NDUS8_GORGO
ID NDUS8_GORGO Reviewed; 210 AA.
AC Q0MQI2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Flags: Precursor;
GN Name=NDUFS8;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16828987; DOI=10.1016/j.gene.2006.03.015;
RA Mishmar D., Ruiz-Pesini E., Mondragon-Palomino M., Procaccio V., Gaut B.,
RA Wallace D.C.;
RT "Adaptive selection of mitochondrial complex I subunits during primate
RT radiation.";
RL Gene 378:11-18(2006).
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 (By similarity). Essential for the catalytic activity and
CC assembly of complex I (By similarity). {ECO:0000250|UniProtKB:O00217}.
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] cluster. {ECO:0000250|UniProtKB:Q56224};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits (By similarity). This is
CC a component of the iron-sulfur (IP) fragment of the enzyme (By
CC similarity). Interacts with RAB5IF (By similarity).
CC {ECO:0000250|UniProtKB:O00217, ECO:0000250|UniProtKB:P42028}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P42028}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P42028}; Matrix side
CC {ECO:0000250|UniProtKB:P42028}.
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; DQ885652; ABH12161.1; -; mRNA.
DR RefSeq; NP_001266636.1; NM_001279707.1.
DR RefSeq; XP_018891215.1; XM_019035670.1.
DR RefSeq; XP_018891216.1; XM_019035671.1.
DR RefSeq; XP_018891217.1; XM_019035672.1.
DR AlphaFoldDB; Q0MQI2; -.
DR SMR; Q0MQI2; -.
DR STRING; 9593.ENSGGOP00000004900; -.
DR Ensembl; ENSGGOT00000005026; ENSGGOP00000004900; ENSGGOG00000005001.
DR GeneID; 101148614; -.
DR KEGG; ggo:101148614; -.
DR CTD; 4728; -.
DR eggNOG; KOG3256; Eukaryota.
DR GeneTree; ENSGT00390000003049; -.
DR HOGENOM; CLU_067218_5_1_1; -.
DR InParanoid; Q0MQI2; -.
DR OMA; RGDLYYT; -.
DR OrthoDB; 1283957at2759; -.
DR Proteomes; UP000001519; Chromosome 11.
DR Bgee; ENSGGOG00000005001; Expressed in heart and 6 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS: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; ISS: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 2: Evidence at transcript level;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW Reference proteome; Repeat; Respiratory chain; Transit peptide;
KW Translocase; Transport; Ubiquinone.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..210
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 8, mitochondrial"
FT /id="PRO_0000251874"
FT DOMAIN 102..131
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 141..170
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 117
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 210 AA; 23703 MW; 663FA09AF05D1CA9 CRC64;
MRCLTTPVLL RALAQAARAG PPGGRSLHSS AVAATYKYVN MQDPEMDMKS VTDRAARTLL
WTELFRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAI
CPAQAITIEA EPRADGSRRT TRYDIDMTKC IYCGFCQEAC PVDAIVEGPN FEFSTETHEE
LLYNKEKLLN NGDKWEAEIT ANIQADYLYR
