NU2M_CANLU
ID NU2M_CANLU Reviewed; 347 AA.
AC Q85PR2; Q1HK89; Q1HKA2; Q1HKB5; Q1HKF4; Q3L6Y7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 77.
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 Canis lupus (Gray wolf).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9612;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-6.
RX PubMed=15964215; DOI=10.1016/j.ympev.2005.04.025;
RA Delisle I., Strobeck C.;
RT "A phylogeny of the Caniformia (order Carnivora) based on 12 complete
RT protein-coding mitochondrial genes.";
RL Mol. Phylogenet. Evol. 37:192-201(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-6; VAL-29; ILE-122
RP ILE-162; ALA-195 AND ILE-345.
RX PubMed=16809672; DOI=10.1101/gr.5117706;
RA Bjornerfeldt S., Webster M.T., Vila C.;
RT "Relaxation of selective constraint on dog mitochondrial DNA following
RT domestication.";
RL Genome Res. 16:990-994(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}.
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DR EMBL; AY170044; AAN84578.1; -; Genomic_DNA.
DR EMBL; AY598501; AAU00447.1; -; Genomic_DNA.
DR EMBL; DQ480503; ABE48156.1; -; Genomic_DNA.
DR EMBL; DQ480504; ABE48169.1; -; Genomic_DNA.
DR EMBL; DQ480505; ABE48182.1; -; Genomic_DNA.
DR EMBL; DQ480506; ABE48195.1; -; Genomic_DNA.
DR EMBL; DQ480507; ABE48208.1; -; Genomic_DNA.
DR EMBL; DQ480508; ABE48221.1; -; Genomic_DNA.
DR RefSeq; YP_626729.1; NC_008092.1.
DR AlphaFoldDB; Q85PR2; -.
DR SMR; Q85PR2; -.
DR GeneID; 4097765; -.
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; 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_0000269894"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
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"
FT VARIANT 6
FT /note="L -> F"
FT /evidence="ECO:0000269|PubMed:15964215,
FT ECO:0000269|PubMed:16809672"
FT VARIANT 29
FT /note="I -> V"
FT /evidence="ECO:0000269|PubMed:16809672"
FT VARIANT 122
FT /note="V -> I"
FT VARIANT 162
FT /note="V -> I"
FT /evidence="ECO:0000269|PubMed:16809672"
FT VARIANT 195
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:16809672"
FT VARIANT 345
FT /note="V -> I"
FT /evidence="ECO:0000269|PubMed:16809672"
SQ SEQUENCE 347 AA; 39102 MW; DA70F6890B55DAAE CRC64;
MKPPILIIIM ATIMTGTMIV MLSSHWLLIW IGFEMNMLAI IPILMKKYNP RAMEASTKYF
LTQATASMLL MMGVTINLLY SGQWVISKIS NPIASIMMTT ALTMKLGLSP FHFWVPEVTQ
GVTLMSGMIL LTWQKIAPMS ILYQISPSIN TNLLMLMALT SVLVGGWGGL NQTQLRKIMA
YSSIAHMGWM AAIITYNPTM MILNLTLYIL MTLSTFMLFM LNSSTTTLSL SHMWNKFPLI
TSMILILMLS LGGLPPLSGF IPKWMIIQEL TKNNMIIIPT LMAITALLNL YFYLRLTYST
ALTMFPSTNN MKMKWQFEYT KKATLLPPLI ITSTMLLPLT PMLSVLD
