FRRS1_XENLA
ID FRRS1_XENLA Reviewed; 590 AA.
AC Q6INU7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Putative ferric-chelate reductase 1;
DE EC=1.-.-.-;
GN Name=frrs1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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; BC072175; AAH72175.1; -; mRNA.
DR RefSeq; NP_001085128.1; NM_001091659.1.
DR AlphaFoldDB; Q6INU7; -.
DR SMR; Q6INU7; -.
DR PRIDE; Q6INU7; -.
DR DNASU; 432203; -.
DR GeneID; 432203; -.
DR KEGG; xla:432203; -.
DR CTD; 432203; -.
DR Xenbase; XB-GENE-989223; frrs1.L.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 432203; Expressed in intestine and 16 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PF03188; Cytochrom_B561; 1.
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..590
FT /note="Putative ferric-chelate reductase 1"
FT /id="PRO_0000314846"
FT TRANSMEM 2..22
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT DOMAIN 12..179
FT /note="Reelin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00363"
FT DOMAIN 217..330
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT DOMAIN 334..533
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 372
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 413
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 445
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 481
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 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 590 AA; 66124 MW; C7B40DFF8C66A89F CRC64;
MNPLGLFLIY LYTCALTPVS GYPNGKVTSA CRSMRPDHGH APQSEPIHSI NVEKTIFKPG
DRIKVTLSGS RFDGFLVQAR DAENLEGSAV GSFSLTDERI SQLLTCDGIQ NSAVSHTSKE
RKLQVELFWI APANSPKHIQ FLATVVEKYK IYWVKIPGPI ISQPKAPSIA PKIPSSTIPV
VPPPSLSLHK RFNSAGCGSS KFCIRNPVSC DPEHNPECFF LSFRKDGQSV LVEMSGPGQG
YISFALSHDQ WMGDDDAYLC VKEDDGVQIN PAYIRGRSHP EVSSMDVLRD VAWRLEDGVI
QCSFRRNIQI PIPKERFDLG RSYFIFLADG DAKDGLLYRH HRQPLMTNRK YCITDFPEDV
GGSRSPLIIK LHGAMMFIAW MTTVSIGVII ARFFKPVWPT SSLFGEKIWF QIHRCLMITT
VFLTVVAFVL PFIYRGYFSK RAGYHPHLGV TVMILTVLQP VLAVFRPPPQ THRRGIFNWT
HWATGTAARI IAVAAMFLGM DLQALDLPDP WDTYTMIGFV LWHVFVDLLL EAHGFCLLKK
AKTMEEDQIG ILNSSPDEAE GHTFKKIVMT VYICGNLAFL ITFLAAINQL
