NDUA9_RAT
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 03-AUG-2022, entry version 119.
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 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}.
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; 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.ENSRNOP00000034135; -.
DR CarbonylDB; Q5BK63; -.
DR iPTMnet; Q5BK63; -.
DR PhosphoSitePlus; Q5BK63; -.
DR jPOST; Q5BK63; -.
DR PaxDb; Q5BK63; -.
DR PRIDE; Q5BK63; -.
DR GeneID; 362440; -.
DR KEGG; rno:362440; -.
DR UCSC; RGD:1307307; rat.
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 OMA; FFNRFAA; -.
DR OrthoDB; 721605at2759; -.
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 tissues.
DR Genevisible; Q5BK63; RN.
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; IDA: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 InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
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