ID A0A2U9CEY2_SCOMX Unreviewed; 172 AA.
AC A0A2U9CEY2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 {ECO:0000256|ARBA:ARBA00016384, ECO:0000256|PIRNR:PIRNR017016};
GN ORFNames=SMAX5B_003581 {ECO:0000313|EMBL:AWP15151.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP15151.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP15151.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|PIRNR:PIRNR017016}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|PIRNR:PIRNR017016}. Mitochondrion intermembrane space
CC {ECO:0000256|ARBA:ARBA00004569}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA8 subunit family.
CC {ECO:0000256|ARBA:ARBA00010705, ECO:0000256|PIRNR:PIRNR017016}.
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DR EMBL; CP026258; AWP15151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CEY2; -.
DR STRING; 52904.ENSSMAP00000032906; -.
DR OMA; RQVNQCA; -.
DR OrthoDB; 1327569at2759; -.
DR Proteomes; UP000246464; Chromosome 16.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
DR InterPro; IPR010625; CHCH.
DR InterPro; IPR016680; NDUFA8.
DR PANTHER; PTHR13344:SF0; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 8; 1.
DR PANTHER; PTHR13344; NADH-UBIQUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF06747; CHCH; 1.
DR PIRSF; PIRSF017016; NDUA8; 1.
DR PROSITE; PS51808; CHCH; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR017016}; Membrane {ECO:0000256|PIRNR:PIRNR017016};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|PIRNR:PIRNR017016};
KW Mitochondrion inner membrane {ECO:0000256|PIRNR:PIRNR017016};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|PIRNR:PIRNR017016};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR017016}.
FT DOMAIN 78..111
FT /note="CHCH"
FT /evidence="ECO:0000259|Pfam:PF06747"
FT REGION 137..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 172 AA; 19751 MW; D4BA63D8546F7C24 CRC64;
MPSTVELPTA QELKVDEVNV SSAVLKAAAH HFGSQCDKAN KEFMLCRWEE KDPRKCIEEG
RKVNECALNF FRQIKGNCAE SFTEYWTCLD YSNLAELRHC RKPQQAFDSC VLDKLGWERP
ALGDLSKVTK VATVRPLPEN PYHSRPRPEP NPTIEGKLEP SKHGSRLFFW SW
//
