ID A0A6H0MVE2_HUMAN Unreviewed; 347 AA. AC A0A6H0MVE2; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 22-FEB-2023, entry version 11. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000256|ARBA:ARBA00021008, ECO:0000256|RuleBase:RU003403}; DE EC=7.1.1.2 {ECO:0000256|ARBA:ARBA00012944, ECO:0000256|RuleBase:RU003403}; GN Name=ND2 {ECO:0000313|EMBL:QIV21633.1}; OS Homo sapiens (Human). OG Mitochondrion {ECO:0000313|EMBL:QIV21633.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:QIV21633.1}; RN [1] {ECO:0000313|EMBL:QIV21633.1} RP NUCLEOTIDE SEQUENCE. RA Furtwaengler A., Rohrlach A., Lamnidis T., Papac L.C., Neumann G.U., RA Siebke I., Reiter E., Steuri N., Hald J., Denaire A., Schnitzler B., RA Wahl J., Ramstein M., Schuenemann V.J., Stockhammer P.W., Hafner A., RA Losch S., Haak W., Schiffels S., Krause J.; RT "Ancient genomes reveal social and genetic structure of Late Neolithic RT Switzerland."; RL Nat. Commun. 0:0-0(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:RU003403}. 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:RU003403}; 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, CC ECO:0000256|RuleBase:RU003403}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU003403}. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC {ECO:0000256|ARBA:ARBA00007012, ECO:0000256|RuleBase:RU003403}. 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; MT079052; QIV21633.1; -; Genomic_DNA. DR PeptideAtlas; A0A6H0MVE2; -. 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:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro. DR InterPro; IPR010933; NADH_DH_su2_C. DR InterPro; IPR003917; NADH_UbQ_OxRdtase_chain2. DR InterPro; IPR001750; ND/Mrp_mem. DR PANTHER; PTHR46552; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1. DR PANTHER; PTHR46552:SF1; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1. DR Pfam; PF06444; NADH_dehy_S2_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01436; NADHDHGNASE2. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|RuleBase:RU003403}; KW Membrane {ECO:0000256|RuleBase:RU003403}; KW Mitochondrion {ECO:0000256|RuleBase:RU003403, ECO:0000313|EMBL:QIV21633.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU003403}; KW NAD {ECO:0000256|RuleBase:RU003403}; KW Respiratory chain {ECO:0000256|RuleBase:RU003403}; KW Translocase {ECO:0000256|RuleBase:RU003403}; KW Transmembrane {ECO:0000256|RuleBase:RU003403}; KW Transmembrane helix {ECO:0000256|RuleBase:RU003403}; KW Transport {ECO:0000256|ARBA:ARBA00022448}; KW Ubiquinone {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 56..76 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 96..115 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 151..171 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 178..196 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 202..219 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 239..257 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 277..305 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 325..346 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT DOMAIN 23..284 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 290..338 FT /note="NADH dehydrogenase subunit 2 C-terminal" FT /evidence="ECO:0000259|Pfam:PF06444" SQ SEQUENCE 347 AA; 38999 MW; 291673B9EB7D7D99 CRC64; MNPLAQPVIY STIFAGTLIT ALSSHWFFTW VGLEMNMLAF IPVLTKKMNP RSTEAAIKYF LTQATASMIL LMAILFNNML SGQWTMTNTT NQYSSLMIMM AMAMKLGMAP FHFWVPEXTQ GTPLTSGLLL LTWQKLAPIS IMYQISPSLN VSLLLTLSIL SIMAGSWGGL NQTQLRKILA YSSITHMGWM MAVLPYNPNM TILNLTIYII LTTTAFLLLN LNSSTTTLLL SRTWNKLTWL TPLIPSTLXX LGGLPPLTGF LPKWAIIEEF TKNNSLIIPT IMATITLLNL YFYLRLIYST SITLLPMSNN VKMKWQFEHT KPTPFLXXLI ALTTLLLPXX XXXXMIL //