NU2M_PANTR
ID NU2M_PANTR Reviewed; 347 AA.
AC O21798; Q9T9W2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 113.
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 Pan troglodytes (Chimpanzee).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-94.
RX PubMed=9475751; DOI=10.1093/genetics/148.1.409;
RA Wise C.A., Sraml M., Easteal S.;
RT "Departure from neutrality at the mitochondrial NADH dehydrogenase subunit
RT 2 gene in humans, but not in chimpanzees.";
RL Genetics 148:409-421(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-94.
RX PubMed=7530363; DOI=10.1073/pnas.92.2.532;
RA Horai S., Hayasaka K., Kondo R., Tsugane K., Takahata N.;
RT "Recent African origin of modern humans revealed by complete sequences of
RT hominoid mitochondrial DNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:532-536(1995).
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; AF014908; AAC25467.1; -; Genomic_DNA.
DR EMBL; AF014909; AAC25468.1; -; Genomic_DNA.
DR EMBL; AF014910; AAC25469.1; -; Genomic_DNA.
DR EMBL; AF014911; AAC25470.1; -; Genomic_DNA.
DR EMBL; AF014912; AAC25471.1; -; Genomic_DNA.
DR EMBL; AF014913; AAC25472.1; -; Genomic_DNA.
DR EMBL; AF014914; AAC25473.1; -; Genomic_DNA.
DR EMBL; AF014915; AAC25474.1; -; Genomic_DNA.
DR EMBL; AF014916; AAC25475.1; -; Genomic_DNA.
DR EMBL; AF014917; AAC25476.1; -; Genomic_DNA.
DR EMBL; AF014918; AAC25477.1; -; Genomic_DNA.
DR EMBL; AF014919; AAC25478.1; -; Genomic_DNA.
DR EMBL; AF014920; AAC25479.1; -; Genomic_DNA.
DR EMBL; AF014921; AAC25480.1; -; Genomic_DNA.
DR EMBL; D38113; BAA85269.1; -; Genomic_DNA.
DR RefSeq; NP_008187.1; NC_001643.1.
DR AlphaFoldDB; O21798; -.
DR SMR; O21798; -.
DR STRING; 9598.ENSPTRP00000061406; -.
DR PaxDb; O21798; -.
DR GeneID; 807865; -.
DR KEGG; ptr:807865; -.
DR CTD; 4536; -.
DR eggNOG; KOG4668; Eukaryota.
DR InParanoid; O21798; -.
DR OrthoDB; 1153818at2759; -.
DR Proteomes; UP000002277; 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_0000117617"
FT TRANSMEM 13..33
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 123..143
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 247..267
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 VARIANT 94
FT /note="P -> S (in strain: Isolate A-292)"
FT /evidence="ECO:0000269|PubMed:7530363,
FT ECO:0000269|PubMed:9475751"
FT /id="VAR_018716"
FT CONFLICT 14
FT /note="F -> L (in Ref. 2; BAA85269)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="T -> I (in Ref. 2; AAC25469/AAC25472/AAC25476/
FT AAC25479/BAA85269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 39020 MW; 2E8269D105810D4E CRC64;
MNPLAQPIIY STIFTGTLIT ALSSHWFFTW VGLEMNMLAF IPILTKKMSP RSTEAATKYF
LTQATASMIL LMAILSNSML SGQWTMTNTT NQYPSLMIMM AMAMKLGMAP FHFWVPEVTQ
GTPLMSGLLL LTWQKLAPIS IMYQISSSLN VNLLLTLSIL SIMAGSWGGL NQTQLRKILA
YSSITHMGWM MAVLPYNPNM TILNLTIYII LTTTAFLLLN LNSSTTTLLL SRTWNKLTWL
TPLIPSTLLS LGGLPPLTGF LPKWVIIEEF TKNNSLIIPT IMAIITLLNL YFYLRLIYST
SITLLPMSNN VKMKWQFEHT KPTPFLPTLI TLTTLLLPIS PFMLMIL
