ID   NURM_NEUCR              Reviewed;         186 AA.
AC   P42116; Q7SGF3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 120.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 17.8 kDa subunit, mitochondrial;
DE            EC=7.1.1.2;
DE   AltName: Full=Complex I-17.8kD;
DE            Short=CI-17.8kD;
DE   Flags: Precursor;
GN   Name=nuo17.8; ORFNames=B20J13.200, NCU00969;
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, AND PROTEIN SEQUENCE OF 27-45.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=8343129; DOI=10.1042/bj2930501;
RA   Azevedo J.E., Abrolat-Scharff J., Eckerskorn C., Werner S.;
RT   "Cloning, in vitro mitochondrial import and membrane assembly of the 17.8
RT   kDa subunit of complex I from Neurospora crassa.";
RL   Biochem. J. 293:501-506(1993).
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: Transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone.
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   -!- SUBUNIT: Complex I is composed of about 40 different subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
CC       membrane protein.
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DR   EMBL; X71414; CAA50537.1; -; mRNA.
DR   EMBL; BX842629; CAE76339.1; -; Genomic_DNA.
DR   EMBL; CM002236; EAA35926.1; -; Genomic_DNA.
DR   PIR; S35057; S35057.
DR   RefSeq; XP_965162.1; XM_960069.3.
DR   AlphaFoldDB; P42116; -.
DR   SMR; P42116; -.
DR   STRING; 367110.P42116; -.
DR   PaxDb; 5141-EFNCRP00000000759; -.
DR   EnsemblFungi; EAA35926; EAA35926; NCU00969.
DR   GeneID; 3881298; -.
DR   KEGG; ncr:NCU00969; -.
DR   VEuPathDB; FungiDB:NCU00969; -.
DR   HOGENOM; CLU_095735_0_1_1; -.
DR   InParanoid; P42116; -.
DR   OrthoDB; 2714228at2759; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   InterPro; IPR034444; Nuo17.8.
DR   PANTHER; PTHR42100; OXIDOREDUCTASE 178 KDA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04320)-RELATED; 1.
DR   PANTHER; PTHR42100:SF1; OXIDOREDUCTASE 178 KDA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04320)-RELATED; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW   Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW   Ubiquinone.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:8343129"
FT   CHAIN           27..186
FT                   /note="NADH-ubiquinone oxidoreductase 17.8 kDa subunit,
FT                   mitochondrial"
FT                   /id="PRO_0000020040"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          22..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   186 AA;  20895 MW;  6A3E738708D37EEE CRC64;
     MSSFRLGVSR VARQVRAPCV RNTRRYASDS HAPADHTHSA AGHGEHHHAN AADANEELGT
     AFYVIFGAIP AFGALYYFSR PGKDGQPNSI TKWLQKWEEH QEALADKNAL VTAALEQAAH
     DKHLFYYVDQ LRSGHYEMKY PEVFQHGSAR NVPAGTYIPL DKVVEVYRKQ HLDEEERKAK
     KLAAAN
//