CYBR1_PONAB
ID CYBR1_PONAB Reviewed; 287 AA.
AC Q5RAJ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Plasma membrane ascorbate-dependent reductase CYBRD1 {ECO:0000250|UniProtKB:Q53TN4};
DE EC=7.2.1.3 {ECO:0000250|UniProtKB:Q53TN4};
DE AltName: Full=Cytochrome b reductase 1 {ECO:0000250|UniProtKB:Q53TN4};
GN Name=CYBRD1 {ECO:0000250|UniProtKB:Q53TN4};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plasma membrane reductase that uses cytoplasmic ascorbate as
CC an electron donor to reduce extracellular Fe(3+) into Fe(2+). Probably
CC functions in dietary iron absorption at the brush border of duodenal
CC enterocytes by producing Fe(2+), the divalent form of iron that can be
CC transported into enterocytes. It is also able to reduce extracellular
CC monodehydro-L-ascorbate and may be involved in extracellular ascorbate
CC regeneration by erythrocytes in blood. May also act as a ferrireductase
CC in airway epithelial cells (By similarity). May also function as a
CC cupric transmembrane reductase (By similarity).
CC {ECO:0000250|UniProtKB:Q53TN4, ECO:0000250|UniProtKB:Q925G2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(3+)(out) + L-ascorbate(in) = Fe(2+)(out) + H(+) +
CC monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:30403,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=7.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30404;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cu(2+)(out) + L-ascorbate(in) = Cu(+)(out) + H(+) +
CC monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:66656,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29036, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:49552, ChEBI:CHEBI:59513;
CC Evidence={ECO:0000250|UniProtKB:Q925G2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66657;
CC Evidence={ECO:0000250|UniProtKB:Q925G2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ascorbate(in) + monodehydro-L-ascorbate radical(out) = L-
CC ascorbate(out) + monodehydro-L-ascorbate radical(in);
CC Xref=Rhea:RHEA:66524, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66525;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:Q53TN4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q53TN4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q53TN4};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q53TN4}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53TN4}. Note=Localized at the brush border of
CC duodenal cells. {ECO:0000250|UniProtKB:Q53TN4}.
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DR EMBL; CR859021; CAH91216.1; -; mRNA.
DR RefSeq; NP_001125716.1; NM_001132244.1.
DR AlphaFoldDB; Q5RAJ4; -.
DR SMR; Q5RAJ4; -.
DR STRING; 9601.ENSPPYP00000014431; -.
DR GeneID; 100172640; -.
DR KEGG; pon:100172640; -.
DR CTD; 79901; -.
DR eggNOG; KOG1619; Eukaryota.
DR InParanoid; Q5RAJ4; -.
DR OrthoDB; 1503869at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140571; F:transmembrane ascorbate ferrireductase activity; ISS:UniProtKB.
DR GO; GO:0140575; F:transmembrane monodehydroascorbate reductase activity; ISS:UniProtKB.
DR GO; GO:0140576; P:ascorbate homeostasis; ISS:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0055072; P:iron ion homeostasis; ISS:UniProtKB.
DR InterPro; IPR043205; CYB561/CYBRD1-like.
DR InterPro; IPR028838; CYBRD1.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR PANTHER; PTHR10106; PTHR10106; 1.
DR PANTHER; PTHR10106:SF12; PTHR10106:SF12; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..287
FT /note="Plasma membrane ascorbate-dependent reductase
FT CYBRD1"
FT /id="PRO_0000314832"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 8..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 33..47
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 48..69
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 70..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 79..105
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 106..118
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 119..144
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 145..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 152..179
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 180..197
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 198..223
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 224..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT DOMAIN 15..221
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT REGION 228..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 70
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 79
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 79
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 83
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 86
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 108
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_note="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 115..118
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 120
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 152
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 159
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 180
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 226
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT MOD_RES 286
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
SQ SEQUENCE 287 AA; 31765 MW; F52CA5EBED9C800A CRC64;
MAMEGYWRFL ALLGSALLVG FLSVIFTLVW VLHYREGLGW DGSALEFNWH PVLMVTGFVF
IQGIAIIVYR LSWTWKCSKL LMKSIHAGLN AVAAILAVIS VVAVFENHNV NNIANMYSLH
SWVGLIAVIC YLLQLLAGFS VFLLPWAPLS LRAFLMPIHV YSGIVIFGTV IATALMGVTE
KLIFSLRDPA YSTFPPEGVF FVNTLGLLIL VFGALIFWIV TRPQWKRPKE PDSTILHPSG
GTEQGARGSM PAYSGNNMDK SDSELNNEVA ARKRNLALDE AGQRSTM
