FRRS1_DANRE
ID FRRS1_DANRE Reviewed; 573 AA.
AC A4QP81;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Putative ferric-chelate reductase 1;
DE EC=1.-.-.-;
GN Name=frrs1; ORFNames=zgc:163022;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Putative ferric-chelate reductases reduce Fe(3+) to Fe(2+)
CC before its transport from the endosome to the cytoplasm.
CC {ECO:0000250|UniProtKB:Q8K385}.
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 -!- SIMILARITY: Belongs to the FRRS1 family. {ECO:0000305}.
CC -!- CAUTION: The cytochrome b561 domain lacks the conserved His residue
CC that binds iron in the heme. The reductase activity is therefore unsure
CC in vivo. {ECO:0000305}.
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DR EMBL; BC139692; AAI39693.1; -; mRNA.
DR RefSeq; NP_001083026.1; NM_001089557.1.
DR AlphaFoldDB; A4QP81; -.
DR SMR; A4QP81; -.
DR GeneID; 100038777; -.
DR KEGG; dre:100038777; -.
DR ZFIN; ZDB-GENE-070424-101; zgc:163022.
DR InParanoid; A4QP81; -.
DR PhylomeDB; A4QP81; -.
DR PRO; PR:A4QP81; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd08544; Reeler; 1.
DR Gene3D; 2.60.40.4060; -; 1.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR002861; Reeler_dom.
DR InterPro; IPR042307; Reeler_sf.
DR Pfam; PF02014; Reeler; 1.
DR SMART; SM00665; B561; 1.
DR SMART; SM00664; DoH; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
DR PROSITE; PS50836; DOMON; 1.
DR PROSITE; PS51019; REELIN; 1.
PE 2: Evidence at transcript level;
KW Electron transport; Glycoprotein; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..573
FT /note="Putative ferric-chelate reductase 1"
FT /id="PRO_0000314845"
FT TRANSMEM 4..24
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT DOMAIN 15..181
FT /note="Reelin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00363"
FT DOMAIN 213..328
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT DOMAIN 332..532
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 370
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 411
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 441
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 477
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 CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 573 AA; 61284 MW; 2A254A784C40B865 CRC64;
MDGVCKSPQR LLFVLVSCFG LVQSYKNGLV SSVCGSMMPN HGANAQISSP PFTVTADKTT
FKEGDQITVT LNSQTGYQFE GFMLQARQVG SSSSIGTFSV TASNMQLLTC DGVSARSVSH
TSNSKKSSIQ AKWTAPTSGQ LGNIQFSVTF VKSDDTFWVG VKSSAVVYNG AGTTGTSTTP
ATVAPTVASI PGCGTTKVCF SQPNNCDPTT STGCYFVAVQ ASSDQSEMRI EMFGPADGYV
AIGFSDDQQM GNDDVYICGK DNNGNLQVQH AFNSGRSRPA ILSLGNVTDI LTAVTNGNIN
CSFISRNTIS TASRAATTNE YYLMIAAGSS SQGNIQFHTN KYVTSTKVNL LNPSVVITSE
EEFPPMVKAH GCLMLISWMA TGSIGMIIAR YLKGVAKGQG CFGKDFWFVA HVSLMTLSII
ATAIAFIIVF VSAGDWAGGA HPVLGCLVMI LSLIQPIVAA FRCEPQHERR FVFNWAHSCN
AFAIKCLAVA AIFTGLALFE EYDSDGWMLK VMGGYLAWEA LMYILQDLNL RAKKKDSQLC
SCEPMRPETI LLFLFIIGNL AFLIALLVGI GSA
