ID A0A2K6M141_RHIBE Unreviewed; 258 AA.
AC A0A2K6M141;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Transmembrane ascorbate-dependent reductase CYB561 {ECO:0000256|ARBA:ARBA00024231};
DE AltName: Full=Cytochrome b-561 {ECO:0000256|ARBA:ARBA00030896};
DE AltName: Full=Cytochrome b561 {ECO:0000256|ARBA:ARBA00032709};
GN Name=CYB561 {ECO:0000313|Ensembl:ENSRBIP00000029493.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000029493.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000029493.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000029493.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule membrane {ECO:0000256|ARBA:ARBA00024185}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00024185}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_017738404.1; XM_017882915.1.
DR RefSeq; XP_017738405.1; XM_017882916.1.
DR AlphaFoldDB; A0A2K6M141; -.
DR Ensembl; ENSRBIT00000053443.1; ENSRBIP00000029493.1; ENSRBIG00000038628.1.
DR GeneID; 108536286; -.
DR KEGG; rbb:108536286; -.
DR GeneTree; ENSGT00950000183197; -.
DR OrthoDB; 2877457at2759; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd08763; Cyt_b561_CYB561; 1.
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:SF14; TRANSMEMBRANE ASCORBATE-DEPENDENT REDUCTASE CYB561; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
PE 4: Predicted;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
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 Reference proteome {ECO:0000313|Proteomes:UP000233180};
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 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..227
FT /note="Cytochrome b561"
FT /evidence="ECO:0000259|PROSITE:PS50939"
SQ SEQUENCE 258 AA; 28262 MW; 15572952E81FCC36 CRC64;
MSSVCLSMEG GAAASTPAAL PYYVAFSQLL GLTLVAMTGA WLGLYRGGIA WESDLQFNAH
PLCMVIGLVF LQGDALLVYR VFRNEAKRTT KVLHGLLHVF ALVIALVGLV AVFDYHRKKG
YTDLYSLHSW CGILVFVLYL VQWLAGFSFF LFPGAPFSLR SRYRPQHIFF GATIFLLSVG
TALLGLKEAL LFNLGDKYSA FEPEGVLANV LGLLLACFGG AVLYILTRAD WKRPSQAEEQ
ALSMDFKTLT EGDSPGSQ
//
