ID A0A3G1TJ06_LEICE Unreviewed; 346 AA. AC A0A3G1TJ06; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 24-JAN-2024, entry version 22. 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:AYC44947.1}; OS Leiothlypis celata orestera. OG Mitochondrion {ECO:0000313|EMBL:AYC44947.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Parulidae; OC Leiothlypis. OX NCBI_TaxID=2320902 {ECO:0000313|EMBL:AYC44947.1}; RN [1] {ECO:0000313|EMBL:AYC44947.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZRH173 {ECO:0000313|EMBL:AYC44947.1}; RA Hanna Z.R., Cicero C., Bowie R.C.K.; RT "Phylogeography of the orange-crowned warbler (Oreothlypis celata; Aves: RT Passeriformes: Parulidae)."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. 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; MG686781; AYC44947.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3G1TJ06; -. 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|RuleBase:RU003403, ECO:0000313|EMBL:AYC44947.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU003403}; KW 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|RuleBase:RU003403}. FT TRANSMEM 5..21 FT /note="Helical" FT /evidence="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 178..196 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 202..222 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 242..261 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 281..304 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 325..345 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT DOMAIN 23..288 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 290..343 FT /note="NADH dehydrogenase subunit 2 C-terminal" FT /evidence="ECO:0000259|Pfam:PF06444" SQ SEQUENCE 346 AA; 38289 MW; 439E9253E9DA052C CRC64; MNPQANLIFI ISLLLGTTIT ISSNHWIMAW TGLEINTLAI LPLISKSHHP RAIEAATKYF LTQAAASALV LFSSMTNAWH TGQWDITQLT HPTSSLILTS AIAMKLGLVP FHFWFPEVLQ GSPLTTGLLL STMMKLPPIT LLYMTSPSLN PTLLTTLAIL STALGGWMGL NQTQIRKILA FSSISHLGWM AIIIIYNPKL TLLNFYLYAM MTTTVFLTLN TIKVLKLSTL MTAWTKIPSL NAMLLLTLLS LAGLPPLTGF LPKWLIIQEL TKQDMAPAAT LISLLSLLSL FFYLRLAYCT TITLPPHTTN HMKQWRTNKS TNITIAILTT MSVMLLPISP MILTIV //