NDUS2_RAT
ID NDUS2_RAT Reviewed; 463 AA.
AC Q641Y2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;
DE EC=7.1.1.2 {ECO:0000269|PubMed:30922174};
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 {ECO:0000312|EMBL:AAH82067.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH82067.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15489334};
RC TISSUE=Testis {ECO:0000312|EMBL:AAH82067.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=30922174; DOI=10.1161/circresaha.118.314284;
RA Dunham-Snary K.J., Wu D., Potus F., Sykes E.A., Mewburn J.D., Charles R.L.,
RA Eaton P., Sultanian R.A., Archer S.L.;
RT "Ndufs2, a Core Subunit of Mitochondrial Complex I, Is Essential for Acute
RT Oxygen-Sensing and Hypoxic Pulmonary Vasoconstriction.";
RL Circ. Res. 124:1727-1746(2019).
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:30922174). Essential for the catalytic activity of
CC complex I (PubMed:30922174). Essential for the assembly of complex I
CC (By similarity). Redox-sensitive, critical component of the oxygen-
CC sensing pathway in the pulmonary vasculature which plays a key role in
CC acute pulmonary oxygen-sensing and hypoxic pulmonary vasoconstriction
CC (PubMed:30922174). Plays an important role in carotid body sensing of
CC hypoxia (By similarity). Essential for glia-like neural stem and
CC progenitor cell proliferation, differentiation and subsequent
CC oligodendrocyte or neuronal maturation (By similarity).
CC {ECO:0000250|UniProtKB:Q91WD5, ECO:0000269|PubMed:30922174}.
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:0000269|PubMed:30922174};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
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:0000269|PubMed:30922174}; Peripheral membrane protein
CC {ECO:0000305|PubMed:30922174}; Matrix side
CC {ECO:0000269|PubMed:30922174}.
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:0000255}.
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DR EMBL; BC082067; AAH82067.1; -; mRNA.
DR RefSeq; NP_001011907.1; NM_001011907.1.
DR RefSeq; XP_003751325.1; XM_003751277.3.
DR AlphaFoldDB; Q641Y2; -.
DR SMR; Q641Y2; -.
DR BioGRID; 252831; 2.
DR IntAct; Q641Y2; 1.
DR MINT; Q641Y2; -.
DR STRING; 10116.ENSRNOP00000055224; -.
DR iPTMnet; Q641Y2; -.
DR PhosphoSitePlus; Q641Y2; -.
DR World-2DPAGE; 0004:Q641Y2; -.
DR jPOST; Q641Y2; -.
DR PaxDb; Q641Y2; -.
DR PRIDE; Q641Y2; -.
DR Ensembl; ENSRNOT00000058423; ENSRNOP00000055224; ENSRNOG00000038372.
DR GeneID; 289218; -.
DR KEGG; rno:289218; -.
DR UCSC; RGD:1307109; rat.
DR CTD; 4720; -.
DR RGD; 1307109; Ndufs2.
DR eggNOG; KOG2870; Eukaryota.
DR GeneTree; ENSGT00390000009529; -.
DR HOGENOM; CLU_015134_1_1_1; -.
DR InParanoid; Q641Y2; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 444312at2759; -.
DR PhylomeDB; Q641Y2; -.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR Reactome; R-RNO-6799198; Complex I biogenesis.
DR PRO; PR:Q641Y2; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000038372; Expressed in heart and 20 other tissues.
DR Genevisible; Q641Y2; RN.
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: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; ISO:RGD.
DR GO; GO:0019826; F:oxygen sensor activity; IMP:UniProtKB.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0071453; P:cellular response to oxygen levels; IMP:UniProtKB.
DR GO; GO:0042063; P:gliogenesis; ISS:UniProtKB.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISO:RGD.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP: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; ISO:RGD.
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 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_0000342702"
FT BINDING 326
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT BINDING 332
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
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; 52562 MW; B9919E581C229C19 CRC64;
MAALRAVCSL RGVGAQVLRA GSGIRLPSQP SRGARRWQPD IEWAEQFSGA VMYPSKETAH
WKPPPWNDVD VLKEKVVTNV TLNFGPQHPA AHGVLRLVLE LSGEMVRKCD PHIGLLHRGT
EKLIEYKTYL QALPYFDRLD YVSMMCNEQA YSLAVEKLLN IQPPPRAQWI RVLFGEITRI
LNHIMAVTTH ALDIGAMTPF FWMFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL
MDDIYEFSKN FSLRIDEVEE MLTNNRIWRN RTVDIGVVSA EDALNYGFSG VMLRGSGIQW
DLRKTQPYDV YDQVEFDVPI GSRGDCYDRY LCRVEEMRQS LRIIEQCLNK MPPGEIKVDD
AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI EAPKGEFGVY LVSDGSSRPY
RCKIKAPGFA HLAGLDKMSK GHMLADVVAI IGTQDIVFGE IDR
