ID F5H0P5_HUMAN Unreviewed; 182 AA.
AC F5H0P5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Lysosomal membrane ascorbate-dependent ferrireductase CYB561A3 {ECO:0000256|ARBA:ARBA00040498};
DE EC=7.2.1.3 {ECO:0000256|ARBA:ARBA00024225};
DE AltName: Full=Cytochrome b ascorbate-dependent protein 3 {ECO:0000256|ARBA:ARBA00042571};
DE AltName: Full=Lysosomal cytochrome b {ECO:0000256|ARBA:ARBA00042550};
DE Flags: Fragment;
GN Name=CYB561A3 {ECO:0000313|Ensembl:ENSP00000438725.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000438725.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000438725.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2] {ECO:0000313|Ensembl:ENSP00000438725.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004107}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F5H0P5; -.
DR SMR; F5H0P5; -.
DR MassIVE; F5H0P5; -.
DR MaxQB; F5H0P5; -.
DR PeptideAtlas; F5H0P5; -.
DR ProteomicsDB; 25403; -.
DR Antibodypedia; 52925; 9 antibodies from 7 providers.
DR Ensembl; ENST00000537364.5; ENSP00000438725.1; ENSG00000162144.10.
DR UCSC; uc058cau.1; human.
DR HGNC; HGNC:23014; CYB561A3.
DR VEuPathDB; HostDB:ENSG00000162144; -.
DR GeneTree; ENSGT00950000183197; -.
DR HOGENOM; CLU_069712_1_3_1; -.
DR OMA; FKFHDMV; -.
DR ChiTaRS; CYB561A3; human.
DR Proteomes; UP000005640; Chromosome 11.
DR Bgee; ENSG00000162144; Expressed in right adrenal gland and 176 other cell types or tissues.
DR ExpressionAtlas; F5H0P5; baseline and differential.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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:SF0; LYSOSOMAL MEMBRANE ASCORBATE-DEPENDENT FERRIREDUCTASE CYB561A3; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
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 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..182
FT /note="Cytochrome b561"
FT /evidence="ECO:0000259|PROSITE:PS50939"
FT NON_TER 182
FT /evidence="ECO:0000313|Ensembl:ENSP00000438725.1"
SQ SEQUENCE 182 AA; 20598 MW; E3F6CF6822476C96 CRC64;
MVSGRFYLSC LLLGSLGSMC ILFTIYWMQY WRGGFAWNGS IYMFNWHPVL MVAGMVVFYG
GASLVYRLPQ SWVGPKLPWK LLHAALHLMA FVLTVVGLVA VFTFHNHGRT ANLYSLHSWL
GITTVFLFAC QWFLGFAVFL LPWASMWLRS LLKPIHVFFG AAILSLSIAS VISGINEKLF
FS
//
