NU2M_MAMPR
ID NU2M_MAMPR Reviewed; 347 AA.
AC Q38PS1; Q2I3I6;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 59.
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 Mammuthus primigenius (Siberian woolly mammoth).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Mammuthus.
OX NCBI_TaxID=37349;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16362058; DOI=10.1038/nature04432;
RA Krause J., Dear P.H., Pollack J.L., Slatkin M., Spriggs H., Barnes I.,
RA Lister A.M., Ebersberger I., Paeaebo S., Hofreiter M.;
RT "Multiplex amplification of the mammoth mitochondrial genome and the
RT evolution of Elephantidae.";
RL Nature 439:724-727(2006).
RN [2]
RP SEQUENCE REVISION TO 199; 231; 256; 265; 279 AND 300.
RA Krause J., Dear P.H., Pollack J.L., Slatkin M., Spriggs H., Barnes I.,
RA Lister A.M., Paabo S., Hofreiter M.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Muscle;
RX PubMed=16448217; DOI=10.1371/journal.pbio.0040073;
RA Rogaev E.I., Moliaka Y.K., Malyarchuk B.A., Kondrashov F.A., Derenko M.V.,
RA Chumakov I., Grigorenko A.P.;
RT "Complete mitochondrial genome and phylogeny of Pleistocene mammoth
RT Mammuthus primigenius.";
RL PLoS Biol. 4:403-410(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ188829; ABA29785.2; -; Genomic_DNA.
DR EMBL; DQ316067; ABC17879.1; -; Genomic_DNA.
DR RefSeq; YP_398755.2; NC_007596.2.
DR AlphaFoldDB; Q38PS1; -.
DR SMR; Q38PS1; -.
DR GeneID; 3773142; -.
DR CTD; 4536; -.
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; Extinct organism protein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Respiratory chain; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..347
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000232849"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 319
FT /note="S -> N (in Ref. 3; ABC17879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38913 MW; F136E495C73C8923 CRC64;
MNPLALSLIL TTLLAGTLIT MMSSHWLTAW MGLEMNMLTM IPILMKTTNP RSTEAATKYF
MTQATASMML MMALTINLMY SGQWSIMKMT NPVASNVALM ALMTKLGSAP FHFWVPEVTQ
GVELTSGMIL LTWQKLAPLS LLYQMATYTN TNLIYLSGLL SILIGGWGGL NQTQLRKILA
YSSISHMGWM LIILPFNPTL TLLNLAIYIL LTLSIFMILA NTLTTSMSSL TLMWNKTPAM
TIMLMTTLLS LGGLPPLSGF TPKWLMIHEL TKNNSIIMPL TMAIMTLLNM YFYMRLIYYS
SLTILPSTNN MKMTWQFTST KHTMMLPTLI TLSNMLLPLT PMISMLE
