ID A0A093CVI3_TAUER Unreviewed; 228 AA.
AC A0A093CVI3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Plasma membrane ascorbate-dependent reductase CYBRD1 {ECO:0000256|ARBA:ARBA00024244};
DE EC=7.2.1.3 {ECO:0000256|ARBA:ARBA00024225};
DE AltName: Full=Cytochrome b reductase 1 {ECO:0000256|ARBA:ARBA00031718};
DE Flags: Fragment;
GN ORFNames=N340_06803 {ECO:0000313|EMBL:KFV16919.1};
OS Tauraco erythrolophus (Red-crested turaco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV16919.1, ECO:0000313|Proteomes:UP000053661};
RN [1] {ECO:0000313|EMBL:KFV16919.1, ECO:0000313|Proteomes:UP000053661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV16919.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00024274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66657;
CC Evidence={ECO:0000256|ARBA:ARBA00024274};
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:0000256|ARBA:ARBA00024157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30404;
CC Evidence={ECO:0000256|ARBA:ARBA00024157};
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:0000256|ARBA:ARBA00024163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66525;
CC Evidence={ECO:0000256|ARBA:ARBA00024163};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004424}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KL466526; KFV16919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093CVI3; -.
DR Proteomes; UP000053661; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140571; F:transmembrane ascorbate ferrireductase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.20.120.1770; -; 1.
DR InterPro; IPR043205; CYB561/CYBRD1-like.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR PANTHER; PTHR10106; CYTOCHROME B561-RELATED; 1.
DR PANTHER; PTHR10106:SF12; PLASMA MEMBRANE ASCORBATE-DEPENDENT REDUCTASE CYBRD1; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053661};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..163
FT /note="Cytochrome b561"
FT /evidence="ECO:0000259|PROSITE:PS50939"
FT REGION 171..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV16919.1"
FT NON_TER 228
FT /evidence="ECO:0000313|EMBL:KFV16919.1"
SQ SEQUENCE 228 AA; 24950 MW; 890A32F13057535B CRC64;
LVSVLSSAII VYRLPWTWKC SKLLMKCIHA GLNTVAMILA IVATVAAFDY HNASNIPNMY
SLHSWIGLIA IIFYSLQLFL GFAVFLLPFA PVPLRAALMP IHVYSGLTIF ATVIATALMG
ITEKLLFSLQ NPSYSASPPE ATFVNCLGLL LVIFGALILW MASRPHWKRP PEENAKVLGP
IGETPEGTEA ESTMTDGSNA DKSDLRINSE ADRKQNLKLD EAGQRSTM
//
