CYAC3_BOVIN
ID CYAC3_BOVIN Reviewed; 265 AA.
AC A5D9A7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Lysosomal membrane ascorbate-dependent ferrireductase CYB561A3 {ECO:0000305};
DE EC=7.2.1.3 {ECO:0000250|UniProtKB:Q6P1H1};
DE AltName: Full=Cytochrome b ascorbate-dependent protein 3 {ECO:0000250|UniProtKB:Q6P1H1};
DE AltName: Full=Lysosomal cytochrome b {ECO:0000250|UniProtKB:Q6P1H1};
DE Short=LCytb {ECO:0000250|UniProtKB:Q6P1H1};
GN Name=CYB561A3 {ECO:0000250|UniProtKB:Q6P1H1};
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=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transmembrane reductase that uses ascorbate as an electron
CC donor in the cytoplasm and transfers electrons across membranes to
CC reduce iron cations Fe(3+) into Fe(2+) in the lumen of the late
CC endosome and lysosome. Reduced iron can then be extruded from the late
CC endosome and lysosome to the cytoplasm by divalent metal-specific
CC transporters. It is therefore most probably involved in endosomal and
CC lysosomal cellular iron homeostasis. {ECO:0000250|UniProtKB:Q6P1H1}.
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:Q6P1H1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30404;
CC Evidence={ECO:0000250|UniProtKB:Q6P1H1};
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q53TN4}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q6P1H1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53TN4}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q6P1H1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53TN4}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6P1H1}.
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DR EMBL; BT030526; ABQ12966.1; -; mRNA.
DR EMBL; BC146220; AAI46221.1; -; mRNA.
DR RefSeq; NP_001092619.1; NM_001099149.1.
DR RefSeq; XP_005227004.1; XM_005226947.3.
DR AlphaFoldDB; A5D9A7; -.
DR SMR; A5D9A7; -.
DR STRING; 9913.ENSBTAP00000024228; -.
DR PaxDb; A5D9A7; -.
DR PRIDE; A5D9A7; -.
DR Ensembl; ENSBTAT00000024228; ENSBTAP00000024228; ENSBTAG00000018202.
DR GeneID; 615893; -.
DR KEGG; bta:615893; -.
DR CTD; 220002; -.
DR VEuPathDB; HostDB:ENSBTAG00000018202; -.
DR VGNC; VGNC:50258; CYB561A3.
DR eggNOG; KOG1619; Eukaryota.
DR GeneTree; ENSGT00950000183197; -.
DR HOGENOM; CLU_069712_1_3_1; -.
DR InParanoid; A5D9A7; -.
DR OMA; FAWDGSI; -.
DR OrthoDB; 1503869at2759; -.
DR TreeFam; TF314222; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000018202; Expressed in retropharyngeal lymph node and 105 other tissues.
DR ExpressionAtlas; A5D9A7; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
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:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR InterPro; IPR043205; CYB561/CYBRD1-like.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR PANTHER; PTHR10106; PTHR10106; 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; Endosome; Glycoprotein; Heme; Iron; Lysosome; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..265
FT /note="Lysosomal membrane ascorbate-dependent
FT ferrireductase CYB561A3"
FT /id="PRO_0000314837"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..45
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..119
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..197
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT DOMAIN 12..219
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT REGION 228..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
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 67
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 76
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 80
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 83
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 112..115
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 117
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 149
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 156
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 177
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 224
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 265 AA; 29803 MW; 3DD4E0ECFDCD244D CRC64;
MAVGWFYLSV LALCSLGSMC ILFTIYWMRY WHGGFAWDGS MLMFNWHPVL MVTGMVVLYS
AASLVYRLPQ SWVGPRLPWK SGHAAMHLLA FLLTVLGLHA VFEFHNHAKI PHLYSLHSWL
GITTVFLFAC QWFLGFSVFL LPWASMWLRS LLKPIHVFFG ASILSLAIAS VVSGINEKLF
FSLKNGTKTY SNLPSEAVFA NCAGMLVVVF GLLVLYILLA SSWKRPEPGM QAEREPTRTR
GRAGTPEVML EGERGLAEPL LQKRS
