NU2M_FELCA
ID NU2M_FELCA Reviewed; 347 AA.
AC P48905;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Felis catus (Cat) (Felis silvestris catus).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000312|Proteomes:UP000011712}; TISSUE=Blood;
RX PubMed=8660972; DOI=10.1006/geno.1996.0188;
RA Lopez J.V., Cevario S., O'Brien S.J.;
RT "Complete nucleotide sequences of the domestic cat (Felis catus)
RT mitochondrial genome and a transposed mtDNA tandem repeat (Numt) in the
RT nuclear genome.";
RL Genomics 33:229-246(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
RX PubMed=7932781; DOI=10.1007/bf00163806;
RA Lopez J.V., Yuhki N., Masuda R., Modi W., O'Brien S.J.;
RT "Numt, a recent transfer and tandem amplification of mitochondrial DNA to
RT the nuclear genome of the domestic cat.";
RL J. Mol. Evol. 39:174-190(1994).
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; U20753; AAC48570.1; -; Genomic_DNA.
DR EMBL; S75098; AAB32046.1; -; Genomic_DNA.
DR PIR; T11403; T11403.
DR RefSeq; NP_008252.1; NC_001700.1.
DR AlphaFoldDB; P48905; -.
DR SMR; P48905; -.
DR STRING; 9685.ENSFCAP00000025710; -.
DR PRIDE; P48905; -.
DR Ensembl; ENSFCAT00000032637; ENSFCAP00000025710; ENSFCAG00000032052.
DR GeneID; 807935; -.
DR KEGG; fca:807935; -.
DR CTD; 4536; -.
DR VGNC; VGNC:80934; MT-ND2.
DR eggNOG; KOG4668; Eukaryota.
DR GeneTree; ENSGT00730000111348; -.
DR HOGENOM; CLU_007100_1_3_1; -.
DR InParanoid; P48905; -.
DR OMA; HFWVPEV; -.
DR OrthoDB; 1153818at2759; -.
DR Proteomes; UP000011712; Mitochondrion.
DR Bgee; ENSFCAG00000032052; Expressed in uterus and 9 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
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 GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
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_0000117587"
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 149..169
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 242..262
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; 39182 MW; AE1C5E693723B285 CRC64;
MNPPIFIIIM LTVISGTMIV VTTSHWLLVW IGFEMNLLAI IPILMKKYNP RAMEAATKYF
LTQAAASMIL MMWIIINLLH SGQWTVLKDL NPMASIMMTT ALAMKLGLAP FHFWVPEVTQ
GISMSSGLIL LTWQKIAPLS ILYQISSTIN PNLILTMSIL SVMIGGWGGL NQTQLRKIMA
YSSIAHMGWM TAIMMYSPTM MILNLTIYII MTLTTFMLFM HNSTTTTASL SQTWNKTPLI
TSLILVLMMS LGGLPPLSGF IPKWMIIQEL TKNELIMMPT LLAMTALLNL YFYMRLTYTT
ALTMFPSNNS MKMKWRFECT KKMTFLPPLV VMSTMLLPLA PMLSILD
