FRO4_ARATH
ID FRO4_ARATH Reviewed; 699 AA.
AC Q8W110; Q9FLW3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ferric reduction oxidase 4;
DE Short=AtFRO4;
DE EC=1.16.1.7;
DE AltName: Full=Ferric-chelate reductase 4;
GN Name=FRO4; OrderedLocusNames=At5g23980; ORFNames=MZF18.140;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16006655; DOI=10.1093/pcp/pci163;
RA Wu H., Li L., Du J., Yuan Y., Cheng X., Ling H.Q.;
RT "Molecular and biochemical characterization of the Fe(III) chelate
RT reductase gene family in Arabidopsis thaliana.";
RL Plant Cell Physiol. 46:1505-1514(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16362328; DOI=10.1007/s00425-005-0165-0;
RA Mukherjee I., Campbell N.H., Ash J.S., Connolly E.L.;
RT "Expression profiling of the Arabidopsis ferric chelate reductase (FRO)
RT gene family reveals differential regulation by iron and copper.";
RL Planta 223:1178-1190(2006).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX DOI=10.1016/j.plantsci.2009.02.011;
RA Jeong J., Connolly E.L.;
RT "Iron uptake mechanisms in plants: Functions of the FRO family of ferric
RT reductases.";
RL Plant Sci. 176:709-714(2009).
RN [7]
RP FUNCTION, AND INDUCTION BY COPPER DEFICIENCY.
RX PubMed=22374396; DOI=10.1105/tpc.111.090431;
RA Bernal M., Casero D., Singh V., Wilson G.T., Grande A., Yang H.,
RA Dodani S.C., Pellegrini M., Huijser P., Connolly E.L., Merchant S.S.,
RA Kraemer U.;
RT "Transcriptome sequencing identifies SPL7-regulated copper acquisition
RT genes FRO4/FRO5 and the copper dependence of iron homeostasis in
RT Arabidopsis.";
RL Plant Cell 24:738-761(2012).
CC -!- FUNCTION: Ferric chelate reductase. May participate in the transport of
CC electrons to a Fe(3+) ion via FAD and heme intermediates
CC (PubMed:16006655). May function as root surface cupric chelate
CC reductase and participate in the reduction of Cu(2+), for Cu(+)
CC acquisition via Cu(+) transporters in response to copper deficiency
CC (PubMed:22374396). {ECO:0000269|PubMed:16006655,
CC ECO:0000269|PubMed:22374396}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-
CC siderophore + NADH; Xref=Rhea:RHEA:15061, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.16.1.7;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques. Detected at low levels in
CC roots, cotyledon veins and shoots. {ECO:0000269|PubMed:16006655,
CC ECO:0000269|PubMed:16362328}.
CC -!- INDUCTION: Induced by copper deficiency in a SPL7-dependent manner.
CC {ECO:0000269|PubMed:22374396}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08721.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB009056; BAB08721.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93241.1; -; Genomic_DNA.
DR EMBL; AF462813; AAL58904.1; -; mRNA.
DR EMBL; BT010474; AAQ65097.1; -; mRNA.
DR RefSeq; NP_197786.2; NM_122303.3.
DR AlphaFoldDB; Q8W110; -.
DR SMR; Q8W110; -.
DR BioGRID; 17738; 2.
DR STRING; 3702.AT5G23980.1; -.
DR PaxDb; Q8W110; -.
DR PRIDE; Q8W110; -.
DR ProteomicsDB; 230044; -.
DR EnsemblPlants; AT5G23980.1; AT5G23980.1; AT5G23980.
DR GeneID; 832463; -.
DR Gramene; AT5G23980.1; AT5G23980.1; AT5G23980.
DR KEGG; ath:AT5G23980; -.
DR Araport; AT5G23980; -.
DR TAIR; locus:2178677; AT5G23980.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_014777_1_0_1; -.
DR InParanoid; Q8W110; -.
DR OMA; YRGLWDM; -.
DR OrthoDB; 190356at2759; -.
DR PhylomeDB; Q8W110; -.
DR BioCyc; ARA:AT5G23980-MON; -.
DR PRO; PR:Q8W110; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W110; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0140618; F:ferric-chelate reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; -; 2.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Electron transport; FAD; Flavoprotein; Heme; Ion transport; Iron; Membrane;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..699
FT /note="Ferric reduction oxidase 4"
FT /id="PRO_0000413202"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..29
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 30..54
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..73
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 74..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..125
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 126..190
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..214
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 215..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..289
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 290..311
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 333..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..548
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 549..568
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..590
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 591..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 157..275
FT /note="Ferric oxidoreductase"
FT DOMAIN 305..408
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 192
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 354..357
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 400..403
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 699 AA; 80251 MW; 297A607E2B49C8AE CRC64;
MGNMRSLVKT LMVVLFLGWI LVWIMISTNL FKSKWTPKLS KYLNTTYFGP QGTNLVLLTV
PMMFIAVLSC VYLHIQKKPT QPQREWKLKR IMGRVIMVMN PLGIVTATEL TFSLLFVALL
AWSLYNYLYL SYHVHLHNDD NAKIWQAKFR AFGLRIGYVG NICWAFLFFP VTRASTILPL
VGLTSESSIK YHIWLGHVSN FCFLVHTVVF LIYWAMINKL METFAWNPTY VPNLAGTIAM
VIGIAMWVTS LPSFRRKKFE IFFYTHHLYG LYIVFYVIHV GDSWFCMILP NIFLFFIDRY
LRFLQSTKRS RLVSARILPS DNLELTFSKT PGLHYTPTSI LFLHVPSISK IQWHPFTITS
SSNLEKDTLS VVIRRQGSWT QKLYTHLSSS IDSLEVSTEG PYGPNSFDVS RHNSLILVSG
GSGITPFISV IRELISQSQN KSTKLPDVLL VCSFKHYHDL AFLDLIFPLD MSASDISRLN
LRIEAYITRE DKKPETTDDH RLLQTKWFKP QPLDSPISPV LGPNNFLWLG VVILSSFVMF
LLLIGIVTRY YIYPVDHNTG SIYNFSYRGL WDMFLGSACI FISSSVVFLW RKKQNKEGDK
EFKNQVQSVE FQTPTSSPGS WFHGHERELE SVPYQSIVQA TSVHFGSKPN LKKILLEAEG
SEDVGVMVCG PRKMRHEVAK ICSSGLAKNL HFEAISFNW
