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 24-JAN-2024, entry version 108. 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}. 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; 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; 9598-ENSPTRP00000002642; -. DR Ensembl; ENSPTRT00000002879.5; ENSPTRP00000002642.4; ENSPTRG00000001577.5. 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; 191at2759; -. DR TreeFam; TF300370; -. DR Proteomes; UP000002277; Chromosome 1. DR Bgee; ENSPTRG00000001577; Expressed in heart and 20 other cell types or 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; Cytochrome-c3 Hydrogenase, chain B; 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 NCBIfam; TIGR01962; NuoD; 1. DR PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1. DR PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1. DR Pfam; PF00346; Complex1_49kDa; 1. DR SUPFAM; SSF56762; HydB/Nqo4-like; 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 //