; -; mRNA.
DR   PIR; S34400; S34400.
DR   RefSeq; NP_085525.1; NC_001284.2.
DR   PDB; 7A23; EM; 3.70 A; K=1-100.
DR   PDB; 7A24; EM; 3.80 A; K=1-100.
DR   PDB; 7AR7; EM; 3.72 A; K=1-88.
DR   PDBsum; 7A23; -.
DR   PDBsum; 7A24; -.
DR   PDBsum; 7AR7; -.
DR   AlphaFoldDB; Q04614; -.
DR   SMR; Q04614; -.
DR   STRING; 3702.ATMG00650.1; -.
DR   PRIDE; Q04614; -.
DR   Araport; ATMG00650; -.
DR   eggNOG; KOG4669; Eukaryota.
DR   InParanoid; Q04614; -.
DR   OrthoDB; 1591545at2759; -.
DR   BioCyc; ARA:ATMG00650-MON; -.
DR   PRO; PR:Q04614; -.
DR   Proteomes; UP000006548; Mitochondrion (cv. C24).
DR   ExpressionAtlas; Q04614; 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:0009536; C:plastid; IEA:UniProt.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   HAMAP; MF_01456; NDH1_NuoK; 1.
DR   InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K.
DR   InterPro; IPR039428; NUOK/Mnh_C1-like.
DR   PANTHER; PTHR11434; PTHR11434; 1.
DR   Pfam; PF00420; Oxidored_q2; 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..100
FT                   /note="NADH-ubiquinone oxidoreductase chain 4L"
FT                   /id="PRO_0000118386"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   100 AA;  11135 MW;  BF54248CC3EBAD5B CRC64;
     MDLIKYFTFS MIIFILGIWG ILLNRRNILI MLMSIELMLL AVNSNFLVFS VSLDDMMGQV
     FALLVLTVAA AESAIGLAIF VITFRVRGTI AVEFINSIQG
 
 
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