C56D2_BOVIN
ID C56D2_BOVIN Reviewed; 222 AA.
AC Q5E965; Q29S15;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Transmembrane reductase CYB561D2 {ECO:0000250|UniProtKB:O14569};
DE EC=7.2.1.3 {ECO:0000250|UniProtKB:O14569};
DE AltName: Full=Cytochrome b561 domain-containing protein 2 {ECO:0000250|UniProtKB:O14569};
GN Name=CYB561D2 {ECO:0000250|UniProtKB:O14569};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transmembrane reductase that may use ascorbate as an electron
CC donor in the cytoplasm and transfer electrons across endoplasmic
CC reticulum membranes to reduce monodehydro-L-ascorbate radical and iron
CC cations Fe(3+) in the lumen of that compartment.
CC {ECO:0000250|UniProtKB:O14569}.
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:0000250|UniProtKB:O14569};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66525;
CC Evidence={ECO:0000250|UniProtKB:O14569};
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:0000250|UniProtKB:Q9WUE3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30404;
CC Evidence={ECO:0000250|UniProtKB:Q9WUE3};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q9WUE3};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:Q9WUE3};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9WUE3}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53TN4}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9WUE3}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53TN4}.
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DR EMBL; BT021055; AAX09072.1; -; mRNA.
DR EMBL; BC113226; AAI13227.1; -; mRNA.
DR RefSeq; NP_001014937.1; NM_001014937.2.
DR RefSeq; XP_005222905.1; XM_005222848.3.
DR RefSeq; XP_005222906.1; XM_005222849.3.
DR AlphaFoldDB; Q5E965; -.
DR SMR; Q5E965; -.
DR STRING; 9913.ENSBTAP00000025505; -.
DR PaxDb; Q5E965; -.
DR Ensembl; ENSBTAT00000025505; ENSBTAP00000025505; ENSBTAG00000019163.
DR GeneID; 523966; -.
DR KEGG; bta:523966; -.
DR CTD; 11068; -.
DR VEuPathDB; HostDB:ENSBTAG00000019163; -.
DR eggNOG; ENOG502QRPJ; Eukaryota.
DR GeneTree; ENSGT00440000038072; -.
DR HOGENOM; CLU_072399_3_0_1; -.
DR InParanoid; Q5E965; -.
DR OMA; ATWHGWA; -.
DR OrthoDB; 1586923at2759; -.
DR TreeFam; TF323584; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000019163; Expressed in thyroid gland and 105 other tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0140575; F:transmembrane monodehydroascorbate reductase activity; ISS:UniProtKB.
DR GO; GO:0140576; P:ascorbate homeostasis; ISS:UniProtKB.
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 Cytoplasmic vesicle; Electron transport; Endoplasmic reticulum; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14569"
FT CHAIN 2..222
FT /note="Transmembrane reductase CYB561D2"
FT /id="PRO_0000151035"
FT TOPO_DOM 2..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..46
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..122
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..186
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT DOMAIN 14..217
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 48
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 86
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 120
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 159
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 222 AA; 24077 MW; B19AB4A9258556A3 CRC64;
MALSVETESH IYRALRTVSG AAAHLVALGF TIFVAVLARP GSSLFSWHPV LMSLAFSFLM
TEALLVFSPE SSLLRSLSRK GRARCHWVLQ LLALLCALLG LGLVILHKEQ LGKAHLATWH
GRAGLLAVLW AGLQCSGGVG LLYPKLLPRW PLAKLKLYHA TSGLVGYLLG GASLLLGMCS
LWFTATVTGG VWYLAVLCPV ITSLVIMNQV SNAYLYRKRI QP
