Tag | Content |
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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 |
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207 | TPPEHLEKTDITEVA | acetylation | [1] | 242 | LQVAFTIKELREMIQ | acetylation | [1] | 379 | PSVPFDPKLGIIPNT | acetylation | [1] | 429 | QVLLKDLKAGLLPSG | acetylation | [1] |
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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. |
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