NU2M_CHEPA
ID NU2M_CHEPA Reviewed; 347 AA.
AC Q330E6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000250|UniProtKB:P03891};
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P03891};
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=MT-ND2 {ECO:0000250|UniProtKB:P03891}; Synonyms=MTND2, NADH2, ND2;
OS Cheiromeles parvidens (Lesser naked bat) (Sulawesi naked bat).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Molossidae;
OC Cheiromeles.
OX NCBI_TaxID=270769;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate SL1;
RA Worthington Wilmer J.M., Schneider C.J., Sorenson M.D.;
RT "Bats and birds: flying in the face of mtDNA evolutionary rates.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P03891}.
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:0000250|UniProtKB:P03891};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits. Interacts with TMEM242
CC (By similarity). {ECO:0000250|UniProtKB:P03891,
CC ECO:0000250|UniProtKB:P03892}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P03892}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR EMBL; AY504546; AAS91411.1; -; Genomic_DNA.
DR AlphaFoldDB; Q330E6; -.
DR SMR; Q330E6; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
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..347
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000256660"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 347 AA; 38970 MW; F32DBB41D79F3B3C CRC64;
MNPLIMSIIM STIILGTLIV MTSSHWLMIW IGFEMNMLAI IPMLMKHHNP RSTEAATKYF
FTQATASMLL MLAVIINLMY SGQWTGMKLF NPTASIIMTL ALTMKLGLAP FHFWVPEVAQ
GIPLSSGLIL LTWQKLAPLT VLYMISPAIN LYLLLTMSMA SIAIGGWGGL NQTQLRKIMA
YSSIAHMGWM TAILIYNPTM TLLNLVIYIL MTTTMFMLLM INSSTTTLSL SHMWNKMPLI
TTITLVTLLS LGGLPPLTGF LPKWMIIQEL TKNDSIILPT LMAITALLNL FFYMRITYAT
SLTMFPTTNN MKIKWQFENT KHLNLLTPMI VLSTLTLPLA PMMTILN