| Identification |
|---|
| HMDB Protein ID
| HMDBP02111 |
| Secondary Accession Numbers
| |
| Name
| Adrenodoxin, mitochondrial precursor |
| Synonyms
|
- Adrenal ferredoxin
- Ferredoxin- 1
- Hepatoredoxin
|
| Gene Name
| FDX1 |
| Protein Type
| Enzyme |
| Biological Properties |
|---|
| General Function
| Energy production and conversion |
| Specific Function
| Participates in the synthesis of thyroid hormones. Transfers electrons from adrenodoxin reductase to the cholesterol side chain cleavage cytochrome P450 |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Function |
| ion binding |
| cation binding |
| binding |
| transition metal ion binding |
| transporter activity |
| iron ion binding |
| electron transporter activity |
| Process |
| physiological process |
| metabolism |
| cellular metabolism |
| generation of precursor metabolites and energy |
| electron transport |
|
| Cellular Location
|
- Secreted
|
| Gene Properties |
|---|
| Chromosome Location
| Chromosome:11 |
| Locus
| 11q22 |
| SNPs
| FDX1 |
| Gene Sequence
|
>555 bp
ATGGCTGCCGCTGGGGGCGCCCGGCTGCTGCGCGCCGCTTCTGCTGTCCTCGGCGGCCCG
GCCGGCCGGTGGCTGCACCACGCTGGGTCCCGCGCTGGATCCAGCGGCCTGCTGAGGAAC
CGGGGGCCGGGCGGTAGCGCGGAGGCGAGCCGGTCGCTGAGCGTGTCGGCGCGGGCCCGG
AGCAGCTCAGAAGATAAAATAACAGTCCACTTTATAAACCGTGATGGTGAAACATTAACA
ACCAAAGGAAAAGTTGGTGATTCTCTGCTAGATGTTGTGGTTGAAAATAATCTAGATATT
GATGGCTTTGGTGCATGTGAGGGAACCCTGGCTTGTTCAACCTGTCACCTCATCTTTGAA
GATCACATATATGAGAAGTTAGATGCAATCACTGATGAGGAGAATGACATGCTCGATCTG
GCATATGGACTAACAGACAGATCACGGTTGGGCTGCCAAATCTGTTTGACAAAATCTATG
GACAATATGACTGTTCGAGTGCCTGAAACAGTGGCTGATGCCAGACAATCCATTGATGTG
GGCAAGACCTCCTGA
|
| Protein Properties |
|---|
| Number of Residues
| 184 |
| Molecular Weight
| 19393.0 |
| Theoretical pI
| 5.62 |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
>Adrenodoxin, mitochondrial precursor
MAAAGGARLLRAASAVLGGPAGRWLHHAGSRAGSSGLLRNRGPGGSAEASRSLSVSARAR
SSSEDKITVHFINRDGETLTTKGKVGDSLLDVVVENNLDIDGFGACEGTLACSTCHLIFE
DHIYEKLDAITDEENDMLDLAYGLTDRSRLGCQICLTKSMDNMTVRVPETVADARQSIDV
GKTS
|
| External Links |
|---|
| GenBank ID Protein
| 557734 |
| UniProtKB/Swiss-Prot ID
| P10109 |
| UniProtKB/Swiss-Prot Entry Name
| ADX_HUMAN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| M23668 |
| GeneCard ID
| FDX1 |
| GenAtlas ID
| FDX1 |
| HGNC ID
| HGNC:3638 |
| References |
|---|
| General References
| - Chang CY, Wu DA, Lai CC, Miller WL, Chung BC: Cloning and structure of the human adrenodoxin gene. DNA. 1988 Nov;7(9):609-15. [PubMed:3229285 ]
- Picado-Leonard J, Voutilainen R, Kao LC, Chung BC, Strauss JF 3rd, Miller WL: Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells. J Biol Chem. 1988 Mar 5;263(7):3240-4. [PubMed:3343244 ]
- Mittal S, Zhu YZ, Vickery LE: Molecular cloning and sequence analysis of human placental ferredoxin. Arch Biochem Biophys. 1988 Aug 1;264(2):383-91. [PubMed:2969697 ]
- Chang CY, Wu DA, Mohandas TK, Chung BC: Structure, sequence, chromosomal location, and evolution of the human ferredoxin gene family. DNA Cell Biol. 1990 Apr;9(3):205-12. [PubMed:2340092 ]
- Johnson D, Norman S, Tuckey RC, Martin LL: Electrochemical behaviour of human adrenodoxin on a pyrolytic graphite electrode. Bioelectrochemistry. 2003 Apr;59(1-2):41-7. [PubMed:12699818 ]
- Skjeldal L, Markley JL, Coghlan VM, Vickery LE: 1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins. Biochemistry. 1991 Sep 17;30(37):9078-83. [PubMed:1909889 ]
|
