CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009039
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NADPH:adrenodoxin oxidoreductase, mitochondrial 
Protein Synonyms/Alias
 AR; Adrenodoxin reductase; Ferredoxin--NADP(+) reductase; Ferredoxin reductase 
Gene Name
 Fdxr 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
207TPPEHLEKTDITEVAacetylation[1]
242LQVAFTIKELREMIQacetylation[1]
379PSVPFDPKLGIIPNTacetylation[1]
429QVLLKDLKAGLLPSGacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver. 
Sequence Annotation
 NP_BIND 187 190 NADP (By similarity).
 NP_BIND 231 232 NADP (By similarity).
 NP_BIND 408 410 FAD (By similarity).
 BINDING 51 51 FAD; via amide nitrogen (By similarity).
 BINDING 72 72 FAD (By similarity).
 BINDING 80 80 FAD; via amide nitrogen (By similarity).
 BINDING 116 116 FAD; via amide nitrogen and carbonyl
 BINDING 243 243 NADP (By similarity).
 BINDING 401 401 FAD; via amide nitrogen (By similarity).
 BINDING 408 408 NADP; via amide nitrogen (By similarity).  
Keyword
 Cholesterol metabolism; Complete proteome; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; Reference proteome; Steroid metabolism; Sterol metabolism; Transit peptide; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 494 AA 
Protein Sequence
MAPRCWRWWS WSAWPGVRPL PSRSTPTPGF CKKFSTQETT PQICVVGSGP AGFYTAQHLL 60
KHHTRAHVDI YEKQLVPFGL VRFGVAPDHP EVKNVINTFT QTARSDRCAF RGNVVVGRDV 120
SVPELREAYH AVVLSYGAED HQPLEIPGEE LPGVVSARAF VGWYNGLPEN QKLAPDLSCD 180
TAVILGQGNV ALDVARILLT PPEHLEKTDI TEVALGVLRQ SRVKTVWIVG RRGPLQVAFT 240
IKELREMIQL PGTQPILDPS DFLGLQDRIK DVPRPRKRLT ELLLRTATEK PGVEEAARRA 300
LASRAWGLRF FRSPQQVLPT PDGRRVAGIR LAVTRLEGVG ESTRAVPTGD VEDLPCGLLL 360
SSVGYKSRPI DPSVPFDPKL GIIPNTEGRV VNAPGLYCSG WVKRGPTGVI TTTMTDSFLT 420
SQVLLKDLKA GLLPSGPRPG YTAIQALLSD RGVRPVSFSD WEKLDAEEVA RGQGTGKPRE 480
KLVDRREMLQ LLGH 494 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:RGD.
 GO:0070402; F:NADPH binding; IDA:RGD.
 GO:0015039; F:NADPH-adrenodoxin reductase activity; IDA:RGD.
 GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
 GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
 GO:0070995; P:NADPH oxidation; IDA:RGD. 
Interpro
 IPR021163; Adrenodoxin_Rdtase.
 IPR016040; NAD(P)-bd_dom. 
Pfam
  
SMART
  
PROSITE
  
PRINTS