NU2M_PARHE
ID NU2M_PARHE Reviewed; 347 AA.
AC Q85PQ0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 65.
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 Paradoxurus hermaphroditus (Asian palm civet).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Viverridae; Paradoxurinae;
OC Paradoxurus.
OX NCBI_TaxID=71117;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12610623; DOI=10.1038/nature01303;
RA Yoder A.D., Burns M.M., Zehr S., Delefosse T., Veron G., Goodman S.M.,
RA Flynn J.J.;
RT "Single origin of Malagasy Carnivora from an African ancestor.";
RL Nature 421:734-737(2003).
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; AY170056; AAN84590.1; -; Genomic_DNA.
DR AlphaFoldDB; Q85PQ0; -.
DR SMR; Q85PQ0; -.
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_0000117619"
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 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
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 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; 39143 MW; F81344319D06E0F9 CRC64;
MKPPILIIIM STVISGTMIV LTSSHWMLTW IGFEMNMLAV IPILMKKFNP RAMEASTKYF
LMQATASMLL MMGITINLLH TGQWTILNNL NPTASTLMTI ALAMKLGLAP FHFWVPEVTQ
GISLSSGMIL LTWQKIAPLS VLYQISPNIN PKLLLLMAIL SVLIGGWGGL NQTQLRKILA
YSSIAHMGWM STILIYNPTM MLLNLIIYIM MTLSTFMLFM HNSTTTTLAL SQTWNKMPLI
TSLILMLMLS LGGLPPLSGF IPKWMIIQEL TKNEMIIMPT FLAITALLNL YFYMRLTYAT
ALTMFPSTNN MKMKWQFENT KKTMFLPPLI VMSTMLIPLT PIISILE