NDUS8_BOVIN
ID NDUS8_BOVIN Reviewed; 212 AA.
AC P42028; Q32KV7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:O00217};
DE AltName: Full=Complex I-23kD;
DE Short=CI-23kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit;
DE AltName: Full=TYKY subunit;
DE Flags: Precursor;
GN Name=NDUFS8;
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 PROTEIN SEQUENCE OF 37-59.
RC TISSUE=Heart;
RX PubMed=1901022; DOI=10.1021/bi00225a032;
RA Dupuis A., Skehel J.M., Walker J.E.;
RT "A homologue of a nuclear-coded iron-sulfur protein subunit of bovine
RT mitochondrial complex I is encoded in chloroplast genomes.";
RL Biochemistry 30:2954-2960(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, IDENTIFICATION IN COMPLEX I, SUBCELLULAR
RP LOCATION, AND FUNCTION.
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 [4]
RP FUNCTION, 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).
RN [5]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=25209663; DOI=10.1038/nature13686;
RA Vinothkumar K.R., Zhu J., Hirst J.;
RT "Architecture of mammalian respiratory complex I.";
RL Nature 515:80-84(2014).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC NADH through the respiratory chain, using ubiquinone as an electron
CC acceptor (PubMed:10852722, PubMed:18721790). Essential for the
CC catalytic activity and assembly of complex I (By similarity).
CC {ECO:0000250|UniProtKB:O00217, ECO:0000269|PubMed:10852722,
CC ECO:0000269|PubMed:18721790}.
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 Evidence={ECO:0000250|UniProtKB:O00217};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q56224};
CC Note=Binds 2 [4Fe-4S] clusters per subunit.
CC {ECO:0000250|UniProtKB:Q56224};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits (PubMed:10852722,
CC PubMed:18721790, PubMed:25209663). This is a component of the iron-
CC sulfur (IP) fragment of the enzyme (PubMed:25209663). Interacts with
CC RAB5IF (By similarity). {ECO:0000250|UniProtKB:O00217,
CC ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790,
CC ECO:0000269|PubMed:25209663}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790,
CC ECO:0000269|PubMed:25209663}; Peripheral membrane protein
CC {ECO:0000305|PubMed:25209663}; Matrix side
CC {ECO:0000305|PubMed:25209663}.
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; M58717; AAA30664.1; -; mRNA.
DR EMBL; BC109906; AAI09907.1; -; mRNA.
DR PIR; A38409; A38409.
DR RefSeq; NP_001289598.1; NM_001302669.1.
DR RefSeq; XP_005227041.1; XM_005226984.2.
DR PDB; 5LC5; EM; 4.35 A; I=37-212.
DR PDB; 5LDW; EM; 4.27 A; I=37-212.
DR PDB; 5LDX; EM; 5.60 A; I=37-212.
DR PDB; 5LNK; EM; 3.90 A; 9=37-212.
DR PDB; 5O31; EM; 4.13 A; I=37-212.
DR PDB; 7QSD; EM; 3.10 A; I=1-212.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5LNK; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P42028; -.
DR SMR; P42028; -.
DR CORUM; P42028; -.
DR DIP; DIP-38810N; -.
DR IntAct; P42028; 2.
DR STRING; 9913.ENSBTAP00000016013; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P42028; -.
DR PeptideAtlas; P42028; -.
DR PRIDE; P42028; -.
DR Ensembl; ENSBTAT00000087227; ENSBTAP00000059175; ENSBTAG00000012072.
DR GeneID; 287027; -.
DR KEGG; bta:287027; -.
DR CTD; 4728; -.
DR VEuPathDB; HostDB:ENSBTAG00000012072; -.
DR VGNC; VGNC:31973; NDUFS8.
DR eggNOG; KOG3256; Eukaryota.
DR GeneTree; ENSGT00390000003049; -.
DR HOGENOM; CLU_067218_5_1_1; -.
DR InParanoid; P42028; -.
DR OrthoDB; 1283957at2759; -.
DR TreeFam; TF105610; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000012072; Expressed in tongue muscle and 106 other tissues.
DR ExpressionAtlas; P42028; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR HAMAP; MF_01351; NDH1_NuoI; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR PANTHER; PTHR10849; PTHR10849; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR TIGRFAMs; TIGR01971; NuoI; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW Repeat; Respiratory chain; Transit peptide; Translocase; Transport;
KW Ubiquinone.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1901022"
FT CHAIN 37..212
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 8, mitochondrial"
FT /id="PRO_0000020011"
FT DOMAIN 104..133
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 143..172
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 116
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 155
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT CONFLICT 129
FT /note="T -> I (in Ref. 2; AAI09907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 23896 MW; 4D5F95E4C918FEF8 CRC64;
MRCLTMPMLL RALAQAQAAR AGHASVRGLH SSAVAATYKY VNLREPSMDM KSVTDRAAQT
LLWTELIRGL GMTLSYLFRE PATINYPFEK GPLSPRFRGE HALRRYPSGE ERCIACKLCE
AVCPAQAITI EAEPRADGSR RTTRYDIDMT KCIYCGFCQE ACPVDAIVEG PNFEFSTETH
EELLYNKEKL LNNGDKWEAE IAANIQADYL YR
