ID H9LNU1_CROCR Unreviewed; 606 AA. AC H9LNU1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAR-2024, entry version 53. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|ARBA:ARBA00021096, ECO:0000256|RuleBase:RU003404}; DE EC=7.1.1.2 {ECO:0000256|ARBA:ARBA00012944, ECO:0000256|RuleBase:RU003404}; GN Name=ND5 {ECO:0000313|EMBL:AEG77628.1}; OS Crocuta crocuta (Spotted hyena). OG Mitochondrion {ECO:0000313|EMBL:AEG77628.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Hyaenidae; Crocuta. OX NCBI_TaxID=9678 {ECO:0000313|EMBL:AEG77628.1}; RN [1] {ECO:0000313|EMBL:AEG77628.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CC8 {ECO:0000313|EMBL:AEG77615.1}, and CC9 RC {ECO:0000313|EMBL:AEG77628.1}; RC TISSUE=Coprolite {ECO:0000313|EMBL:AEG77628.1}; RX PubMed=22456883; DOI=10.1098/rspb.2012.0358; RA Bon C., Berthonaud V., Maksud F., Labadie K., Poulain J., Artiguenave F., RA Wincker P., Aury J.M., Elalouf J.M.; RT "Coprolites as a source of information on the genome and diet of the cave RT hyena."; RL Proc. R. Soc. B 279:2825-2830(2012). RN [2] {ECO:0000313|EMBL:QIP89280.1} RP NUCLEOTIDE SEQUENCE. RA Westbury M.V., Hartmann S., Barlow A., Preick M., Ridush B., Nagel D., RA Rathgeber T., Ziegler R., Baryshnikov G., Sheng G., Ludwig A., Wiesel I., RA Dalen L., Bibi F., Werdelin L., Heller R., Hofreiter M.; RT "Hyena paleogenomes reveal a complex evolutionary history of cross- RT continental gene flow between spotted and cave hyena."; RL Sci. Adv. 6:0-eaay0456(2020). 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. Essential for the catalytic activity and assembly of complex CC I. {ECO:0000256|RuleBase:RU003404}. 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:0000256|ARBA:ARBA00000766, CC ECO:0000256|RuleBase:RU003404}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004448}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC {ECO:0000256|RuleBase:RU003404}. 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; JF894378; AEG77615.1; -; Genomic_DNA. DR EMBL; JF894379; AEG77628.1; -; Genomic_DNA. DR EMBL; MN320459; QIP89280.1; -; Genomic_DNA. DR EMBL; MN320463; QIP89332.1; -; Genomic_DNA. DR EMBL; MN320464; QIP89345.1; -; Genomic_DNA. DR EMBL; MN320467; QIP89384.1; -; Genomic_DNA. DR RefSeq; YP_007625676.1; NC_020670.1. DR AlphaFoldDB; H9LNU1; -. DR GeneID; 14842179; -. DR CTD; 4540; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR InterPro; IPR010934; NADH_DH_su5_C. DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR003945; NU5C-like. DR InterPro; IPR001516; Proton_antipo_N. DR NCBIfam; TIGR01974; NDH_I_L; 1. DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR Pfam; PF06455; NADH5_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR PRINTS; PR01434; NADHDHGNASE5. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|ARBA:ARBA00022982}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003404}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU003404}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003404}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU003404}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU003404}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003404}; KW Ubiquinone {ECO:0000256|RuleBase:RU003404}. FT TRANSMEM 6..27 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 39..58 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 78..96 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 117..134 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 140..160 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 172..191 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 245..263 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 275..294 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 368..386 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 406..428 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 449..468 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 488..507 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 586..604 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT DOMAIN 68..118 FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5 FT N-terminal" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 134..417 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 422..601 FT /note="NADH dehydrogenase subunit 5 C-terminal" FT /evidence="ECO:0000259|Pfam:PF06455" SQ SEQUENCE 606 AA; 67955 MW; 409341813C6A8CB4 CRC64; MNLFNSLTMT AMFILLLPII MTSTQMYKSS LYPSYVKTTT SYAFAIVMIP ALMFIYSGQE AIISNWHWMT VQTLKLSMSF KLDYFSIMFM PVALFVTRSI MEFSIWYMHA DPYINRFFKY LLMFLITMII LVTANNLFQL FVGWEGVGIM SFLLIGWWYG RTDANTAALQ AVLYNRIGDV GFILAMAWFL TNSNTWEFQQ IFATKHESLN TPLMGLLLAA TGKSAQFGLH PWLPSAMEGP TPVSALLHSS TMVVAGVFLL IRFHPLMEQS KTAQTLTLCL GAITTLFTAI CALTQNDIKK IIAFSTSSQL GLMIVTIGIN QPYLAFLHIC THAFFKAMLF MCSGSIIHSL NDEQDIRKMG GLFKSMPFTT TALIVGSLAL TGMPFLTGFY SKDLIIETAS TSHTNAWALL MTLIATSLTA AYSTRIMFFT LLEQPRFNSL SPINENNPLL INSIKHLLIG SIFAGYLISH NIPPTTTPQT TMPHYLKLIA LMATITGFVL ALELSLVTKN LKLNPASNMF KFSNLLGYFP TIIHRSLPLA NLTMSQKSAS TLLDLIWLEN VLPKSISYFQ MKSSTIVSNQ KGLIKLYFLS FMITLTISLL LLNYHE //