ID A0A6C0R3C3_SANVI Unreviewed; 348 AA. AC A0A6C0R3C3; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 27-NOV-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:QHZ87563.1}; OS Sander vitreus (Walleye) (Perca vitrea). OG Mitochondrion {ECO:0000313|EMBL:QHZ87563.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Percoidei; Percidae; Luciopercinae; Sander. OX NCBI_TaxID=283036 {ECO:0000313|EMBL:QHZ87563.1}; RN [1] {ECO:0000313|EMBL:QHZ87563.1} RP NUCLEOTIDE SEQUENCE. RA Sandel M.W.; RL Submitted (DEC-2019) 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 + NADH + 5 H(+)(in) = a ubiquinol + NAD(+) + 4 CC H(+)(out); 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: Mitochondrion inner membrane CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU003403}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004448, CC 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; MN853162; QHZ87563.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6C0R3C3; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. 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; IPR050175; Complex_I_Subunit_2. 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}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003403}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU003403}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, 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 59..80 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 92..115 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 145..165 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 177..193 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 199..218 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 230..253 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 273..293 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..287 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 289..343 FT /note="NADH dehydrogenase subunit 2 C-terminal" FT /evidence="ECO:0000259|Pfam:PF06444" SQ SEQUENCE 348 AA; 37761 MW; 17DF2661BF83878D CRC64; MAPYTLAIML FTLGLGTSIT FASSHWLIAW MGLEINTLAI IPLMAQDHSP RGVEASAKYF IVQSTAGAAL LFASATNAWF TGYWDIQQIS HPLPVALITT ALAFKMGLAP LHTWLPEIIQ GLNLTTGLIL STWQKLAPFT LMLQIYPPAT PTLIVLGLAS ILFGGWGGLN QTQLRKLLAY SSITHLGWMI LVLQFSPPLA LLSLLTYFLM TFSAFLVFKF NKATTINTLA ISWAKAPIIT TLLPPVLLSL GGLPPLTGFM SKWLILQELA SQGLAVTATL AALSSLLSLY FYLRIAHAMT LTTPPNDIPG MTPWRHGASP LSQPMAMAMI VSIILLPLTP AILAFFTR //