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NDUA8_NEUCR
ID   NDUA8_NEUCR             Reviewed;         183 AA.
AC   P21976; Q7RVL8;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 20.8 kDa subunit;
GN   ORFNames=B1O14.280, NCU02472;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 38-45.
RX   PubMed=2142943; DOI=10.1016/s0021-9258(19)38267-5;
RA   Videira A., Tropschug M., Wachter E., Schneider H., Werner S.;
RT   "Molecular cloning of subunits of complex I from Neurospora crassa. Primary
RT   structure and in vitro expression of a 22-kDa polypeptide.";
RL   J. Biol. Chem. 265:13060-13065(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I), that is believed not to be
CC       involved in catalysis. Complex I functions in the transfer of electrons
CC       from NADH to the respiratory chain. The immediate electron acceptor for
CC       the enzyme is believed to be ubiquinone.
CC   -!- COFACTOR:
CC       Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC         Evidence={ECO:0000305};
CC       Note=Binds 1 iron-sulfur cluster. {ECO:0000305};
CC   -!- SUBUNIT: Complex I is composed of about 40 different subunits. This is
CC       a component of the hydrophobic fraction.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the complex I NDUFA8 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; M55323; AAA33571.1; -; mRNA.
DR   EMBL; BX842631; CAE76413.1; -; Genomic_DNA.
DR   EMBL; CM002236; EAA35830.1; -; Genomic_DNA.
DR   PIR; A36621; A36621.
DR   PIR; T47251; T47251.
DR   RefSeq; XP_965066.1; XM_959973.3.
DR   AlphaFoldDB; P21976; -.
DR   SMR; P21976; -.
DR   STRING; 5141.EFNCRP00000001979; -.
DR   TCDB; 3.D.1.6.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   EnsemblFungi; EAA35830; EAA35830; NCU02472.
DR   GeneID; 3881206; -.
DR   KEGG; ncr:NCU02472; -.
DR   VEuPathDB; FungiDB:NCU02472; -.
DR   HOGENOM; CLU_081931_1_0_1; -.
DR   InParanoid; P21976; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
DR   InterPro; IPR010625; CHCH.
DR   InterPro; IPR016680; NDUFA8.
DR   PANTHER; PTHR13344; PTHR13344; 1.
DR   Pfam; PF06747; CHCH; 1.
DR   PIRSF; PIRSF017016; NDUA8; 1.
DR   PROSITE; PS51808; CHCH; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome; Repeat;
KW   Respiratory chain; Transport.
FT   CHAIN           1..183
FT                   /note="NADH-ubiquinone oxidoreductase 20.8 kDa subunit"
FT                   /id="PRO_0000118736"
FT   DOMAIN          44..87
FT                   /note="CHCH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DOMAIN          88..130
FT                   /note="CHCH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          161..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           47..57
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           69..79
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           91..101
FT                   /note="Cx9C motif 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           112..122
FT                   /note="Cx9C motif 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   COMPBIAS        165..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        47..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        57..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        91..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        101..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   CONFLICT        20
FT                   /note="P -> R (in Ref. 1; AAA33571)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="V -> L (in Ref. 1; AAA33571)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="A -> R (in Ref. 1; AAA33571)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   183 AA;  20753 MW;  45F2F8650B63AAC2 CRC64;
     MASRIPQFNQ QVLYDTTPLP DSIPKVKELG ASSAPLMSAA YFIGARCRDY NDDFMQCKNE
     NPGKGEFECL KEGRRVTRCA RSVIADINKS CLEEFRKHWT CLEDNNQQLW QCRPAEWKLN
     KCVFENLGLK KEIPDQPPNV TPVHLRKQMI YAHWPIPRSA EPFVPPTQTG DNNKAPAAAS
     SSS
 
 
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