ID H9M5Z8_GALVR Unreviewed; 598 AA. AC H9M5Z8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 29-MAY-2024, entry version 49. 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:AES86250.1}; OS Galeopterus variegatus (Malayan flying lemur) (Cynocephalus variegatus). OG Mitochondrion {ECO:0000313|EMBL:AES86250.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Dermoptera; Cynocephalidae; Galeopterus. OX NCBI_TaxID=482537 {ECO:0000313|EMBL:AES86250.1}; RN [1] {ECO:0000313|EMBL:AES86250.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Malayan {ECO:0000313|EMBL:AES86250.1}; RX PubMed=22464472; DOI=10.1016/j.jgg.2012.02.003; RA Xu L., Chen S.Y., Nie W.H., Jiang X.L., Yao Y.G.; RT "Evaluating the Phylogenetic Position of Chinese Tree Shrew (Tupaia RT belangeri chinensis) Based on Complete Mitochondrial Genome: Implication RT for Using Tree Shrew as an Alternative Experimental Animal to Primates in RT Biomedical Research."; RL J. Genet. Genomics 39:131-137(2012). 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; JN800721; AES86250.1; -; Genomic_DNA. DR AlphaFoldDB; H9M5Z8; -. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:TreeGrafter. 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 GO; GO:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter. 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 34..52 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 79..100 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 112..129 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 135..154 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 166..185 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 205..228 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 240..258 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 270..289 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 296..314 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 320..342 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 363..381 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 401..427 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 581..597 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT DOMAIN 63..113 FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5 FT N-terminal" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 129..411 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 417..596 FT /note="NADH dehydrogenase subunit 5 C-terminal" FT /evidence="ECO:0000259|Pfam:PF06455" SQ SEQUENCE 598 AA; 66669 MW; C2C38ED92A270C06 CRC64; MNLTTSLMIT SLTILIIPTL SNMHKHYPYH VKTLTQVAFL TSLLPALTFI YSNQDAVTSN WHWITIQTLE LSINLKLDYF SMIFTPTALF ITWSIMEFSL WYMNSDPNIN KFFKYLLVFL IMMLILTTAN NLMQLLIGWE GVGIMSFLLI GWWYSRTDAN TAALQAIIYN RIGDIGFILA MAWFSTHSNT WNLQQLFILN TDPNLIPLVG LLLAAAGKSA QFGLHPWLPS AMEGPTPVSA LLHSSTMVVA GIFLLIRFHP LMENNKTIQT LALCLGALTT LFTAICALTQ NDIKKIIAFS TSSQLGLMMV TVGINQPYLA FLHICMHAFF KAMLFMCSGS IIHNLNNEQD IRKMGGLYKT MPLTSTSLTI GNLALTGMPF LTGFYSKDLI IETMNTSYTN AWALTVTLIA TSLTAAYSTR IIFLALLGQP RFPALMNTNE NNPHLANPTK RLMIGSIFAG FIISSNIPPT DIPQMTMPPY LKLSTLLITT FGFILALELC LDSLNPNTKS PSPLHNFSTL LGFFPTLAHR TVPHLNLTMS QNMASQTLDL TWLEKTIPKS IAHLQTLAAT NISNQKGLIK LYFLSFLITI TMTSLLII //