ID Q76HH2_THUAA Unreviewed; 348 AA. AC Q76HH2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 14-DEC-2022, entry version 87. 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:BAD06493.1}; OS Thunnus alalunga (Albacore) (Scomber alalunga). OG Mitochondrion {ECO:0000313|EMBL:BAD06493.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Pelagiaria; Scombriformes; Scombridae; Thunnus. OX NCBI_TaxID=8235 {ECO:0000313|EMBL:BAD06493.1}; RN [1] {ECO:0000313|EMBL:BAD06493.1} RP NUCLEOTIDE SEQUENCE. RA Manchado M., Catanese G., Infante C.; RT "Complete mitochondrial DNA sequence of albacore (Thunnus alalunga)."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEI53252.1} RP NUCLEOTIDE SEQUENCE. RA Martinez Ibarra C., Ishizaki S., Nagashima Y.; RT "Development of a PCR-based method for differentiation of tuna and related RT species in canned products."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AKE49667.1} RP NUCLEOTIDE SEQUENCE. RA Pang J.H., Cheng Q.Q., Sun D.D., Zhang H., Jin S.F.; RT "Phylogenetic relationship of Scombridae fishes inferred from complete RT mitochondrial DNA sequences."; RL Submitted (DEC-2014) 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; GU256526; ADA69862.1; -; Genomic_DNA. DR EMBL; JN086151; AEI53252.1; -; Genomic_DNA. DR EMBL; KP259549; AKE49667.1; -; Genomic_DNA. DR EMBL; AB101291; BAD06493.1; -; Genomic_DNA. DR RefSeq; NP_955706.1; NC_005317.1. DR AlphaFoldDB; Q76HH2; -. DR GeneID; 2702240; -. DR CTD; 4536; -. 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 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 60..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 151..170 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 177..195 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 201..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..293 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 323..346 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT DOMAIN 23..280 FT /note="Proton_antipo_M" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 289..342 FT /note="NADH_dehy_S2_C" FT /evidence="ECO:0000259|Pfam:PF06444" SQ SEQUENCE 348 AA; 37632 MW; F0C05ECF3CECBA9F CRC64; MNPYILATLL FGLGLGTTIT FASSHWLLAW MGLEMNTLAI IPLMAQNHHP RAVEATTKYF LTQATAAAML LFASTTNAWL TGQWNIEQMT HPIPTTMIML ALALKIGLAP VHAWLPEVLQ GLDLTTGLIL STWQKLAPFA LILQIHPTNP ALLIVLGVAS TLVGGWGGLN QTQLRKILAY SSIAHLGWMI LILQFSPSLT LLTLLTYFIM TFSAFLVFKL NKATNINTLA TSWAKAPALT SLTPLVLLSL GGLPPLTGFM PKWLILQELS KQDLAPVATL AALSALLSLY FYLRLSYAMT LTMSPNNLSG TASWRLPSLQ PTLPVATSLV ATLALLPLTP AITAILTL //