ID A0A5Q2MQH2_CAPHI Unreviewed; 347 AA. AC A0A5Q2MQH2; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 12-AUG-2020, entry version 4. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000256|RuleBase:RU003403}; DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU003403}; GN Name=ND2 {ECO:0000313|EMBL:QGG43632.1}; OS Capra hircus (Goat). OG Mitochondrion {ECO:0000313|EMBL:QGG43632.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Caprinae; Capra. OX NCBI_TaxID=9925 {ECO:0000313|EMBL:QGG43632.1}; RN [1] {ECO:0000313|EMBL:QGG43632.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Andaman {ECO:0000313|EMBL:QGG43632.1}; RC TISSUE=Blood {ECO:0000313|EMBL:QGG43632.1}; RA De A.K., Muthiyan R., Sunder J., Perumal P., Malakar D., Muniswamy K., RA Kundu A., Bhattacharya D.; RT "Capra hircus (Andaman Local Goat from Andaman and Nicobar Islands, India) RT mitochondrion sequence, complete genome."; RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone. CC {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|RuleBase:RU003403}; Multi-pass membrane CC protein {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; MK234706; QGG43632.1; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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, ECO:0000313|EMBL:QGG43632.1}; 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 5..22 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 66..84 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 323..346 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT DOMAIN 23..287 FT /note="Proton_antipo_M" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 290..343 FT /note="NADH_dehy_S2_C" FT /evidence="ECO:0000259|Pfam:PF06444" SQ SEQUENCE 347 AA; 39149 MW; 02F4C02D4F1963D0 CRC64; MNPIIFIIIL MTVMLGTTIV MISSHWLLIW VGFEMNMLAI IPIMMKKHNP RATEASTKYF LTQSTASMLL MMAIIINLMF SGQWTVTKLF HPTASMLMTM ALAMKLGMAP FHFWVPEVTQ GIPLSSGLIL LTWQKLAPMS VLYQILPSIN LNLILTLSIL SIMIGGWGGL NQTQLRKIMA YSSIAHMGWM TAVLLYNPTM MLLNLIIYIT MTSTMFLLFM ANSTTTTLSL SHTWNKAPIM TVLVLITLLS MGGLPPLSGF MPKWMIIQEM TKNNSIILPT LMAITALLNL YFYMRLTYST TLTMFPSTNN MKMKWQFSTT KRMTLLPTMT VLSTMLLPLT PILSILE //