ID   NDUA9_PONAB             Reviewed;         377 AA.
AC   P0CB81; Q0MQB2; Q5R5S0;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;
DE   AltName: Full=Complex I-39kD;
DE            Short=CI-39kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 39 kDa subunit;
DE   Flags: Precursor;
GN   Name=NDUFA9;
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=Brain cortex;
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:Q16795}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits (By
CC       similarity). This a component of the hydrophobic protein fraction (By
CC       similarity). Interacts with BLOC1S1 (By similarity). Interacts with
CC       SLC2A4 (By similarity). Interacts with CLOCK (By similarity). Interacts
CC       with RAB5IF (By similarity). {ECO:0000250|UniProtKB:Q16795,
CC       ECO:0000250|UniProtKB:Q5BK63}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q16795}.
CC   -!- PTM: Acetylated on lysine residues. BLOC1S1 is required for
CC       acetylation. Acetylated by CLOCK in a circadian manner.
CC       {ECO:0000250|UniProtKB:Q16795}.
CC   -!- SIMILARITY: Belongs to the complex I NDUFA9 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CR860786; CAH92896.1; -; mRNA.
DR   RefSeq; NP_001127602.1; NM_001134130.1.
DR   AlphaFoldDB; P0CB81; -.
DR   SMR; P0CB81; -.
DR   STRING; 9601.ENSPPYP00000004753; -.
DR   Ensembl; ENSPPYT00000004941; ENSPPYP00000004753; ENSPPYG00000004171.
DR   GeneID; 100174681; -.
DR   KEGG; pon:100174681; -.
DR   CTD; 4704; -.
DR   eggNOG; KOG2865; Eukaryota.
DR   GeneTree; ENSGT00390000006865; -.
DR   InParanoid; P0CB81; -.
DR   OrthoDB; 721605at2759; -.
DR   Proteomes; UP000001595; Chromosome 12.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Electron transport; FAD; Flavoprotein; Mitochondrion;
KW   Reference proteome; Respiratory chain; Transit peptide; Transport.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           36..377
FT                   /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT                   subunit 9, mitochondrial"
FT                   /id="PRO_0000234301"
FT   MOD_RES         175
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DC69"
FT   MOD_RES         189
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DC69"
FT   MOD_RES         370
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DC69"
SQ   SEQUENCE   377 AA;  42575 MW;  32DA35F1EFC20AB6 CRC64;
     MAAAAQSRVV RVLSMSRSAI TAIATSVCHG PPRRQLHHAL IPHGKGGRSS VSGIVATVFG
     ATGFLGRYVV NHLGRMGSQV IIPYRCDTYD IMHLRPMGDL GQLLFLEWDA RDKDSIRRVV
     QHSNVVINLI GRDWETRNFD FEDVFVKIPQ AIAQLSKEAG VEKFIHVSHL NANIKSSSRY
     LRNKAVGEKV VRDAFPEAII IKPSDIFGRE DRFLNSFASM HRFGPTPLGS LGWKTVKQPV
     YVVDVSKGIV NAVKDPDANG KSFAFVGPNR YLLFHLVKYI FAVAHRLFLP FPLPLFAYRW
     VARVFEISPF EPWITRDKVE RMHITDMKLP HLPGLEDLGI QATPLELKAI EVLRRHRTYR
     WLSAEIEDVK PAKTVNI