GenomeNet

Database: UniProt
Entry: A0A060WDC7_ONCMY
LinkDB: A0A060WDC7_ONCMY
Original site: A0A060WDC7_ONCMY 
ID   A0A060WDC7_ONCMY        Unreviewed;       237 AA.
AC   A0A060WDC7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
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   ORFNames=GSONMT00067414001 {ECO:0000313|EMBL:CDQ62570.1};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ62570.1, ECO:0000313|Proteomes:UP000193380};
RN   [1] {ECO:0000313|EMBL:CDQ62570.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24755649; DOI=10.1038/ncomms4657;
RA   Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA   Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA   Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA   Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA   Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA   Guiguen Y.;
RT   "The rainbow trout genome provides novel insights into evolution after
RT   whole-genome duplication in vertebrates.";
RL   Nat. Commun. 5:3657-3657(2014).
RN   [2] {ECO:0000313|EMBL:CDQ62570.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; FR904411; CDQ62570.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A060WDC7; -.
DR   STRING; 8022.A0A060WDC7; -.
DR   PaxDb; 8022-A0A060WDC7; -.
DR   Proteomes; UP000193380; Unassembled WGS sequence.
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:UP000193380};
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        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        101..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        170..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          66..237
FT                   /note="Cytochrome b561"
FT                   /evidence="ECO:0000259|PROSITE:PS50939"
SQ   SEQUENCE   237 AA;  26452 MW;  5126B51D46915464 CRC64;
     MHDYTPPNTC STPSECLHLS QWNETMECGS ELAVDTMKKE LKSRAILADC STRMRSIVSF
     YFCYLLCLCL GIACVVFVSI WNSQWRGGFA WDGSALQFNW HPVLMVTGLV VLYGNGAVLY
     RIPLTWGQNK LPWKLLHAGV MLLALLCSIL GLCAVFDFHH TNSTPNLYSL HSWIGICTTA
     LFTTQWVMGL AGFLLPCSPM SFRKLLKPAH VWMGGCILIL SIVSCISGIN EKLFFAL
//
DBGET integrated database retrieval system