CYAC3_RAT
ID CYAC3_RAT Reviewed; 256 AA.
AC Q5U2W7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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:0000312|RGD:1304670};
DE AltName: Full=Cytochrome b561 family member A3 {ECO:0000312|RGD:1304670};
DE AltName: Full=Lysosomal cytochrome b {ECO:0000250|UniProtKB:Q6P1H1};
DE Short=LCytb {ECO:0000250|UniProtKB:Q6P1H1};
GN Name=Cyb561a3 {ECO:0000312|RGD:1304670};
GN Synonyms=Cybasc3 {ECO:0000312|RGD:1304670};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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: 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; BC085835; AAH85835.1; -; mRNA.
DR RefSeq; NP_001014186.1; NM_001014164.1.
DR RefSeq; XP_006231112.1; XM_006231050.3.
DR RefSeq; XP_006231113.1; XM_006231051.3.
DR RefSeq; XP_006231114.1; XM_006231052.3.
DR RefSeq; XP_006231115.1; XM_006231053.3.
DR RefSeq; XP_006231116.1; XM_006231054.3.
DR RefSeq; XP_006231117.1; XM_006231055.3.
DR AlphaFoldDB; Q5U2W7; -.
DR SMR; Q5U2W7; -.
DR STRING; 10116.ENSRNOP00000028094; -.
DR GlyGen; Q5U2W7; 1 site.
DR PaxDb; Q5U2W7; -.
DR PRIDE; Q5U2W7; -.
DR GeneID; 361729; -.
DR KEGG; rno:361729; -.
DR UCSC; RGD:1304670; rat.
DR CTD; 220002; -.
DR RGD; 1304670; Cyb561a3.
DR VEuPathDB; HostDB:ENSRNOG00000020702; -.
DR eggNOG; KOG1619; Eukaryota.
DR HOGENOM; CLU_069712_1_3_1; -.
DR InParanoid; Q5U2W7; -.
DR OMA; FAWDGSI; -.
DR PhylomeDB; Q5U2W7; -.
DR TreeFam; TF314222; -.
DR PRO; PR:Q5U2W7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020702; Expressed in spleen and 18 other tissues.
DR Genevisible; Q5U2W7; RN.
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:0005764; C:lysosome; ISO:RGD.
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..256
FT /note="Lysosomal membrane ascorbate-dependent
FT ferrireductase CYB561A3"
FT /id="PRO_0000314840"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..40
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..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..202
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..256
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 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 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 256 AA; 28650 MW; 59ADA7D62A162BE5 CRC64;
MASGWFYMSC MVLGSLGSMC ILFTTYWMQY WRGGFAWDGT VLMFNWHPVL MVSGMVVLYG
AASLVYRLPA SWVGPKLPWK VLHAALHLLA FTVTVVGLTA VFGFHNHSKI THLYSLHSWL
GITTVALFAC QWFLGFAVFL LPWASQWLRS LLKPVHVFFG ACILSLSIAS VISGINEKLF
FVLKNATRPY SSLPGEAVFA NSTGILVVSF GLLVLYILLA SSWRRPDPGA LTDRQVWLLV
SHYRWDKAKK ACFAPC
