NU2M_GADMO
ID NU2M_GADMO Reviewed; 348 AA.
AC P55780;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=MT-ND2; Synonyms=MTND2, NADH2, ND2;
OS Gadus morhua (Atlantic cod).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Norwegian coastal 1;
RX PubMed=8018725; DOI=10.1016/0167-4781(94)90015-9;
RA Johansen S., Johansen T.;
RT "Sequence analysis of 12 structural genes and a novel non-coding region
RT from mitochondrial DNA of Atlantic cod, Gadus morhua.";
RL Biochim. Biophys. Acta 1218:213-217(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Norwegian coastal 1;
RX PubMed=8817926;
RA Johansen S., Bakke I.;
RT "The complete mitochondrial DNA sequence of Atlantic cod (Gadus morhua):
RT relevance to taxonomic studies among codfishes.";
RL Mol. Mar. Biol. Biotechnol. 5:203-214(1996).
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; X76363; CAA53964.1; -; Genomic_DNA.
DR EMBL; X99772; CAA68107.1; -; Genomic_DNA.
DR PIR; S45350; S45350.
DR RefSeq; NP_008614.1; NC_002081.1.
DR AlphaFoldDB; P55780; -.
DR SMR; P55780; -.
DR GeneID; 808445; -.
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; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..348
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117588"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 348 AA; 37893 MW; DA6EF3E3F0C1255D CRC64;
MNPFILSILL LSLGLGTTLT FASSHWLLAW MGLEISTLAI IPLMSQHHHP RAVEATTKYF
ITQAAAAALI LFASTTNAWI TGQWDINFDL HFFPASMLTM ALALKMGLAP VHFWLPEVLQ
GLDLTTGLIL STWQKLAPFI LMCQIMPVNS SLITFLGVTS TLVGGWGGLN QTQLRKILAY
SSIAHLGWMI LVMQFNQQLA LLALIIYIPM TFSTFMIFKT NSSTTVNTLA ASWAKTPALT
AITPMILLSL GGLPPLSGFM PKWMILQELT KQDIPLTASI AALSALLSLY FYLRVSYAMT
LTISPNNLNA TTPWRLQTTA STLPLAISAT ISAMLLPLAP ATLALLSL