NDUS2_MESAU
ID NDUS2_MESAU Reviewed; 138 AA.
AC P86250;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial {ECO:0000250|UniProtKB:P17694};
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:Q91WD5};
DE AltName: Full=Complex I-49kD {ECO:0000250|UniProtKB:P17694};
DE Short=CI-49kD {ECO:0000250|UniProtKB:P17694};
DE AltName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit {ECO:0000250|UniProtKB:P17694};
DE Flags: Fragments;
GN Name=NDUFS2 {ECO:0000250|UniProtKB:P17694};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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 Evidence={ECO:0000250|UniProtKB:P17694};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P17694};
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:0000255}.
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DR AlphaFoldDB; P86250; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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 Gene3D; 1.10.645.10; -; 2.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR11993; PTHR11993; 2.
DR Pfam; PF00346; Complex1_49kDa; 2.
DR SUPFAM; SSF56762; SSF56762; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW Reference proteome; Respiratory chain; Translocase; Transport; Ubiquinone.
FT CHAIN <1..138
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 2, mitochondrial"
FT /id="PRO_0000394421"
FT NON_CONS 11..12
FT /evidence="ECO:0000305"
FT NON_CONS 20..21
FT /evidence="ECO:0000305"
FT NON_CONS 29..30
FT /evidence="ECO:0000305"
FT NON_CONS 74..75
FT /evidence="ECO:0000305"
FT NON_CONS 94..95
FT /evidence="ECO:0000305"
FT NON_CONS 115..116
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 138 AA; 15937 MW; 19CF54EF543A6495 CRC64;
TYLQALPYFD RLLNIQPPPR EKMFEFYERM HAAYIRPGGV HQDLPLGLMD DIYEFSKNFS
LRIDEVEEML TNNRKTQPYD VYDQVEFDVP IGSRLYTEGY QVPPGATYTA IEAPKGHMLA
DVVAIIGTQD IVFGEIDR
