ID   NU2M_BRALA              Reviewed;         346 AA.
AC   O21001; O79416;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 2;
GN   Name=ND2; Synonyms=NAD2, NADH2;
OS   Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomidae; Branchiostoma.
OX   NCBI_TaxID=7740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9254918; DOI=10.1093/oxfordjournals.molbev.a025821;
RA   Delarbre C., Barriel V., Tillier S., Janvier P., Gachelin G.;
RT   "The main features of the craniate mitochondrial DNA between the ND1 and
RT   the COI genes were established in the common ancestor with the lancelet.";
RL   Mol. Biol. Evol. 14:807-813(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9628930; DOI=10.1093/nar/26.13.3279;
RA   Spruyt N., Delarbre C., Gachelin G., Laudet V.;
RT   "Complete sequence of the amphioxus (Branchiostoma lanceolatum)
RT   mitochondrial genome: relations to vertebrates.";
RL   Nucleic Acids Res. 26:3279-3285(1998).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR   EMBL; Y09524; CAA70709.1; -; Genomic_DNA.
DR   EMBL; Y16474; CAA76248.1; -; Genomic_DNA.
DR   PIR; C71390; C71390.
DR   RefSeq; NP_007538.1; NC_001912.1.
DR   AlphaFoldDB; O21001; -.
DR   SMR; O21001; -.
DR   GeneID; 808208; -.
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; IPR003917; NADH_UbQ_OxRdtase_chain2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01436; NADHDHGNASE2.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..346
FT                   /note="NADH-ubiquinone oxidoreductase chain 2"
FT                   /id="PRO_0000117561"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        79
FT                   /note="S -> G (in Ref. 1; CAA70709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92
FT                   /note="N -> H (in Ref. 1; CAA70709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="F -> L (in Ref. 1; CAA70709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="V -> A (in Ref. 1; CAA70709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199
FT                   /note="L -> S (in Ref. 1; CAA70709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        210
FT                   /note="I -> V (in Ref. 1; CAA70709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="Q -> H (in Ref. 1; CAA70709)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   346 AA;  37371 MW;  73E1715D0BE5D824 CRC64;
     MSPYISPLFS ITMIMSVMLI SSSGHWVFMW LGLELGTLAF IPILVWWHSS LEVEATVKYF
     IVQAMAAAVF FLGGMVSLSG DFMGGVNQLM GNIGDMMIML AVVTKLGLAP FHYWVVDVVQ
     GLNYIPGAVL LTWQKVPGLA VLTQLATCNN SSMLLLFGMV SALVGGLGGL GQTQMRKLLA
     FSSISHLGWL VVGCVAGSLL GLSYFTLYVI LSIPLFSILH MLNGGHLNQL RTGLMFNPLM
     SVLLGVGFLS LGGLPPFFGF FGKWLLLTHF VGQLLLGVSV VLITGTLISL FYYLRVSYLC
     IVVLGPQQIM SGLNWRKMQL SGLMSGLLVL NMLGLFLVGG ASCLPK