ID H6UPA4_LOXCY Unreviewed; 175 AA.
AC H6UPA4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-NOV-2024, entry version 41.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 6 {ECO:0000256|ARBA:ARBA00021095, ECO:0000256|RuleBase:RU004430};
DE EC=7.1.1.2 {ECO:0000256|ARBA:ARBA00012944, ECO:0000256|RuleBase:RU004430};
GN Name=ND6 {ECO:0000313|EMBL:AEQ59312.1};
OS Loxodonta cyclotis (African forest elephant).
OG Mitochondrion {ECO:0000313|EMBL:AEQ59312.1}.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=99490 {ECO:0000313|EMBL:AEQ59312.1};
RN [1] {ECO:0000313|EMBL:AEQ59312.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Coco {ECO:0000313|EMBL:AEQ59312.1};
RC TISSUE=Blood {ECO:0000313|EMBL:AEQ59312.1};
RX PubMed=22260276; DOI=10.1111/j.1365-294X.2012.05461.x;
RA Brandt A.L., Ishida Y., Georgiadis N.J., Roca A.L.;
RT "Forest elephant mitochondrial genomes reveal that elephantid
RT diversification in Africa tracked climate transitions.";
RL Mol. Ecol. 21:1175-1189(2012).
RN [2] {ECO:0000313|EMBL:AFX94966.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL0001 {ECO:0000313|EMBL:AFX94966.1};
RX PubMed=23798975; DOI=10.1111/j.1752-4571.2012.00286.x;
RA Ishida Y., Georgiadis N.J., Hondo T., Roca A.L.;
RT "Triangulating the provenance of African elephants using mitochondrial
RT DNA.";
RL Evol. Appl. 6:253-265(2013).
RN [3] {ECO:0000313|EMBL:QSJ48885.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B6059 {ECO:0000313|EMBL:QSJ48885.1}, B6079
RC {ECO:0000313|EMBL:QSJ48950.1}, B6130 {ECO:0000313|EMBL:QSJ48898.1},
RC and B8030 {ECO:0000313|EMBL:QSJ48924.1};
RX PubMed=33338432;
RA de Flamingh A., Coutu A., Sealy J., Chirikure S., Bastos A.D.S.,
RA Libanda-Mubusisi N.M., Malhi R.S., Roca A.L.;
RT "Sourcing Elephant Ivory from a Sixteenth-Century Portuguese Shipwreck.";
RL Curr. Biol. 31:621-628(2021).
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:RU004430}.
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:RU004430};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004225, ECO:0000256|RuleBase:RU004430}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004225,
CC ECO:0000256|RuleBase:RU004430}.
CC -!- SIMILARITY: Belongs to the complex I subunit 6 family.
CC {ECO:0000256|ARBA:ARBA00005698, ECO:0000256|RuleBase:RU004430}.
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DR EMBL; JN673264; AEQ59312.1; -; Genomic_DNA.
DR EMBL; JQ438501; AFX94966.1; -; Genomic_DNA.
DR EMBL; MT636092; QSJ48885.1; -; Genomic_DNA.
DR EMBL; MT636093; QSJ48898.1; -; Genomic_DNA.
DR EMBL; MT636095; QSJ48924.1; -; Genomic_DNA.
DR EMBL; MT636097; QSJ48950.1; -; Genomic_DNA.
DR RefSeq; YP_007626834.1; NC_020759.1.
DR AlphaFoldDB; H6UPA4; -.
DR GeneID; 14842600; -.
DR CTD; 4541; -.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.1200; NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ; 1.
DR InterPro; IPR050269; ComplexI_Subunit6.
DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR PANTHER; PTHR11435; NADH UBIQUINONE OXIDOREDUCTASE SUBUNIT ND6; 1.
DR PANTHER; PTHR11435:SF1; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 6; 1.
DR Pfam; PF00499; Oxidored_q3; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU004430};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004430};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU004430};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU004430};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|RuleBase:RU004430};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU004430};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU004430};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004430};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU004430};
KW Ubiquinone {ECO:0000256|RuleBase:RU004430}.
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004430"
FT TRANSMEM 50..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004430"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004430"
FT TRANSMEM 114..136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004430"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004430"
SQ SEQUENCE 175 AA; 19022 MW; 8C91189B340559E9 CRC64;
MMYIVFIMSV LYVVGFIGFS SKPSPVYGGM SLVVSGGLGC GIIMSSGGSF LGLVVFLVYL
GGMMVVFGYT IAMATEEYPE TWGSNVVILS AFLVGLLMEI SMVMWLLSGE HELMGFYFGG
LGGLVVLGEG GFEYVREDYS GGASLYSYGF WFLAMAGWML FVSIFIAIEV TRKRY
//