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NDUS1_MESAU
ID   NDUS1_MESAU             Reviewed;         190 AA.
AC   P86203;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial {ECO:0000250|UniProtKB:P15690};
DE            EC=7.1.1.2 {ECO:0000250|UniProtKB:P28331};
DE   AltName: Full=Complex I-75kD {ECO:0000250|UniProtKB:P15690};
DE            Short=CI-75kD {ECO:0000250|UniProtKB:P15690};
DE   Flags: Fragments;
GN   Name=NDUFS1 {ECO:0000250|UniProtKB:P15690};
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 catalysing the entry and
CC       efficient transfer of electrons within complex I (By similarity). Plays
CC       a key role in the assembly and stability of complex I and participates
CC       in the association of complex I with ubiquinol-cytochrome reductase
CC       complex (Complex III) to form supercomplexes (By similarity).
CC       {ECO:0000250|UniProtKB:P28331}.
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:P28331};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:P29915};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:P29915};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P29915};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit.
CC       {ECO:0000250|UniProtKB:P29915};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits (By similarity). This is
CC       the largest subunit of complex I and it is a component of the iron-
CC       sulfur (IP) fragment of the enzyme (By similarity). Complex I
CC       associates with ubiquinol-cytochrome reductase complex (Complex III) to
CC       form supercomplexes (By similarity). Interacts with MDM2 and AKAP1 (By
CC       similarity). {ECO:0000250|UniProtKB:P15690,
CC       ECO:0000250|UniProtKB:P28331, ECO:0000250|UniProtKB:Q91VD9}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P15690}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P15690}; Matrix side
CC       {ECO:0000250|UniProtKB:P15690}.
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P86203; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; 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:0008137; F:NADH dehydrogenase (ubiquinone) activity; 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.
PE   1: Evidence at protein level;
KW   2Fe-2S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW   Oxidoreductase; Reference proteome; Respiratory chain; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           <1..>190
FT                   /note="NADH-ubiquinone oxidoreductase 75 kDa subunit,
FT                   mitochondrial"
FT                   /id="PRO_0000394295"
FT   NON_CONS        16..17
FT                   /evidence="ECO:0000305"
FT   NON_CONS        36..37
FT                   /evidence="ECO:0000305"
FT   NON_CONS        44..45
FT                   /evidence="ECO:0000305"
FT   NON_CONS        53..54
FT                   /evidence="ECO:0000305"
FT   NON_CONS        67..68
FT                   /evidence="ECO:0000305"
FT   NON_CONS        76..77
FT                   /evidence="ECO:0000305"
FT   NON_CONS        98..99
FT                   /evidence="ECO:0000305"
FT   NON_CONS        137..138
FT                   /evidence="ECO:0000305"
FT   NON_CONS        147..148
FT                   /evidence="ECO:0000305"
FT   NON_CONS        161..162
FT                   /evidence="ECO:0000305"
FT   NON_CONS        180..181
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         190
SQ   SEQUENCE   190 AA;  20736 MW;  B3DC03A97075FA9C CRC64;
     FASEIAGVDD LGTTGRKTES IDVMDAVGSN IVVSTRFAYD GLKRQRLTEP MVRGLLTYTS
     WEDALSRFEA PLFNARVALI GSPVDLTYRY DHLGDSPKIA SQVAALDLGY KPGVEAIRKN
     PPKLLFLLGA DGGCITRSAT YVNTEGRVAV TPPGLAREDW KALSEIAGIT LPYDTLDQVR
     DFYMTDSISR
 
 
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