CYBR1_XENLA
ID CYBR1_XENLA Reviewed; 283 AA.
AC Q6DDR3; Q6DCI4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 62.
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;
GN Name=cybrd1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-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+). It is
CC also able to reduce extracellular monodehydro-L-ascorbate and may be
CC involved in extracellular ascorbate regeneration (By similarity). May
CC also function as a 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH77470.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC077470; AAH77470.1; ALT_INIT; mRNA.
DR EMBL; BC078045; AAH78045.1; -; mRNA.
DR RefSeq; NP_001086436.1; NM_001092967.1.
DR AlphaFoldDB; Q6DDR3; -.
DR SMR; Q6DDR3; -.
DR DNASU; 445864; -.
DR GeneID; 445864; -.
DR KEGG; xla:445864; -.
DR CTD; 445864; -.
DR Xenbase; XB-GENE-1011692; cybrd1.L.
DR OrthoDB; 1503869at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 445864; Expressed in spleen and 19 other tissues.
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; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..283
FT /note="Plasma membrane ascorbate-dependent reductase
FT CYBRD1"
FT /id="PRO_0000314835"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 6..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 31..45
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 46..67
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 68..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 77..103
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 104..116
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 117..142
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 143..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 150..177
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 178..195
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 196..220
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 221..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT DOMAIN 13..218
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT REGION 234..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48
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 68
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 77
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 77
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 81
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 84
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 106
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_note="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 113..116
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 118
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 150
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 157
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 178
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 223
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
SQ SEQUENCE 283 AA; 31481 MW; 69D0253A98C07779 CRC64;
MEGYKSFLAF LVSSLLLGFL GVIFTLVWVL HWREGLGWDG GAAEFNWHPV LVTSGFIFIQ
GIAIIVYRLP WTWKCSKLLM KFIHAGLHLT ALIFTIVALV AVFDFHNAKN IPNMYSLHSW
IGLTVVILYA LQLVLGVSIY LLPFASNTLR AALMPVHVYS GLFIFGTVIA TALMGITEKL
IFSLKEPPYS KLPPEAIFVN TFGLLILVFG GLVVWMVTTP AWKRPREQGM EILSPTVSSP
DETEEGSTIT DCSNTEKSDV ELNSEAARKR ILKLDEAGQR STM
