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Database: UniProt
Entry: G5BDK1_HETGA
LinkDB: G5BDK1_HETGA
Original site: G5BDK1_HETGA 
ID   G5BDK1_HETGA            Unreviewed;       252 AA.
AC   G5BDK1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   ORFNames=GW7_17464 {ECO:0000313|EMBL:EHB07362.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB07362.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB07362.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
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   EMBL; JH169663; EHB07362.1; -; Genomic_DNA.
DR   RefSeq; XP_004868654.1; XM_004868597.2.
DR   RefSeq; XP_012922532.1; XM_013067078.1.
DR   RefSeq; XP_012922533.1; XM_013067079.1.
DR   RefSeq; XP_012922534.1; XM_013067080.1.
DR   AlphaFoldDB; G5BDK1; -.
DR   STRING; 10181.G5BDK1; -.
DR   Ensembl; ENSHGLT00100007327; ENSHGLP00100007233; ENSHGLG00100032823.
DR   GeneID; 101699814; -.
DR   eggNOG; KOG1619; Eukaryota.
DR   InParanoid; G5BDK1; -.
DR   OMA; EFHYHPT; -.
DR   OrthoDB; 2877457at2759; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   Bgee; ENSHGLG00000011329; Expressed in pituitary gland and 10 other cell types or tissues.
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   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:UP000006813};
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        16..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        200..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..221
FT                   /note="Cytochrome b561"
FT                   /evidence="ECO:0000259|PROSITE:PS50939"
SQ   SEQUENCE   252 AA;  27911 MW;  77FCDB89FEED7E78 CRC64;
     MESGTGLGST PSTLPYYVAF SQLLGLTVVA MTGAWLGLYR GGIAWESALQ FNVHPLCMVI
     GLIFLQGDAL LVYRVFRKEA KHTTKVLHGL LHVFAFIISL VGLVAVFDYH RKMGYADLYS
     LHSWCGILVF VLYFVQWLVG FSFFLFPGAS FSLRSRYRPQ HIFFGATIFL LSVGTALLGL
     KEAVLFKLGN KYSMFEPEGI LANVLGLLLA CFGVAVLYIL AQADWKRPPQ AEEQALSMDF
     KTLTEGDSPS SQ
//
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