ID A0A3B5BM55_9TELE Unreviewed; 252 AA.
AC A0A3B5BM55;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
GN Name=CYB561A3 {ECO:0000313|Ensembl:ENSSPAP00000029792.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000029792.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000029792.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B5BM55; -.
DR STRING; 144197.ENSSPAP00000029792; -.
DR Ensembl; ENSSPAT00000030275.1; ENSSPAP00000029792.1; ENSSPAG00000022379.1.
DR GeneTree; ENSGT00950000183197; -.
DR Proteomes; UP000261400; Unplaced.
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 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 45..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..218
FT /note="Cytochrome b561"
FT /evidence="ECO:0000259|PROSITE:PS50939"
SQ SEQUENCE 252 AA; 28282 MW; C4A93D09FE7AF770 CRC64;
MKPSMLFSVS YGLCLALSLL SVIFVICWSS RWRGGFAWDR SALQFNWHPV LMVSGLVVLY
GNAAVVYRVP FTWKQRKSTW KLVHAGLMLL ALLLAILGLC AVFDFHRGFH IRDLYSLHSW
VGICTVVTFA FQWVLGLAAF LLPCSTQRLR SALKPVHIWL GKAILILSLT SSISGINEKL
LLTLTGAPYS SLPVEAKFAN SLGIFILAFG MIVFGILSKK EWRWPQRQES AYVSMDLITI
IFVLLLITAT KK
//
