CYBRD1
entrez
79901
canonical
uniprot
Q53TN4
canonical
ensembl
ENSG00000071967
resolver
ensp
ENSP00000319141
resolver
ensp
ENSP00000364401
resolver
ensp
ENSP00000386739
resolver
genesymbol
CYBRD1
resolver
genesymbol_syn
DCYTB
resolver
genesymbol_syn
FRRS3
resolver
hgnc
HGNC:20797
resolver
uniprot
B2RE79
resolver
uniprot
B4DWD7
resolver
uniprot
Q6KC16
resolver
uniprot
Q6KC17
resolver
uniprot
Q6P147
resolver
uniprot
Q6ZR51
resolver
uniprot
Q9H0Q8
resolver
uniprot
Q9H5G5
resolver
uniprot_entry
CYBR1_HUMAN
resolver
uniprot_sec
B2RE79
resolver
uniprot_sec
B4DWD7
resolver
uniprot_sec
Q6KC16
resolver
uniprot_sec
Q6KC17
resolver
uniprot_sec
Q6P147
resolver
uniprot_sec
Q6ZR51
resolver
uniprot_sec
Q9H0Q8
resolver
uniprot_sec
Q9H5G5
resolver
activity_regulation
ACTIVITY REGULATION: Activated by chelators like citrate, malate, and oxalate especially at alkaline pH. {ECO:0000269|PubMed:30272000}.
uniprot
proteins
amino_acid_sequence
MAMEGYWRFLALLGSALLVGFLSVIFALVWVLHYREGLGWDGSALEFNWHPVLMVTGFVFIQGIAIIVYRLPWTWKCSKLLMKSIHAGLNAVAAILAIISVVAVFENHNVNNIANMYSLHSWVGLIAVICYLLQLLSGFSVFLLPWAPLSLRAFLMPIHVYSGIVIFGTVIATALMGLTEKLIFSLRDPAYSTFPPEGVFVNTLGLLILVFGALIFWIVTRPQWKRPKEPNSTILHPNGGTEQGARGSMPAYSGNNMDKSDSELNSEVAARKRNLALDEAGQRSTM
uniprot
proteins
ec_number
7.2.1.3
uniprot
proteins
function
FUNCTION: Plasma membrane reductase that uses cytoplasmic ascorbate as an electron donor to reduce extracellular Fe(3+) into Fe(2+) (PubMed:30272000). Probably functions in dietary iron absorption at the brush border of duodenal enterocytes by producing Fe(2+), the divalent form of iron that can be transported into enterocytes (PubMed:30272000). It is also able to reduce extracellular monodehydro-L-ascorbate and may be involved in extracellular ascorbate regeneration by erythrocytes in blood (PubMed:17068337). May also act as a ferrireductase in airway epithelial cells (Probable). May also function as a cupric transmembrane reductase (By similarity). {ECO:0000250|UniProtKB:Q925G2, ECO:0000269|PubMed:17068337, ECO:0000269|PubMed:30272000, ECO:0000305|PubMed:16510471}.
uniprot
proteins
mass_dalton
31641
uniprot
proteins
mutagenesis
MUTAGEN 58; /note="F->L: Decreased transmembrane ascorbate ferrireductase activity."; /evidence="ECO:0000269|PubMed:30272000"; MUTAGEN 79; /note="K->S: Decreased heme b reduction by ascorbate."; /evidence="ECO:0000269|PubMed:30272000"; MUTAGEN 83; /note="K->S: Decreased heme b reduction by ascorbate."; /evidence="ECO:0000269|PubMed:30272000"; MUTAGEN 107; /note="N->A,F: Decreased transmembrane ascorbate ferrireductase activity."; /evidence="ECO:0000269|PubMed:30272000"; MUTAGEN 108; /note="H->A: Loss of transmembrane ascorbate ferrireductase activity."; /evidence="ECO:0000269|PubMed:30272000"; MUTAGEN 108; /note="H->Q: Loss of iron binding. Loss of transmembrane ascorbate ferrireductase activity."; /evidence="ECO:0000269|PubMed:30272000"; MUTAGEN 117; /note="Y->A,S: Decreased transmembrane ascorbate ferrireductase activity."; /evidence="ECO:0000269|PubMed:30272000"; MUTAGEN 131; /note="Y->L: Decreased transmembrane ascorbate ferrireductase activity."; /evidence="ECO:0000269|PubMed:30272000"; MUTAGEN 152; /note="R->E: Decreased heme b reduction by ascorbate."; /evidence="ECO:0000269|PubMed:30272000"; MUTAGEN 184; /note="F->A: Decreased transmembrane ascorbate ferrireductase activity."; /evidence="ECO:0000269|PubMed:30272000
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
12949720
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15338274
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16510471
uniprot
proteins
pubmed
16521301
uniprot
proteins
pubmed
16521311
uniprot
proteins
pubmed
16521312
uniprot
proteins
pubmed
17068337
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17087784
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19673882
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
30272000
uniprot
proteins
sequence_length
286
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17068337}; Multi-pass membrane protein {ECO:0000269|PubMed:30272000}. Apical cell membrane {ECO:0000305|PubMed:12949720}; Multi-pass membrane protein {ECO:0000269|PubMed:30272000}. Note=Localized at the brush border of duodenal cells. {ECO:0000269|PubMed:12949720}.
uniprot
proteins
transmembrane_region
TRANSMEM 8..32; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG"; TRANSMEM 48..69; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG"; TRANSMEM 79..105; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG"; TRANSMEM 119..144; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG"; TRANSMEM 152..179; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG"; TRANSMEM 198..222; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG
uniprot
proteins