ID   V5N318_9PRIM            Unreviewed;       347 AA.
AC   V5N318;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   22-FEB-2023, entry version 41.
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:AHA82094.1};
OS   Homo heidelbergensis (Heidelberg man).
OG   Mitochondrion {ECO:0000313|EMBL:AHA82094.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=1425170 {ECO:0000313|EMBL:AHA82094.1};
RN   [1] {ECO:0000313|EMBL:AHA82094.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Femur VIII {ECO:0000313|EMBL:AHA82094.1};
RC   TISSUE=Bone {ECO:0000313|EMBL:AHA82094.1};
RX   PubMed=24305051;
RA   Meyer M., Fu Q., Aximu-Petri A., Glocke I., Nickel B., Arsuaga J.L.,
RA   Martinez I., Gracia A., de Castro J.M., Carbonell E., Paabo S.;
RT   "A mitochondrial genome sequence of a hominin from Sima de los Huesos.";
RL   Nature 505:403-406(2014).
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}.
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DR   EMBL; KF683087; AHA82094.1; -; Genomic_DNA.
DR   RefSeq; YP_008963988.1; NC_023100.1.
DR   GeneID; 17961566; -.
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   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|RuleBase:RU003403};
KW   Membrane {ECO:0000256|RuleBase:RU003403};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003403, ECO:0000313|EMBL:AHA82094.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU003403};
KW   NAD {ECO:0000256|RuleBase:RU003403};
KW   Respiratory chain {ECO:0000256|RuleBase:RU003403};
KW   Translocase {ECO:0000256|RuleBase:RU003403};
KW   Transmembrane {ECO:0000256|RuleBase:RU003403};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU003403};
KW   Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Ubiquinone {ECO:0000256|RuleBase:RU003403}.
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        96..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        178..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        202..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        239..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        277..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   TRANSMEM        325..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003403"
FT   DOMAIN          23..284
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          290..344
FT                   /note="NADH dehydrogenase subunit 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06444"
SQ   SEQUENCE   347 AA;  38887 MW;  5C9A30A2742F700C CRC64;
     MNPLAQPXXX STIFTGTLIT ALSSHWFFTW VGLEMNMLAF IPVLTKKMNP RSTEAAIKYF
     LTQATASMIL LMAILFNNML SGQWTMTNTX XXXXSLMIMM AMAMKLGMAP FHFWVPEVTQ
     GTPLTSGLLL LTWQKLAPIS IMYQISPSLN VSLLLTLSIL SIMAGSWGGL NQTQLRKILA
     YSSITHMGWM MAVLPYNPNM TILNLTIYIX LTTTAFLLLN LNSSTTTLLL SRTWNKLTWL
     TPLIPSTLLS LGGLPPLTGF LPKWAIIEEF TKNNSLIIPT IMATITLLNL YFYLRLIYST
     SITLLPMSNN VKMKWQFEHT KPTPFLPTLI ALTTLLLPIS PFMLXXX
//