FRRS1_BOVIN
ID FRRS1_BOVIN Reviewed; 591 AA.
AC A2VE04;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Ferric-chelate reductase 1;
DE EC=1.-.-.-;
GN Name=FRRS1;
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].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ferric-chelate reductases reduce Fe(3+) to Fe(2+) before its
CC 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}.
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DR EMBL; BC133504; AAI33505.1; -; mRNA.
DR RefSeq; NP_001077164.1; NM_001083695.1.
DR AlphaFoldDB; A2VE04; -.
DR SMR; A2VE04; -.
DR STRING; 9913.ENSBTAP00000004475; -.
DR PaxDb; A2VE04; -.
DR GeneID; 516522; -.
DR KEGG; bta:516522; -.
DR CTD; 391059; -.
DR eggNOG; KOG4293; Eukaryota.
DR HOGENOM; CLU_028305_2_1_1; -.
DR InParanoid; A2VE04; -.
DR OrthoDB; 599276at2759; -.
DR Proteomes; UP000009136; 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:0016722; F:oxidoreductase activity, acting on metal ions; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
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; Heme; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..591
FT /note="Ferric-chelate reductase 1"
FT /id="PRO_0000314842"
FT TRANSMEM 6..26
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
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 490..510
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT DOMAIN 13..179
FT /note="Reelin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00363"
FT DOMAIN 216..331
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT DOMAIN 335..533
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 373
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 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 591 AA; 65660 MW; 80ED278CA93D3351 CRC64;
MTAPGFTVSA FILLLHVSFV ANYPSGKVTK SCGGMIPEHG HTPQSHPAHN ISVSQKTFRP
GDQIKVTLSG PPFKGFLLEA RDAENLSGPP VGSFTLIDSH VSQLLTCEDV QGSAVSHRSP
SKKTEIKVFW DAPSGAPNHI TFLATVVEKY KIYWVKIPGP VISQPNVPPF TTPEATIAPM
PTVPSVSHLT RSFNASDCGN KKFCIRSPLN CDPEKERACV LLSFTRDDQS VMVEMSGPSK
GYLSVAFSHD RWMGDDDAYV CILEDQIVHI QPSHLTGRSH PIMDFGDPLE DMAWRLVDGV
MQCSFRRNIT LPGVKNRFDL NASYYIFVAD GAAVDGRIHK HSQQPLITYE KYNVTGDPKN
IGGSHSLLLL KVHGALMFVA WMTTVSVGVL IARFFKPVWS KALFGDAAWF QVHRTLMLTT
SALTFIAFLL PFIYRGGWNW HAGYHPYLGF IVMVLAVLQL LLAAFRPPLH DPRRQMFNWT
HWSMGTAARI IAVAAMFLGM DLPGLNLPGP WKTYAMIGFV AWHVGTEIIL EIHAYRLSRK
VEILDDDRIQ ILQSFTAAEA EGYVFKKVVL AIYVCGNLTF LTMFLSAINR L
