Cytochrome b reductase 1

Details

Name
Cytochrome b reductase 1
Synonyms
  • 1.-.-.-
  • DCYTB
  • Duodenal cytochrome b
  • Ferric-chelate reductase 3
  • FRRS3
Gene Name
CYBRD1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0052290|Cytochrome b reductase 1
MAMEGYWRFLALLGSALLVGFLSVIFALVWVLHYREGLGWDGSALEFNWHPVLMVTGFVF
IQGIAIIVYRLPWTWKCSKLLMKSIHAGLNAVAAILAIISVVAVFENHNVNNIANMYSLH
SWVGLIAVICYLLQLLSGFSVFLLPWAPLSLRAFLMPIHVYSGIVIFGTVIATALMGLTE
KLIFSLRDPAYSTFPPEGVFVNTLGLLILVFGALIFWIVTRPQWKRPKEPNSTILHPNGG
TEQGARGSMPAYSGNNMDKSDSELNSEVAARKRNLALDEAGQRSTM
Number of residues
286
Molecular Weight
31641.005
Theoretical pI
Not Available
GO Classification
Functions
ferric-chelate reductase activity / metal ion binding / oxidoreductase activity
Processes
cellular iron ion homeostasis / response to iron ion
Components
brush border membrane / cell / extracellular exosome / integral component of membrane / lysosomal membrane / plasma membrane
General Function
Ferric-chelate reductase that reduces Fe(3+) to Fe(2+). Present at the brush border of duodenal enterocytes where it probably reduces dietary Fe(3+) thereby facilitating its transport into the mucosal cells. Uses ascorbate as electron donor. May be involved in extracellular ascorbate recycling in erythrocyte membranes. May also act as a ferrireductase in airway epithelial cells.
Specific Function
Ferric-chelate reductase activity
Pfam Domain Function
Transmembrane Regions
12-32 49-69 85-105 123-143 158-178 199-219
Cellular Location
Membrane
Gene sequence
>lcl|BSEQ0052291|Cytochrome b reductase 1 (CYBRD1)
ATGGCCATGGAGGGCTACTGGCGCTTCCTGGCGCTGCTGGGGTCGGCACTGCTCGTCGGC
TTCCTGTCGGTGATCTTCGCCCTCGTCTGGGTCCTCCACTACCGAGAGGGGCTTGGCTGG
GATGGGAGCGCACTAGAGTTTAACTGGCACCCAGTGCTCATGGTCACCGGCTTCGTCTTC
ATCCAGGGCATCGCCATCATCGTCTACAGACTGCCGTGGACCTGGAAATGCAGCAAGCTC
CTGATGAAATCCATCCATGCAGGGTTAAATGCAGTTGCTGCCATTCTTGCAATTATCTCT
GTGGTGGCCGTGTTTGAGAACCACAATGTTAACAATATAGCCAATATGTACAGTCTGCAC
AGCTGGGTTGGACTGATAGCTGTCATATGCTATTTGTTACAGCTTCTTTCAGGTTTTTCA
GTCTTTCTGCTTCCATGGGCTCCGCTTTCTCTCCGAGCATTTCTCATGCCCATACATGTT
TATTCTGGAATTGTCATCTTTGGAACAGTGATTGCAACAGCACTTATGGGATTGACAGAG
AAACTGATTTTTTCCCTGAGAGATCCTGCATACAGTACATTCCCGCCAGAAGGTGTTTTC
GTAAATACGCTTGGCCTTCTGATCCTGGTGTTCGGGGCCCTCATTTTTTGGATAGTCACC
AGACCGCAATGGAAACGTCCTAAGGAGCCAAATTCTACCATTCTTCATCCAAATGGAGGC
ACTGAACAGGGAGCAAGAGGTTCCATGCCAGCCTACTCTGGCAACAACATGGACAAATCA
GATTCAGAGTTAAACAGTGAAGTAGCAGCAAGGAAAAGAAACTTAGCTCTGGATGAGGCT
GGGCAGAGATCTACCATGTAA
Chromosome Location
2
Locus
2q31.1
External Identifiers
ResourceLink
UniProtKB IDQ53TN4
UniProtKB Entry NameCYBR1_HUMAN
HGNC IDHGNC:20797
General References
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  15. Zaahl MG, Merryweather-Clarke AT, Kotze MJ, van der Merwe S, Warnich L, Robson KJ: Gene symbol: DCYTB/CYBRD1. Disease: primary iron overload. Hum Genet. 2005 Dec;118(3-4):548-9. [Article]
  16. Zaahl MG, Merryweather-Clarke AT, Kotze MJ, van der Merwe S, Warnich L, Robson KJ: Gene symbol: DCYTB/CYBRD1. Disease: primary iron overload. Hum Genet. 2005 Dec;118(3-4):549. [Article]
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  18. Su D, May JM, Koury MJ, Asard H: Human erythrocyte membranes contain a cytochrome b561 that may be involved in extracellular ascorbate recycling. J Biol Chem. 2006 Dec 29;281(52):39852-9. doi: 10.1074/jbc.M606543200. Epub 2006 Oct 26. [Article]
  19. Turi JL, Wang X, McKie AT, Nozik-Grayck E, Mamo LB, Crissman K, Piantadosi CA, Ghio AJ: Duodenal cytochrome b: a novel ferrireductase in airway epithelial cells. Am J Physiol Lung Cell Mol Physiol. 2006 Aug;291(2):L272-80. doi: 10.1152/ajplung.00342.2005. Epub 2006 Mar 1. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB13257Ferrous sulfate anhydrousapprovedunknownsubstrateDetails
DB14520Tetraferric tricitrate decahydrateapprovedunknownsubstrateDetails