ID   NDUA8_PONAB             Reviewed;         172 AA.
AC   P0CB91; Q5RA56;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;
DE   AltName: Full=Complex I-19kD;
DE            Short=CI-19kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 19 kDa subunit;
GN   Name=NDUFA8;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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:0000250|UniProtKB:P51970}.
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC       {ECO:0000250|UniProtKB:P51970}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P51970}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P51970}. Mitochondrion intermembrane space
CC       {ECO:0000250|UniProtKB:P51970}. Mitochondrion
CC       {ECO:0000250|UniProtKB:P51970}.
CC   -!- DOMAIN: Contains four C-X9-C motifs that are predicted to form a helix-
CC       coil-helix structure, permitting the formation of intramolecular
CC       disulfide bonds. {ECO:0000250|UniProtKB:P51970}.
CC   -!- SIMILARITY: Belongs to the complex I NDUFA8 subunit family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR859165; CAH91354.1; -; mRNA.
DR   RefSeq; NP_001125798.1; NM_001132326.1.
DR   AlphaFoldDB; P0CB91; -.
DR   SMR; P0CB91; -.
DR   STRING; 9601.ENSPPYP00000022282; -.
DR   Ensembl; ENSPPYT00000043806; ENSPPYP00000027772; ENSPPYG00000038544.
DR   GeneID; 100172726; -.
DR   KEGG; pon:100172726; -.
DR   CTD; 4702; -.
DR   eggNOG; KOG3458; Eukaryota.
DR   GeneTree; ENSGT00390000008938; -.
DR   InParanoid; P0CB91; -.
DR   OrthoDB; 1526152at2759; -.
DR   Proteomes; UP000001595; Chromosome 9.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Disulfide bond; Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Repeat;
KW   Respiratory chain; Transport.
FT   CHAIN           1..172
FT                   /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT                   subunit 8"
FT                   /id="PRO_0000250707"
FT   DOMAIN          33..74
FT                   /note="CHCH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DOMAIN          75..118
FT                   /note="CHCH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          133..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           36..46
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           56..66
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           78..88
FT                   /note="Cx9C motif 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           100..110
FT                   /note="Cx9C motif 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        36..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        46..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        78..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        88..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   172 AA;  20135 MW;  E1656F5BB783E349 CRC64;
     MPGIVELPTL EELKVDEVKI SSAVLKAAAH HYGAQCDKPN KEFMLCRWEE KDPRRCLEEG
     KLVNKCALDF FRQIKRHCAE PFTEYWTCID YTGQQLFRHC RKQQAKFDEC VLDKMGWVRP
     DLGELSKVTK VKTDRPLPEN PYHSRPRPDP SPEIEGDLKP AIHGSRFYFW TK