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NDUA9_BOVIN
ID   NDUA9_BOVIN             Reviewed;         380 AA.
AC   P34943; Q3T0K3;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 142.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Heart;
RX   PubMed=1832859; DOI=10.1042/bj2780821;
RA   Fearnley I.M., Finel M., Skehel J.M., Walker J.E.;
RT   "NADH:ubiquinone oxidoreductase from bovine heart mitochondria. cDNA
RT   sequences of the import precursors of the nuclear-encoded 39 kDa and 42 kDa
RT   subunits.";
RL   Biochem. J. 278:821-829(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, SUBUNIT, IDENTIFICATION IN COMPLEX I, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=10852722; DOI=10.1021/bi000335t;
RA   Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E.;
RT   "Resolution of the membrane domain of bovine complex I into subcomplexes:
RT   implications for the structural organization of the enzyme.";
RL   Biochemistry 39:7229-7235(2000).
RN   [4]
RP   SUBUNIT, IDENTIFICATION IN COMPLEX I, AND SUBCELLULAR LOCATION.
RX   PubMed=18721790; DOI=10.1016/j.ab.2008.07.029;
RA   Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A.,
RA   Robinson N.C.;
RT   "Subunit analysis of bovine heart complex I by reversed-phase high-
RT   performance liquid chromatography, electrospray ionization-tandem mass
RT   spectrometry, and matrix-assisted laser desorption/ionization-time-of-
RT   flight mass spectrometry.";
RL   Anal. Biochem. 382:116-121(2008).
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;
CC       Note=Binds 1 FAD per subunit.;
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits
CC       (PubMed:10852722, PubMed:18721790). This a component of the hydrophobic
CC       protein fraction (PubMed:10852722, PubMed:18721790). Interacts with
CC       BLOC1S1 (By similarity). Interacts with SLC2A4 (By similarity).
CC       Interacts with CLOCK (By similarity). Interacts with RAB5IF (By
CC       similarity). {ECO:0000250|UniProtKB:Q16795,
CC       ECO:0000250|UniProtKB:Q5BK63, ECO:0000269|PubMed:10852722,
CC       ECO:0000269|PubMed:18721790}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790}.
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}.
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DR   EMBL; X59418; CAA42053.1; -; mRNA.
DR   EMBL; BC102359; AAI02360.1; -; mRNA.
DR   PIR; S17676; S17676.
DR   RefSeq; NP_991386.1; NM_205817.1.
DR   PDB; 7QSD; EM; 3.10 A; P=1-380.
DR   PDBsum; 7QSD; -.
DR   AlphaFoldDB; P34943; -.
DR   SMR; P34943; -.
DR   CORUM; P34943; -.
DR   DIP; DIP-38819N; -.
DR   IntAct; P34943; 3.
DR   MINT; P34943; -.
DR   STRING; 9913.ENSBTAP00000007189; -.
DR   TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   PaxDb; P34943; -.
DR   PeptideAtlas; P34943; -.
DR   PRIDE; P34943; -.
DR   Ensembl; ENSBTAT00000007189; ENSBTAP00000007189; ENSBTAG00000005465.
DR   GeneID; 404188; -.
DR   KEGG; bta:404188; -.
DR   CTD; 4704; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005465; -.
DR   VGNC; VGNC:56233; NDUFA9.
DR   eggNOG; KOG2865; Eukaryota.
DR   GeneTree; ENSGT00390000006865; -.
DR   HOGENOM; CLU_007383_6_4_1; -.
DR   InParanoid; P34943; -.
DR   OMA; FFNRFAA; -.
DR   OrthoDB; 721605at2759; -.
DR   TreeFam; TF105961; -.
DR   Reactome; R-BTA-611105; Respiratory electron transport.
DR   Reactome; R-BTA-6799198; Complex I biogenesis.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000005465; Expressed in corpus luteum and 104 other tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR   GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
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   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   3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW   FAD; Flavoprotein; Mitochondrion; Reference proteome; Respiratory chain;
KW   Transit peptide; Transport.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT   CHAIN           36..380
FT                   /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT                   subunit 9, mitochondrial"
FT                   /id="PRO_0000019991"
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"
SQ   SEQUENCE   380 AA;  42849 MW;  B453FA19D48D03CD CRC64;
     MAAAVHPRVV RVLPMSRSSV PALAASVFHS PPQRQLHHAV IPHGKGGRSS VSGIVATVFG
     ATGFLGRYVV NHLGRMGSQV IVPHRCEPYD TMHLRPMGDL GQIIFMDWNG RDKDSIRRAV
     EHSSVVINLV GREWETQNFD FEDVFVKIPQ AIAQVSKEAG VEKFIHISHL NADIKSSSKY
     LRSKAVGEKE VRETFPEATI IKPAEIFGRE DRFLNYFANI RWFGGVPLIS LGKKTVKQPV
     YIVDVTKGII NAIKDPDARG KTFAFVGPSR YLLFDLVQYV FAVAHRPFLP YPLPHFAYRW
     IGRLFEISPF EPWTTRDKVE RIHTTDKILP HLPGLEDLGV EATPLELKAI EVLRRHRTYR
     WLSSEIEDVQ PAKTIPTSGP
 
 
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