NDUAA_BOVIN
ID NDUAA_BOVIN Reviewed; 343 AA.
AC P34942;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;
DE AltName: Full=Complex I-42kD;
DE Short=CI-42kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 42 kDa subunit;
DE Flags: Precursor;
GN Name=NDUFA10;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Heart;
RX PubMed=1832859; DOI=10.1042/bj2780821;
RA Fearnley I.M., Finel M., Skehel J.M., Walker J.E.;
RT "NADH:ubiquinone oxidoreductase from bovine heart mitochondria. cDNA
RT sequences of the import precursors of the nuclear-encoded 39 kDa and 42 kDa
RT subunits.";
RL Biochem. J. 278:821-829(1991).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, IDENTIFICATION IN COMPLEX I, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10852722; DOI=10.1021/bi000335t;
RA Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E.;
RT "Resolution of the membrane domain of bovine complex I into subcomplexes:
RT implications for the structural organization of the enzyme.";
RL Biochemistry 39:7229-7235(2000).
RN [3]
RP SUBUNIT, IDENTIFICATION IN COMPLEX I, AND SUBCELLULAR LOCATION.
RX PubMed=18721790; DOI=10.1016/j.ab.2008.07.029;
RA Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A.,
RA Robinson N.C.;
RT "Subunit analysis of bovine heart complex I by reversed-phase high-
RT performance liquid chromatography, electrospray ionization-tandem mass
RT spectrometry, and matrix-assisted laser desorption/ionization-time-of-
RT flight mass spectrometry.";
RL Anal. Biochem. 382:116-121(2008).
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.
CC {ECO:0000250|UniProtKB:O95299}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Complex I is composed of 45 different subunits. This a
CC component of the hydrophobic protein fraction.
CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790}.
CC -!- PTM: Phosphorylation at Ser-238 by PINK1 is required for the binding
CC and/or reduction of the complex I substrate ubiquinone.
CC {ECO:0000250|UniProtKB:Q99LC3}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA10 subunit family.
CC {ECO:0000305}.
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DR EMBL; X59419; CAA42054.1; -; mRNA.
DR PIR; S17677; S17677.
DR RefSeq; NP_788828.1; NM_176655.2.
DR PDB; 5LC5; EM; 4.35 A; O=114-341.
DR PDB; 5LDW; EM; 4.27 A; O=114-343.
DR PDB; 5LDX; EM; 5.60 A; O=114-341.
DR PDB; 5O31; EM; 4.13 A; O=24-343.
DR PDB; 7QSD; EM; 3.10 A; O=1-343.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P34942; -.
DR SMR; P34942; -.
DR CORUM; P34942; -.
DR DIP; DIP-38803N; -.
DR IntAct; P34942; 1.
DR STRING; 9913.ENSBTAP00000004245; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR iPTMnet; P34942; -.
DR PaxDb; P34942; -.
DR PeptideAtlas; P34942; -.
DR PRIDE; P34942; -.
DR GeneID; 338060; -.
DR KEGG; bta:338060; -.
DR CTD; 4705; -.
DR eggNOG; KOG3877; Eukaryota.
DR HOGENOM; CLU_050591_0_1_1; -.
DR InParanoid; P34942; -.
DR OrthoDB; 1147235at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR CDD; cd02030; NDUO42; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR015828; NDUFA10.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000543; NADH_UQ_42KD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW FAD; Flavoprotein; Mitochondrion; Phosphoprotein; Reference proteome;
KW Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1832859"
FT CHAIN 24..343
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 10, mitochondrial"
FT /id="PRO_0000019987"
FT MOD_RES 110
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC3"
FT MOD_RES 110
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LC3"
FT MOD_RES 238
FT /note="Phosphoserine; by PINK1"
FT /evidence="ECO:0000250|UniProtKB:Q99LC3"
SQ SEQUENCE 343 AA; 39264 MW; F1AA5A93B438BA42 CRC64;
MALRLLRLVP PRVGGIHTSV QFKLQYGPLA YILGEKATKK MTEKSKLITV DGNICSGKSK
LAKEIAEKLG LKHFPEAGIH YVDSTTGDGK PLPVQFSGNC SLEKFYDDPK SNDGNSYRLQ
AWLYASRLLQ YADALEHLLS TGQGVVLERS IYSDFVFLEA MYRQGFIRKQ CVDHYNQVKK
VTICEYLPPH VVVYVDVPVP EVQSRIQKKG NPHEMKITSA YLQDIENAYK GTFLPEMSEK
CEVLQYSAWE AQDAEKVVED IEYLKYDKGP WLDQNDRNLH KLRMLVQDKL EVLNYTSIPV
FLPEVTVGAH QSDQVFQEFT ELPGRKYRAG YNEDVGDKWI WLK
