ID NDUA9_GORGO Reviewed; 377 AA.
AC Q0MQB3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 24-JAN-2024, entry version 79.
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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16828987; DOI=10.1016/j.gene.2006.03.015;
RA Mishmar D., Ruiz-Pesini E., Mondragon-Palomino M., Procaccio V., Gaut B.,
RA Wallace D.C.;
RT "Adaptive selection of mitochondrial complex I subunits during primate
RT radiation.";
RL Gene 378:11-18(2006).
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. {ECO:0000250|UniProtKB:Q16795}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA9 subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABH12230.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ885721; ABH12230.1; ALT_INIT; mRNA.
DR RefSeq; NP_001266630.1; NM_001279701.1.
DR AlphaFoldDB; Q0MQB3; -.
DR SMR; Q0MQB3; -.
DR STRING; 9593.ENSGGOP00000021812; -.
DR Ensembl; ENSGGOT00000006107.3; ENSGGOP00000005949.3; ENSGGOG00000006076.3.
DR GeneID; 101144771; -.
DR KEGG; ggo:101144771; -.
DR CTD; 4704; -.
DR eggNOG; KOG2865; Eukaryota.
DR GeneTree; ENSGT00390000006865; -.
DR HOGENOM; CLU_007383_6_4_1; -.
DR InParanoid; Q0MQB3; -.
DR OrthoDB; 141210at2759; -.
DR Proteomes; UP000001519; Chromosome 12.
DR Bgee; ENSGGOG00000006076; Expressed in heart and 6 other cell types or tissues.
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:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:1901006; P:ubiquinone-6 biosynthetic process; IBA:GO_Central.
DR CDD; cd05271; NDUFA9_like_SDR_a; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR12126:SF10; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 9, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12126; NADH-UBIQUINONE OXIDOREDUCTASE 39 KDA SUBUNIT-RELATED; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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_0000251810"
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; 42506 MW; 01A82C616F62D942 CRC64;
MAAAAQSRVV RVLSMSRSAI TAIATSVCHG PPCRQLHHAL IPHGKGGRSS VSGIVATVFG
ATGFLGRYVV NHLGRMGSQV IIPYRCDKYD IMHLRPMGDL GQLLFLEWDA RDKDSIRRVV
QHSNVVINLI GRDWETKNFD FEDVFVKIPQ AIAQLSKEAG VEKFIHVSHL NANIKSSSRY
LRNKAVGEKV VRDAFPEAII IKPSDIFGRE DRFLNSFASM HRFGPIPLGS LGWKTVKQPV
YVVDVSKGIV NAVKDPDANG KSFAFVGPSR YLLFHLVKYI FAVAHRLFLP FPLPLFAYRW
VARVFEISPF EPWITRDKVE RMHITDMKLP HLPGLEDLGI QATPLELKAI EVLRRHRTYR
WLSAEIEDVK PAKTVNI
//
