ID NDUS8_PANTR Reviewed; 210 AA. AC Q0MQI3; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 93. 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 Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9598; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ885651; ABH12160.1; -; mRNA. DR RefSeq; NP_001065248.1; NM_001071780.1. DR RefSeq; XP_016775310.1; XM_016919821.1. DR RefSeq; XP_016775311.1; XM_016919822.1. DR RefSeq; XP_016775312.1; XM_016919823.1. DR RefSeq; XP_016775313.1; XM_016919824.1. DR AlphaFoldDB; Q0MQI3; -. DR SMR; Q0MQI3; -. DR STRING; 9598.ENSPTRP00000054355; -. DR Ensembl; ENSPTRT00000061813.3; ENSPTRP00000054355.3; ENSPTRG00000003978.6. DR GeneID; 451375; -. DR KEGG; ptr:451375; -. DR CTD; 4728; -. DR VGNC; VGNC:50384; NDUFS8. DR GeneTree; ENSGT00390000003049; -. DR InParanoid; Q0MQI3; -. DR OMA; QFFRAPY; -. DR OrthoDB; 176717at2759; -. DR Proteomes; UP000002277; Chromosome 11. DR Bgee; ENSPTRG00000003978; Expressed in hindlimb stylopod muscle and 21 other cell types or 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: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 Gene3D; 3.30.70.3270; -; 1. 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 NCBIfam; TIGR01971; NuoI; 1. DR PANTHER; PTHR10849:SF20; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1. DR PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1. DR Pfam; PF12838; Fer4_7; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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_0000251875" 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; 23705 MW; 8C3EBD205BFA0112 CRC64; MRCLTTPMLL RALAQAARAG PPGGRSLHSS AVAATYKYVN MQDPEMDMKS VTDRAARTLL WTELFRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAI CPAQAITIEA EPRADGSRRT TRYDIDMTKC IYCGFCQEAC PVDAIVEGPN FEFSTETHEE LLYNKEKLLN NGDKWEAEIA ANIQADYLYR //