NDUS2_BOVIN
ID NDUS2_BOVIN Reviewed; 463 AA.
AC P17694; Q0P5K5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 163.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-463, AND PROTEIN SEQUENCE OF 34-55.
RC TISSUE=Heart;
RX PubMed=2498081; DOI=10.1002/j.1460-2075.1989.tb03424.x;
RA Fearnley I.M., Runswick M.J., Walker J.E.;
RT "A homologue of the nuclear coded 49 kd subunit of bovine mitochondrial
RT NADH-ubiquinone reductase is coded in chloroplast DNA.";
RL EMBO J. 8:665-672(1989).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, IDENTIFICATION IN COMPLEX I, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=10852722; DOI=10.1021/bi000335t;
RA Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E.;
RT "Resolution of the membrane domain of bovine complex I into subcomplexes:
RT implications for the structural organization of the enzyme.";
RL Biochemistry 39:7229-7235(2000).
RN [4]
RP PARTIAL PROTEIN SEQUENCE, AND METHYLATION AT ARG-118.
RX PubMed=23836892; DOI=10.1074/jbc.m113.488106;
RA Carroll J., Ding S., Fearnley I.M., Walker J.E.;
RT "Post-translational modifications near the quinone binding site of
RT mammalian complex I.";
RL J. Biol. Chem. 288:24799-24808(2013).
RN [5]
RP SUBUNIT, IDENTIFICATION IN COMPLEX I, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18721790; DOI=10.1016/j.ab.2008.07.029;
RA Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A.,
RA Robinson N.C.;
RT "Subunit analysis of bovine heart complex I by reversed-phase high-
RT performance liquid chromatography, electrospray ionization-tandem mass
RT spectrometry, and matrix-assisted laser desorption/ionization-time-of-
RT flight mass spectrometry.";
RL Anal. Biochem. 382:116-121(2008).
RN [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=25209663; DOI=10.1038/nature13686;
RA Vinothkumar K.R., Zhu J., Hirst J.;
RT "Architecture of mammalian respiratory complex I.";
RL Nature 515:80-84(2014).
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 (PubMed:10852722, PubMed:18721790). Essential for the
CC catalytic activity and assembly of complex I (By similarity). Redox-
CC sensitive, critical component of the oxygen-sensing pathway in the
CC pulmonary vasculature which plays a key role in acute pulmonary oxygen-
CC sensing and hypoxic pulmonary vasoconstriction (By similarity). Plays
CC an important role in carotid body sensing of hypoxia (By similarity).
CC Essential for glia-like neural stem and progenitor cell proliferation,
CC differentiation and subsequent oligodendrocyte or neuronal maturation
CC (By similarity). {ECO:0000250|UniProtKB:Q91WD5,
CC ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}.
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 (PubMed:10852722,
CC PubMed:18721790, PubMed:25209663). Component of the iron-sulfur (IP)
CC fragment of the enzyme (PubMed:25209663). Interacts with NDUFAF3 (By
CC similarity). Interacts with NDUFAF7 (By similarity). Interacts with
CC CERS2 (By similarity). {ECO:0000250|UniProtKB:O75306,
CC ECO:0000250|UniProtKB:Q91WD5, ECO:0000269|PubMed:10852722,
CC ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790,
CC ECO:0000269|PubMed:25209663}; Peripheral membrane protein
CC {ECO:0000305|PubMed:25209663}; Matrix side
CC {ECO:0000305|PubMed:25209663}.
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; BC119924; AAI19925.1; -; mRNA.
DR EMBL; X14338; CAA32523.1; -; mRNA.
DR PIR; S04104; S04104.
DR RefSeq; NP_001068605.1; NM_001075137.1.
DR PDB; 5LC5; EM; 4.35 A; D=38-463.
DR PDB; 5LDW; EM; 4.27 A; D=35-463.
DR PDB; 5LDX; EM; 5.60 A; D=35-463.
DR PDB; 5O31; EM; 4.13 A; D=34-463.
DR PDB; 7QSD; EM; 3.10 A; D=1-463.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P17694; -.
DR SMR; P17694; -.
DR CORUM; P17694; -.
DR DIP; DIP-38816N; -.
DR IntAct; P17694; 3.
DR STRING; 9913.ENSBTAP00000002852; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P17694; -.
DR PRIDE; P17694; -.
DR Ensembl; ENSBTAT00000002852; ENSBTAP00000002852; ENSBTAG00000002203.
DR GeneID; 327697; -.
DR KEGG; bta:327697; -.
DR CTD; 4720; -.
DR VEuPathDB; HostDB:ENSBTAG00000002203; -.
DR VGNC; VGNC:31969; NDUFS2.
DR eggNOG; KOG2870; Eukaryota.
DR GeneTree; ENSGT00390000009529; -.
DR HOGENOM; CLU_015134_1_2_1; -.
DR InParanoid; P17694; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 444312at2759; -.
DR TreeFam; TF300370; -.
DR BRENDA; 7.1.1.2; 908.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000002203; Expressed in cardiac ventricle and 107 other tissues.
DR ExpressionAtlas; P17694; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA: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; IDA: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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Acetylation; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Methylation; Mitochondrion; Mitochondrion inner membrane; NAD;
KW Oxidoreductase; Reference proteome; Respiratory chain; Transit peptide;
KW Translocase; Transport; Ubiquinone.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2498081"
FT CHAIN 34..463
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 2, mitochondrial"
FT /id="PRO_0000118582"
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:0000269|PubMed:23836892"
FT CONFLICT 162
FT /note="Q -> R (in Ref. 2; CAA32523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 52556 MW; 7EE8B22C289EA76F CRC64;
MAALRALCRL RGAAAQVLRP GAGVRLPIQP SRGARQWQPD VEWAEQYGGA VMYPTKETAH
WKPPPWNDVD PPKDTLVSNL TLNFGPQHPA AHGVLRLVME LSGEMVRKCD PHIGLLHRGT
EKLIEYKTYL QALPYFDRLD YVSMMCNEQA YSLAVEKLLN IQPPPRAQWI RVLFGEITRL
LNHIMAVTTH ALDIGAMTPF FWMFEEREKM FEFYERVSGA RMHAAYVRPG GVHQDLPLGL
MDDIYEFSKN FSLRIDELEE MLTNNRIWRN RTVDIGIVTA EDALNYGFSG VMLRGSGIQW
DLRKTQPYDV YDQVEFDVPI GSRGDCYDRY LCRVEEMRQS IRIISQCLNK MPPGEIKVDD
AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI EAPKGEFGVY LVSDGSSRPY
RCKIKAPGFA HLAGLDKMSK GHMLADVVAI IGTQDIVFGE VDR
