ID H9LNU1_CROCR Unreviewed; 606 AA. AC H9LNU1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 13-APR-2016, entry version 23. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|RuleBase:RU003404, ECO:0000256|SAAS:SAAS00370141}; DE EC=1.6.5.3 {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; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Hyaenidae; OC 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., RA Artiguenave F., Wincker P., Aury J.M., Elalouf J.M.; RT "Coprolites as a source of information on the genome and diet of the RT cave hyena."; RL Proc. R. Soc. B 279:2825-2830(2012). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). {ECO:0000256|SAAS:SAAS00205316}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). {ECO:0000256|RuleBase:RU003404, CC ECO:0000256|SAAS:SAAS00370008}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU003404, ECO:0000256|SAAS:SAAS00370072}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU003404, CC ECO:0000256|SAAS:SAAS00370072}. 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 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:respiratory chain; 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|SAAS:SAAS00448190}; KW Membrane {ECO:0000256|SAAS:SAAS00464283, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU000318, KW ECO:0000256|SAAS:SAAS00448066, ECO:0000313|EMBL:AEG77628.1}; KW Mitochondrion inner membrane {ECO:0000256|SAAS:SAAS00448105}; KW NAD {ECO:0000256|RuleBase:RU000317, ECO:0000256|SAAS:SAAS00448053}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000317, KW ECO:0000256|SAAS:SAAS00464177}; KW Respiratory chain {ECO:0000256|SAAS:SAAS00448195}; KW Transmembrane {ECO:0000256|RuleBase:RU003404, KW ECO:0000256|SAAS:SAAS00464191, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00464492, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00448204}; KW Ubiquinone {ECO:0000256|RuleBase:RU000318, KW ECO:0000256|SAAS:SAAS00448240}. FT TRANSMEM 6 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 117 134 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 140 160 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 172 191 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 245 263 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 275 294 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 368 386 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 406 428 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 449 468 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 488 507 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 586 604 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 65 121 Proton_antipo_N. {ECO:0000259|Pfam: FT PF00662}. FT DOMAIN 134 418 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 422 601 NADH5_C. {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 //