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NDUS2_GORGO
ID   NDUS2_GORGO             Reviewed;         463 AA.
AC   Q0MQG4;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
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; DQ885670; ABH12179.1; -; mRNA.
DR   RefSeq; NP_001266668.1; NM_001279739.1.
DR   AlphaFoldDB; Q0MQG4; -.
DR   SMR; Q0MQG4; -.
DR   STRING; 9593.ENSGGOP00000007564; -.
DR   Ensembl; ENSGGOT00000007766; ENSGGOP00000007564; ENSGGOG00000007729.
DR   GeneID; 101153768; -.
DR   KEGG; ggo:101153768; -.
DR   CTD; 4720; -.
DR   eggNOG; KOG2870; Eukaryota.
DR   GeneTree; ENSGT00390000009529; -.
DR   HOGENOM; CLU_015134_1_1_1; -.
DR   InParanoid; Q0MQG4; -.
DR   OMA; IMGTSME; -.
DR   OrthoDB; 444312at2759; -.
DR   Proteomes; UP000001519; Chromosome 1.
DR   Bgee; ENSGGOG00000007729; Expressed in heart and 6 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: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: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_0000251856"
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;  52558 MW;  25D39B077D5C63A3 CRC64;
     MAALRVLCGL 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
 
 
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