ID   NDUA9_RAT               Reviewed;         377 AA.
AC   Q5BK63; B5DER7;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   24-JAN-2024, entry version 125.
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   AltName: Full=Sperm flagella protein 3;
DE   Flags: Precursor;
GN   Name=Ndufa9 {ECO:0000312|EMBL:AAH91192.1, ECO:0000312|RGD:1307307};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:AAH91192.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver {ECO:0000312|EMBL:AAH91192.1}, and Pituitary anterior
RC   lobe;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3] {ECO:0000305}
RP   INTERACTION WITH SLC2A4.
RX   PubMed=16396496; DOI=10.1021/pr0502626;
RA   Foster L.J., Rudich A., Talior I., Patel N., Huang X., Furtado L.M.,
RA   Bilan P.J., Mann M., Klip A.;
RT   "Insulin-dependent interactions of proteins with GLUT4 revealed through
RT   stable isotope labeling by amino acids in cell culture (SILAC).";
RL   J. Proteome Res. 5:64-75(2006).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC   STRAIN=Holtzman; TISSUE=Epididymis, and Sperm;
RX   PubMed=19423663; DOI=10.1530/rep-09-0052;
RA   Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT   "Identification of novel immunodominant epididymal sperm proteins using
RT   combinatorial approach.";
RL   Reproduction 138:81-93(2009).
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:0000305};
CC       Note=Binds 1 FAD per subunit. {ECO:0000305};
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 (PubMed:16396496). Interacts with CLOCK (By similarity).
CC       Interacts with RAB5IF (By similarity). {ECO:0000250|UniProtKB:Q16795,
CC       ECO:0000269|PubMed:16396496}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q16795}.
CC   -!- TISSUE SPECIFICITY: Expressed by the principal cells of the epididymis.
CC       Detected in flagella of epididymal sperm (at protein level).
CC       {ECO:0000269|PubMed:19423663}.
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:0000255}.
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DR   EMBL; CH473964; EDM01826.1; -; Genomic_DNA.
DR   EMBL; BC091192; AAH91192.1; -; mRNA.
DR   EMBL; BC168777; AAI68777.1; -; mRNA.
DR   RefSeq; NP_001094222.1; NM_001100752.1.
DR   AlphaFoldDB; Q5BK63; -.
DR   SMR; Q5BK63; -.
DR   BioGRID; 263453; 4.
DR   IntAct; Q5BK63; 3.
DR   MINT; Q5BK63; -.
DR   STRING; 10116.ENSRNOP00000072757; -.
DR   CarbonylDB; Q5BK63; -.
DR   GlyGen; Q5BK63; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; Q5BK63; -.
DR   PhosphoSitePlus; Q5BK63; -.
DR   jPOST; Q5BK63; -.
DR   PaxDb; 10116-ENSRNOP00000034135; -.
DR   GeneID; 362440; -.
DR   KEGG; rno:362440; -.
DR   UCSC; RGD:1307307; rat.
DR   AGR; RGD:1307307; -.
DR   CTD; 4704; -.
DR   RGD; 1307307; Ndufa9.
DR   VEuPathDB; HostDB:ENSRNOG00000061684; -.
DR   eggNOG; KOG2865; Eukaryota.
DR   HOGENOM; CLU_007383_6_4_1; -.
DR   InParanoid; Q5BK63; -.
DR   OrthoDB; 141210at2759; -.
DR   PhylomeDB; Q5BK63; -.
DR   TreeFam; TF105961; -.
DR   Reactome; R-RNO-611105; Respiratory electron transport.
DR   Reactome; R-RNO-6799198; Complex I biogenesis.
DR   PRO; PR:Q5BK63; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Proteomes; UP000234681; Chromosome 4.
DR   Bgee; ENSRNOG00000061684; Expressed in heart and 20 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   GO; GO:0009749; P:response to glucose; IEP:RGD.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-like.
DR   PANTHER; PTHR12126:SF11; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 9, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12126; NADH-UBIQUINONE OXIDOREDUCTASE 39 KDA SUBUNIT-RELATED; 1.
DR   Pfam; PF05368; NmrA; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   Genevisible; Q5BK63; RN.
PE   1: Evidence at protein 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_0000308374"
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;  42559 MW;  578C531D5223CD5C CRC64;
     MAAAVRFQVV RALPMSRPAI SAAATSVFCS SSHRQLHHAV IPHGKGGRSS VSGVVATVFG
     ATGFLGRYVV NHLGRMGSQV IIPYRCDIYD TMHLRLMGDL GQLIFLEWDA RDKDSIRKAV
     QHSNVVINLI GREWETRNFD FEDVFVNIPR AIAQASKEAG VERFIHVSHL NASMKSSAKS
     LRSKAVGEKE VRTVFPDAII IRPSDMFGRE DRFLNHFANY RWFLAVPLVS LGFKTVKQPV
     YVADVSKGIA NATKNPDAIG KTFAFTGPNR YLLFHLVKYI FGMTHRTFIP YPLPRFVYSW
     IGRLFGLSPF EPWTTKDKVE RIHISDVMAT DLPGLEDLGV QPTPLELKSI EVLRRHRTYR
     WLSSEIEETK PAKTVNY
//