ID H9LNU1_CROCR Unreviewed; 606 AA. AC H9LNU1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-OCT-2020, entry version 37. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|RuleBase:RU003404}; DE EC=7.1.1.2 {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) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone. CC {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}. 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 GeneID; 14842179; -. DR CTD; 4540; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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; IPR003945; NADHpl_OxRdtase_5. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR001516; Proton_antipo_N. DR Pfam; PF06455; NADH5_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR TIGRFAMs; TIGR01974; NDH_I_L; 1. 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, ECO:0000313|EMBL:AEG77628.1}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW NAD {ECO:0000256|RuleBase:RU003404}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU003404}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU003404}; Transport {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 65..121 FT /note="Proton_antipo_N" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 134..418 FT /note="Proton_antipo_M" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 422..601 FT /note="NADH5_C" 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 //