ID A0A172MEF5_9SAUR Unreviewed; 345 AA. AC A0A172MEF5; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 03-MAY-2023, entry version 23. 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:ANC96279.1}; OS Bavayia cyclura. OG Mitochondrion {ECO:0000313|EMBL:ANC96279.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Gekkota; Pygopoidea; Diplodactylidae; OC Bavayia. OX NCBI_TaxID=143557 {ECO:0000313|EMBL:ANC96279.1}; RN [1] {ECO:0000313|EMBL:ANC96279.1} RP NUCLEOTIDE SEQUENCE. RA Skipwith P.L., Bauer A.M., Jackman T.R., Sadlier R.A.; RT "Old but not ancient: coalescent species tree of New Caledonian geckos RT reveals recent post-inundation diversification."; RL J. Biogeogr. 0:0-0(2016). 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; KU158041; ANC96279.1; -; Genomic_DNA. DR AlphaFoldDB; A0A172MEF5; -. 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|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU003403}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003403}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU003403}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792, KW ECO:0000256|RuleBase:RU003403}; NAD {ECO:0000256|RuleBase:RU003403}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU003403}; KW Translocase {ECO:0000256|RuleBase:RU003403}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU003403}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU003403}; Transport {ECO:0000256|ARBA:ARBA00022448}; KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 56..75 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 95..115 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 152..171 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 202..221 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 233..254 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 274..294 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 324..342 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT DOMAIN 23..285 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 290..342 FT /note="NADH dehydrogenase subunit 2 C-terminal" FT /evidence="ECO:0000259|Pfam:PF06444" SQ SEQUENCE 345 AA; 38033 MW; 3153D7D7428AC6E6 CRC64; MNPATLTLLY LSMILGTIIT MTSSHWILAW AGLEMNTLAI IPIISKQHHP RATEAATKYF LIQATASAVI LFASSLNAWK TGQWNIYYTP SPESIILLTL AIAMKLGLAP LHFWLPEVLQ GSPLLTTAII STWQKLAPTT ILYMIMDNLN QHTLMILGLT SAVLGGWMGL NQTQTRKIMA FSSIAHMGWV FMALAIDPNL TLLTLSIYLL LTMAMFTSLM TTTSKTLLDL GTAWPQTPTL LSITMLTLVS LGGLPPLTGF MPKWLILKEL ITNNLSTIST LMALSTLPSL FFYIRMSHMT SLTLPPETTS TGHKWRFKLN QAPATTPIIL ASLLLPLTPL IMNFC //