ID   H6UPA4_LOXCY            Unreviewed;       175 AA.
AC   H6UPA4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   29-SEP-2021, entry version 33.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 6 {ECO:0000256|RuleBase:RU004430};
DE            EC=7.1.1.2 {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 + 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:RU004430};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000256|RuleBase:RU004430}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU004430}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family.
CC       {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   GeneID; 14842600; -.
DR   CTD; 4541; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.1200; -; 1.
DR   InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR   InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR   Pfam; PF00499; Oxidored_q3; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|RuleBase:RU004430};
KW   Membrane {ECO:0000256|RuleBase:RU004430};
KW   Mitochondrion {ECO:0000256|RuleBase:RU004430, ECO:0000313|EMBL:AEQ59312.1};
KW   NAD {ECO:0000256|RuleBase:RU004430};
KW   Respiratory chain {ECO:0000256|RuleBase:RU004430};
KW   Translocase {ECO:0000256|RuleBase:RU004430};
KW   Transmembrane {ECO:0000256|RuleBase:RU004430};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU004430};
KW   Transport {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
//