ID   V5N318_9PRIM            Unreviewed;       347 AA.
AC   V5N318;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00387861};
DE            EC=7.1.1.2 {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS01109717};
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   Huesos.";
RL   Nature 505:403-406(2014).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I) that is believed to belong to
CC       the minimal assembly required for catalysis. Complex I functions
CC       in the transfer of electrons from NADH to the respiratory chain.
CC       The immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone. {ECO:0000256|RuleBase:RU003403,
CC       ECO:0000256|SAAS:SAAS00093760}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4
CC         H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565,
CC         Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389,
CC         ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=7.1.1.2; Evidence={ECO:0000256|RuleBase:RU003403,
CC         ECO:0000256|SAAS:SAAS01125045};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00093751};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003403,
CC       ECO:0000256|SAAS:SAAS00093751}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC       {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00573211}.
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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: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|RuleBase:RU003403,
KW   ECO:0000256|SAAS:SAAS00464461};
KW   Membrane {ECO:0000256|RuleBase:RU003403,
KW   ECO:0000256|SAAS:SAAS00093718};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003403,
KW   ECO:0000256|SAAS:SAAS00464403, ECO:0000313|EMBL:AHA82094.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU003403,
KW   ECO:0000256|SAAS:SAAS00464436};
KW   NAD {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00093707};
KW   Respiratory chain {ECO:0000256|RuleBase:RU003403,
KW   ECO:0000256|SAAS:SAAS00093685};
KW   Translocase {ECO:0000256|RuleBase:RU003403,
KW   ECO:0000256|SAAS:SAAS01109684};
KW   Transmembrane {ECO:0000256|RuleBase:RU003403,
KW   ECO:0000256|SAAS:SAAS00093696};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU003403,
KW   ECO:0000256|SAAS:SAAS00464584};
KW   Transport {ECO:0000256|SAAS:SAAS00093687};
KW   Ubiquinone {ECO:0000256|RuleBase:RU003403,
KW   ECO:0000256|SAAS:SAAS00093675}.
FT   TRANSMEM     56     76       Helical. {ECO:0000256|RuleBase:RU003403}.
FT   TRANSMEM     96    115       Helical. {ECO:0000256|RuleBase:RU003403}.
FT   TRANSMEM    151    171       Helical. {ECO:0000256|RuleBase:RU003403}.
FT   TRANSMEM    178    196       Helical. {ECO:0000256|RuleBase:RU003403}.
FT   TRANSMEM    202    219       Helical. {ECO:0000256|RuleBase:RU003403}.
FT   TRANSMEM    239    257       Helical. {ECO:0000256|RuleBase:RU003403}.
FT   TRANSMEM    277    305       Helical. {ECO:0000256|RuleBase:RU003403}.
FT   TRANSMEM    325    344       Helical. {ECO:0000256|RuleBase:RU003403}.
FT   DOMAIN       23    284       Proton_antipo_M. {ECO:0000259|Pfam:
FT                                PF00361}.
FT   DOMAIN      290    343       NADH_dehy_S2_C. {ECO:0000259|Pfam:
FT                                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
//