NU2M_AILME
ID NU2M_AILME Reviewed; 347 AA.
AC Q534B1; A5JFJ7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
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 Ailuropoda melanoleuca (Giant panda).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16012099; DOI=10.1080/10635150590923326;
RA Flynn J.J., Finarelli J.A., Zehr S., Hsu J., Nedbal M.A.;
RT "Molecular phylogeny of the Carnivora (Mammalia): assessing the impact of
RT increased sampling on resolving enigmatic relationships.";
RL Syst. Biol. 54:317-337(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17499457; DOI=10.1016/j.gene.2007.04.009;
RA Peng R., Zeng B., Meng X., Yue B., Zhang Z., Zou F.;
RT "The complete mitochondrial genome and phylogenetic analysis of the giant
RT panda (Ailuropoda melanoleuca).";
RL Gene 397:76-83(2007).
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; AY750642; AAW83866.1; -; Genomic_DNA.
DR EMBL; EF212882; ABP38211.1; -; Genomic_DNA.
DR RefSeq; YP_001249285.1; NC_009492.1.
DR AlphaFoldDB; Q534B1; -.
DR SMR; Q534B1; -.
DR STRING; 9646.ENSAMEP00000021354; -.
DR GeneID; 5179725; -.
DR KEGG; aml:5179725; -.
DR CTD; 4536; -.
DR eggNOG; KOG4668; Eukaryota.
DR HOGENOM; CLU_007100_1_3_1; -.
DR InParanoid; Q534B1; -.
DR OMA; HFWVPEV; -.
DR OrthoDB; 1153818at2759; -.
DR TreeFam; TF343996; -.
DR Proteomes; UP000008912; Mitochondrion.
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; Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..347
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117539"
FT TRANSMEM 5..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
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"
FT CONFLICT 10
FT /note="T -> M (in Ref. 1; AAW83866)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="E -> K (in Ref. 1; AAW83866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38755 MW; 0D0303473B6867CE CRC64;
MKPAILITIT STVVLGTMIV LFSSHWFMIW VGFEMNMLAI IPILMKKYNP RAMEASTKYF
LTQATASMLL MLSIIINLLC SGHWTVSTIP NPVASTMITI ALTMKLGLSP FHFWVPEVTQ
GISLSSGMIL LTWQKIAPLS ILYQISPSVN SNLLLMMAIT SMLVGGWGGL NQTQLRKILA
YSSITHMGWM AAIMVYNPTL AILNLTIYIM MTLGTFMLFM HSSSTTTLSL SYTWNKFPLM
APLILMLMLS LGGLPPLSGF IPKWMIIQEL TKNDMIIMPT LMAITALLNL YFYTRLTYTT
ALTMFPATNN MKMKWQFETT KKTTLLAPLI VTSTMLLPLT PMLAALD
