ID NDUS1_RAT Reviewed; 727 AA. AC Q66HF1; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 140. DE RecName: Full=NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial; DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P28331}; DE Flags: Precursor; GN Name=Ndufs1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP PROTEIN SEQUENCE OF 185-200; 247-266; 429-441; 484-499; 519-528; 544-557 RP AND 625-643, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; RA Lubec G., Afjehi-Sadat L., Chen W.-Q.; RL Submitted (APR-2007) to UniProtKB. 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 catalysing the entry and CC efficient transfer of electrons within complex I (By similarity). Plays CC a key role in the assembly and stability of complex I and participates CC in the association of complex I with ubiquinol-cytochrome reductase CC complex (Complex III) to form supercomplexes (By similarity). CC {ECO:0000250|UniProtKB:P28331}. 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:P28331}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000250|UniProtKB:Q56223}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. CC {ECO:0000250|UniProtKB:Q56223}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:Q56223}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. CC {ECO:0000250|UniProtKB:Q56223}; CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex CC I) which is composed of 45 different subunits (By similarity). This is CC the largest subunit of complex I and it is a component of the iron- CC sulfur (IP) fragment of the enzyme (By similarity). Complex I CC associates with ubiquinol-cytochrome reductase complex (Complex III) to CC form supercomplexes (By similarity). Interacts with MDM2 and AKAP1 (By CC similarity). {ECO:0000250|UniProtKB:P15690, CC ECO:0000250|UniProtKB:P28331, ECO:0000250|UniProtKB:Q91VD9}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P15690}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P15690}; Matrix side CC {ECO:0000250|UniProtKB:P15690}. CC -!- SIMILARITY: Belongs to the complex I 75 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; BC081892; AAH81892.1; -; mRNA. DR RefSeq; NP_001005550.1; NM_001005550.1. DR AlphaFoldDB; Q66HF1; -. DR SMR; Q66HF1; -. DR BioGRID; 256969; 4. DR IntAct; Q66HF1; 3. DR MINT; Q66HF1; -. DR STRING; 10116.ENSRNOP00000015851; -. DR CarbonylDB; Q66HF1; -. DR GlyGen; Q66HF1; 8 sites, 1 O-linked glycan (8 sites). DR iPTMnet; Q66HF1; -. DR PhosphoSitePlus; Q66HF1; -. DR SwissPalm; Q66HF1; -. DR jPOST; Q66HF1; -. DR PaxDb; 10116-ENSRNOP00000015851; -. DR Ensembl; ENSRNOT00000104288.1; ENSRNOP00000087012.1; ENSRNOG00000011849.7. DR Ensembl; ENSRNOT00055038087; ENSRNOP00055031070; ENSRNOG00055022105. DR Ensembl; ENSRNOT00060034327; ENSRNOP00060028160; ENSRNOG00060019699. DR Ensembl; ENSRNOT00065048952; ENSRNOP00065040141; ENSRNOG00065028358. DR GeneID; 301458; -. DR KEGG; rno:301458; -. DR UCSC; RGD:1359670; rat. DR AGR; RGD:1359670; -. DR CTD; 4719; -. DR RGD; 1359670; Ndufs1. DR eggNOG; KOG2282; Eukaryota. DR GeneTree; ENSGT00940000153514; -. DR HOGENOM; CLU_000422_11_6_1; -. DR InParanoid; Q66HF1; -. DR OMA; QDQAMAY; -. DR OrthoDB; 19999at2759; -. DR PhylomeDB; Q66HF1; -. DR TreeFam; TF105756; -. DR Reactome; R-RNO-611105; Respiratory electron transport. DR Reactome; R-RNO-6799198; Complex I biogenesis. DR PRO; PR:Q66HF1; -. DR Proteomes; UP000002494; Chromosome 9. DR Bgee; ENSRNOG00000011849; Expressed in heart and 20 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0005758; C:mitochondrial intermembrane space; 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:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; ISO:RGD. 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:0008637; P:apoptotic mitochondrial changes; ISS:UniProtKB. DR GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB. DR GO; GO:0045333; P:cellular respiration; 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:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB. DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB. DR CDD; cd00207; fer2; 1. DR CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1. DR Gene3D; 3.10.20.740; -; 1. DR Gene3D; 3.30.200.210; -; 1. DR Gene3D; 3.30.70.20; -; 1. DR Gene3D; 3.40.50.740; -; 1. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS. DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu. DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. DR InterPro; IPR015405; NDUFS1-like_C. DR NCBIfam; TIGR01973; NuoG; 1. DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1. DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1. DR Pfam; PF13510; Fer2_4; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1. DR Pfam; PF09326; NADH_dhqG_C; 1. DR SMART; SM00929; NADH-G_4Fe-4S_3; 1. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51839; 4FE4S_HC3; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00641; COMPLEX1_75K_1; 1. DR PROSITE; PS00642; COMPLEX1_75K_2; 1. DR PROSITE; PS00643; COMPLEX1_75K_3; 1. DR Genevisible; Q66HF1; RN. PE 1: Evidence at protein level; KW 2Fe-2S; 4Fe-4S; Acetylation; Direct protein sequencing; Electron transport; KW Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; KW Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome; KW Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone. FT TRANSIT 1..23 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:P15690" FT CHAIN 24..727 FT /note="NADH-ubiquinone oxidoreductase 75 kDa subunit, FT mitochondrial" FT /id="PRO_0000271388" FT DOMAIN 30..108 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 108..147 FT /note="4Fe-4S His(Cys)3-ligated-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT DOMAIN 245..301 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 64 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT BINDING 75 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT BINDING 78 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT BINDING 92 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT BINDING 124 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 128 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 131 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 137 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 176 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q56223" FT BINDING 179 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q56223" FT BINDING 182 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q56223" FT BINDING 226 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q56223" FT MOD_RES 84 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91VD9" FT MOD_RES 499 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91VD9" FT MOD_RES 709 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91VD9" SQ SEQUENCE 727 AA; 79412 MW; EDAC634B2697984A CRC64; MLRIPVKRAL IGLSKSPKGY VRSTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL LANHPLDCPI CDQGGECDLQ DQSMMFGSDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ RLTEPMVRNE KGLLTYTSWE DALSRVAGML QSFEGKAVAA IAGGLVDAEA LVALKDLLNK VDSDTLCTEE IFPNEGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK SWLHNDLKVA LIGSPVDLTY RYDHLGDSPK ILQDIASGNH EFSKVLNAAK KPMVVLGSSA LQRDDGAAIL AAVSSIAQKI RVASGAAAEW KVMNILHRIA SQVAALDLGY KPGVEAIRKN PPKLLFLLGA DGGCITRQDL PKDCFIVYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE GRAQQTKVAV TPPGLAREDW KIIRALSEIA GITLPYDTLD QVRNRLGEVS PNLVRYDDVE EANYFQQASE LAKLVDQEFL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA VEEPSIC //