GenomeNet

Database: UniProt
Entry: P0CB98
LinkDB: P0CB98
Original site: P0CB98 
ID   NDUS8_PONPY             Reviewed;         210 AA.
AC   P0CB98; Q0MQI1; Q5RC57;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   05-DEC-2018, entry version 44.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;
DE            EC=1.6.99.3;
DE            EC=7.1.1.2;
DE   AltName: Full=Complex I-23kD;
DE            Short=CI-23kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit;
DE   Flags: Precursor;
GN   Name=NDUFS8;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9600;
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.,
RA   Gaut B., 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
CC       chain NADH dehydrogenase (Complex I) that is believed to belong to
CC       the minimal assembly required for catalysis. Complex I functions
CC       in the transfer of electrons from NADH to the respiratory chain.
CC       The immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4
CC         H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565,
CC         Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389,
CC         ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=7.1.1.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + H(+) + NADH = AH2 + NAD(+); Xref=Rhea:RHEA:11356,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.99.3;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits This is a
CC       component of the iron-sulfur (IP) fragment of the enzyme.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC       {ECO:0000305}.
DR   EMBL; DQ885653; ABH12162.1; -; mRNA.
DR   ProteinModelPortal; P0CB98; -.
DR   SMR; P0CB98; -.
DR   HOGENOM; HOG000228289; -.
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:0003954; F:NADH dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR   HAMAP; MF_01351; NDH1_NuoI; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR   PANTHER; PTHR10849; PTHR10849; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   TIGRFAMs; TIGR01971; NuoI; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Mitochondrion; NAD; Oxidoreductase; Repeat; Respiratory chain;
KW   Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT       1     34       Mitochondrion. {ECO:0000250}.
FT   CHAIN        35    210       NADH dehydrogenase [ubiquinone] iron-
FT                                sulfur protein 8, mitochondrial.
FT                                /FTId=PRO_0000389267.
FT   DOMAIN      102    131       4Fe-4S ferredoxin-type 1.
FT   DOMAIN      141    170       4Fe-4S ferredoxin-type 2.
FT   METAL       111    111       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       114    114       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       117    117       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       121    121       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       150    150       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       153    153       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       156    156       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       160    160       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   210 AA;  23705 MW;  8C3EBD205BFA0112 CRC64;
     MRCLTTPMLL RALAQAARAG PPGGRSLHSS AVAATYKYVN MQDPEMDMKS VTDRAARTLL
     WTELFRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAI
     CPAQAITIEA EPRADGSRRT TRYDIDMTKC IYCGFCQEAC PVDAIVEGPN FEFSTETHEE
     LLYNKEKLLN NGDKWEAEIA ANIQADYLYR
//
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