C56D1_MOUSE
ID C56D1_MOUSE Reviewed; 229 AA.
AC A2AE42; B2RPT5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Probable transmembrane reductase CYB561D1 {ECO:0000305};
DE EC=7.2.1.3 {ECO:0000305};
DE AltName: Full=Cytochrome b561 domain-containing protein 1 {ECO:0000312|MGI:MGI:1919273};
GN Name=Cyb561d1 {ECO:0000312|MGI:MGI:1919273};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probable transmembrane reductase that may use ascorbate as an
CC electron donor and transfer electrons across membranes to reduce
CC monodehydro-L-ascorbate radical and iron cations Fe(3+) in another
CC cellular compartment. {ECO:0000305}.
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:0000305};
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:0000305};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:Q53TN4};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; AL671854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137590; AAI37591.1; -; mRNA.
DR CCDS; CCDS38598.1; -.
DR RefSeq; NP_001074789.2; NM_001081320.2.
DR AlphaFoldDB; A2AE42; -.
DR SMR; A2AE42; -.
DR STRING; 10090.ENSMUSP00000102266; -.
DR PhosphoSitePlus; A2AE42; -.
DR EPD; A2AE42; -.
DR PaxDb; A2AE42; -.
DR PRIDE; A2AE42; -.
DR ProteomicsDB; 273860; -.
DR Antibodypedia; 20066; 114 antibodies from 21 providers.
DR Ensembl; ENSMUST00000106655; ENSMUSP00000102266; ENSMUSG00000048796.
DR GeneID; 72023; -.
DR KEGG; mmu:72023; -.
DR UCSC; uc008qyi.1; mouse.
DR CTD; 284613; -.
DR MGI; MGI:1919273; Cyb561d1.
DR VEuPathDB; HostDB:ENSMUSG00000048796; -.
DR eggNOG; ENOG502RYMK; Eukaryota.
DR GeneTree; ENSGT00440000038072; -.
DR HOGENOM; CLU_072399_3_0_1; -.
DR InParanoid; A2AE42; -.
DR OMA; WFQATVK; -.
DR OrthoDB; 1586923at2759; -.
DR PhylomeDB; A2AE42; -.
DR TreeFam; TF323584; -.
DR BioGRID-ORCS; 72023; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Cyb561d1; mouse.
DR PRO; PR:A2AE42; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; A2AE42; protein.
DR Bgee; ENSMUSG00000048796; Expressed in granulocyte and 90 other tissues.
DR ExpressionAtlas; A2AE42; baseline and differential.
DR Genevisible; A2AE42; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0140571; F:transmembrane ascorbate ferrireductase activity; IEA:UniProtKB-EC.
DR GO; GO:0140575; F:transmembrane monodehydroascorbate reductase activity; IEA:InterPro.
DR InterPro; IPR045150; CYB561D1/2.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR PANTHER; PTHR15422; PTHR15422; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
PE 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..229
FT /note="Probable transmembrane reductase CYB561D1"
FT /id="PRO_0000320295"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..53
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..128
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..193
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 22..224
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 55
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 93
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 127
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 166
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
SQ SEQUENCE 229 AA; 25519 MW; 08C734B1E25DECD0 CRC64;
MHSMEVGLVP APAREPRLTR WLRRGSGILA HLIALGFTIF LTVLSRPGTS LFSWHPVFMA
LAFCLCMAEA ILLFSPEHSL FFFCSRKTRI RLHWAGQTMA ILCAVLGLGF IISSKIRSEM
SHLVSWHSWI GALTLLATGG QALCGLCLLC PRAARVSRVA RLKLYHLTCG LVVYLMATVT
VLLGMYSVWF QAQIKGTAWY LCLGLPLYPA LVIMHQISSS YLPRKKVEI
