NDUS2_PANTR
ID NDUS2_PANTR Reviewed; 463 AA.
AC Q0MQG5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:Q91WD5};
DE AltName: Full=Complex I-49kD;
DE Short=CI-49kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit;
DE Flags: Precursor;
GN Name=NDUFS2;
OS Pan troglodytes (Chimpanzee).
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 [MRNA].
RX PubMed=16828987; DOI=10.1016/j.gene.2006.03.015;
RA Mishmar D., Ruiz-Pesini E., Mondragon-Palomino M., Procaccio V., Gaut B.,
RA Wallace D.C.;
RT "Adaptive selection of mitochondrial complex I subunits during primate
RT radiation.";
RL Gene 378:11-18(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 (By similarity). Essential for the catalytic activity and
CC assembly of complex I (By similarity). Redox-sensitive, critical
CC component of the oxygen-sensing pathway in the pulmonary vasculature
CC which plays a key role in acute pulmonary oxygen-sensing and hypoxic
CC pulmonary vasoconstriction (By similarity). Plays an important role in
CC carotid body sensing of hypoxia (By similarity). Essential for glia-
CC like neural stem and progenitor cell proliferation, differentiation and
CC subsequent oligodendrocyte or neuronal maturation (By similarity).
CC {ECO:0000250|UniProtKB:Q91WD5}.
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:Q91WD5};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster.;
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits. Component of the iron-
CC sulfur (IP) fragment of the enzyme. Interacts with NDUFAF3. Interacts
CC with NDUFAF7 (By similarity). Interacts with CERS2 (By similarity).
CC {ECO:0000250|UniProtKB:O75306, ECO:0000250|UniProtKB:Q91WD5}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q641Y2}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q641Y2}; Matrix side
CC {ECO:0000250|UniProtKB:Q641Y2}.
CC -!- PTM: Dimethylation at Arg-118 by NDUFAF7 takes place after NDUFS2
CC assembles into the complex I, leading to stabilize the early
CC intermediate complex. {ECO:0000250|UniProtKB:O75306}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; DQ885669; ABH12178.1; -; mRNA.
DR RefSeq; NP_001065294.1; NM_001071826.1.
DR RefSeq; XP_009432179.1; XM_009433904.1.
DR RefSeq; XP_009432189.1; XM_009433914.1.
DR AlphaFoldDB; Q0MQG5; -.
DR SMR; Q0MQG5; -.
DR STRING; 9598.ENSPTRP00000002642; -.
DR PaxDb; Q0MQG5; -.
DR Ensembl; ENSPTRT00000002879; ENSPTRP00000002642; ENSPTRG00000001577.
DR GeneID; 747334; -.
DR KEGG; ptr:747334; -.
DR CTD; 4720; -.
DR VGNC; VGNC:8078; NDUFS2.
DR eggNOG; KOG2870; Eukaryota.
DR GeneTree; ENSGT00390000009529; -.
DR HOGENOM; CLU_015134_1_1_1; -.
DR InParanoid; Q0MQG5; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 444312at2759; -.
DR TreeFam; TF300370; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000001577; Expressed in heart and 20 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR GO; GO:0019826; F:oxygen sensor activity; ISS:UniProtKB.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0071453; P:cellular response to oxygen levels; ISS:UniProtKB.
DR GO; GO:0042063; P:gliogenesis; 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:0061351; P:neural precursor cell proliferation; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR Gene3D; 1.10.645.10; -; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR11993; PTHR11993; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR TIGRFAMs; TIGR01962; NuoD; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Acetylation; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Methylation; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Oxidoreductase; Reference proteome; Respiratory chain;
KW Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P17694"
FT CHAIN 34..463
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 2, mitochondrial"
FT /id="PRO_0000251857"
FT BINDING 326
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 332
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91WD5"
FT MOD_RES 118
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P17694"
SQ SEQUENCE 463 AA; 52564 MW; 5B3882F1A57448EC CRC64;
MAALRALCGF RGVAAQVLRP GAGVRLPIQP SRGVRQWQPD VEWAQQFGGA VMYPSKETAH
WKPPPWNDVD PPKDTIVKNM TLNFGPQHPA AHGVLRLVME LSGEMVRKCD PHIGLLHRGT
EKLIEYKTYL QALPYFDRLD YVSMMCNEQA YSLAVEKLLN IRPPPRAQWI RVLFGEITRL
LNHIMAVTTH ALDLGAMTPF FWLFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL
MDDIYQFSKN FSLRLDELEE LLTNNRIWRN RTIDIGVVTA EEALNYGFSG VMLRGSGIQW
DLRKTQPYDV YDQVEFDVPV GSRGDCYDRY LCRVEEMRQS LRIIAQCLNK MPPGEIKVDD
AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI EAPKGEFGVY LVSDGSSRPY
RCKIKAPGFA HLAGLDKMSK GHMLADVVAI IGTQDIVFGE VDR
