FRO2_ARATH
ID FRO2_ARATH Reviewed; 725 AA.
AC P92949; Q9LMM3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ferric reduction oxidase 2;
DE Short=AtFRO2;
DE EC=1.16.1.7;
DE AltName: Full=Ferric-chelate reductase 2;
DE AltName: Full=Protein FERRIC CHELATE REDUCTASE DEFECTIVE 1;
GN Name=FRO2; Synonyms=FRD1; OrderedLocusNames=At1g01580; ORFNames=F22L4.12;
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 [GENOMIC DNA / MRNA], FUNCTION, MUTAGENESIS OF THR-384,
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY IRON.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10067892; DOI=10.1038/17800;
RA Robinson N.J., Procter C.M., Connolly E.L., Guerinot M.L.;
RT "A ferric-chelate reductase for iron uptake from soils.";
RL Nature 397:694-697(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root;
RA Yang J.H., Liu Y.J., Yang E.Q., Liu S.W., Liu Y.D., Li J.K., Wu C.X.;
RT "Molecular Cloning of the FRO2 Gene from Arabidopsis roots.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
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 [6]
RP INDUCTION.
RX PubMed=12805609; DOI=10.1104/pp.102.016089;
RA Vert G.A., Briat J.F., Curie C.;
RT "Dual regulation of the Arabidopsis high-affinity root iron uptake system
RT by local and long-distance signals.";
RL Plant Physiol. 132:796-804(2003).
RN [7]
RP FUNCTION, INDUCTION BY IRON; CADMIUM AND ZINC, AND TISSUE SPECIFICITY.
RX PubMed=14526117; DOI=10.1104/pp.103.025122;
RA Connolly E.L., Campbell N.H., Grotz N., Prichard C.L., Guerinot M.L.;
RT "Overexpression of the FRO2 ferric chelate reductase confers tolerance to
RT growth on low iron and uncovers posttranscriptional control.";
RL Plant Physiol. 133:1102-1110(2003).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION BY IRON AND COPPER.
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 [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16813577; DOI=10.1111/j.1365-313x.2006.02803.x;
RA Durrett T.P., Connolly E.L., Rogers E.E.;
RT "Arabidopsis cpFtsY mutants exhibit pleiotropic defects including an
RT inability to increase iron deficiency-inducible root Fe(III) chelate
RT reductase activity.";
RL Plant J. 47:467-479(2006).
RN [10]
RP TOPOLOGY.
RX PubMed=16845482; DOI=10.1007/s11103-006-9015-0;
RA Schagerloef U., Wilson G., Hebert H., Al-Karadaghi S., Haegerhaell C.;
RT "Transmembrane topology of FRO2, a ferric chelate reductase from
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 62:215-221(2006).
RN [11]
RP INDUCTION BY CYTOKININ.
RX PubMed=18397377; DOI=10.1111/j.1365-313x.2008.03502.x;
RA Seguela M., Briat J.-F., Vert G., Curie C.;
RT "Cytokinins negatively regulate the root iron uptake machinery in
RT Arabidopsis through a growth-dependent pathway.";
RL Plant J. 55:289-300(2008).
RN [12]
RP FUNCTION, AND INDUCTION BY GLYCINE BETAINE.
RX PubMed=18513375; DOI=10.1111/j.1399-3054.2008.01141.x;
RA Einset J., Winge P., Bones A.M., Connolly E.L.;
RT "The FRO2 ferric reductase is required for glycine betaine's effect on
RT chilling tolerance in Arabidopsis roots.";
RL Physiol. Plantarum 134:334-341(2008).
RN [13]
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 [14]
RP INDUCTION BY CARBON MONOXIDE.
RX PubMed=20055961; DOI=10.1111/j.1467-7652.2009.00469.x;
RA Kong W.W., Zhang L.P., Guo K., Liu Z.P., Yang Z.M.;
RT "Carbon monoxide improves adaptation of Arabidopsis to iron deficiency.";
RL Plant Biotechnol. J. 8:88-99(2010).
CC -!- FUNCTION: Flavocytochrome that transfers electrons across the plasma
CC membrane to reduce ferric iron chelates to form soluble ferrous iron in
CC the rhizosphere. May be involved in the delivery of iron to developing
CC pollen grains. Acts also as a copper-chelate reductase. Involved in
CC glycine betaine-mediated chilling tolerance and reactive oxygen species
CC accumulation. {ECO:0000269|PubMed:10067892,
CC ECO:0000269|PubMed:14526117, ECO:0000269|PubMed:16006655,
CC ECO:0000269|PubMed:18513375}.
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: Cell membrane {ECO:0000269|PubMed:16813577};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16813577}.
CC -!- TISSUE SPECIFICITY: Expressed in the epidermal cells of the roots. High
CC expression in lateral roots and root hairs. Detected in leaves, stems,
CC siliques and in flowers in anthers and styles.
CC {ECO:0000269|PubMed:10067892, ECO:0000269|PubMed:14526117,
CC ECO:0000269|PubMed:16006655, ECO:0000269|PubMed:16362328,
CC ECO:0000269|PubMed:16813577}.
CC -!- INDUCTION: Circadian-regulation. Up-regulated in roots by iron
CC deficiency, carbon monoxide and by treatment with glycine betaine.
CC Down-regulated by zinc, cadmium and cytokinin. Not regulated by copper.
CC {ECO:0000269|PubMed:10067892, ECO:0000269|PubMed:12805609,
CC ECO:0000269|PubMed:14526117, ECO:0000269|PubMed:16362328,
CC ECO:0000269|PubMed:18397377, ECO:0000269|PubMed:18513375,
CC ECO:0000269|PubMed:20055961}.
CC -!- DOMAIN: The C-terminus is probably located inside the membrane.
CC {ECO:0000269|PubMed:16845482}.
CC -!- DISRUPTION PHENOTYPE: Impaired growth on media with no added iron. No
CC response to glycine betaine in chilling assays.
CC {ECO:0000269|PubMed:10067892}.
CC -!- MISCELLANEOUS: Post-transcriptionally regulated by iron. Coordinately
CC regulated with the iron transport protein IRT1.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF81316.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y09581; CAA70770.1; -; Genomic_DNA.
DR EMBL; AY302057; AAP51420.1; -; mRNA.
DR EMBL; AC061957; AAF81316.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27308.1; -; Genomic_DNA.
DR PIR; E86146; E86146.
DR RefSeq; NP_171664.1; NM_100040.3.
DR AlphaFoldDB; P92949; -.
DR SMR; P92949; -.
DR BioGRID; 24646; 1.
DR IntAct; P92949; 1.
DR STRING; 3702.AT1G01580.1; -.
DR TCDB; 5.B.1.4.4; the phagocyte (gp91(phox)) nadph oxidase family.
DR iPTMnet; P92949; -.
DR PaxDb; P92949; -.
DR PRIDE; P92949; -.
DR ProteomicsDB; 230043; -.
DR EnsemblPlants; AT1G01580.1; AT1G01580.1; AT1G01580.
DR GeneID; 839411; -.
DR Gramene; AT1G01580.1; AT1G01580.1; AT1G01580.
DR KEGG; ath:AT1G01580; -.
DR Araport; AT1G01580; -.
DR TAIR; locus:2025351; AT1G01580.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_014777_1_0_1; -.
DR InParanoid; P92949; -.
DR PhylomeDB; P92949; -.
DR BioCyc; ARA:AT1G01580-MON; -.
DR BRENDA; 1.16.1.10; 399.
DR PRO; PR:P92949; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P92949; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0055072; P:iron ion homeostasis; IMP:TAIR.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IMP:TAIR.
DR Gene3D; 3.40.50.80; -; 2.
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 SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Electron transport; FAD; Flavoprotein; Heme; Ion transport;
KW Iron; Membrane; Metal-binding; NAD; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..725
FT /note="Ferric reduction oxidase 2"
FT /id="PRO_0000413200"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16845482"
FT TRANSMEM 29..48
FT /note="Helical"
FT TOPO_DOM 49..74
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16845482"
FT TRANSMEM 75..93
FT /note="Helical"
FT TOPO_DOM 94..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16845482"
FT TRANSMEM 126..149
FT /note="Helical"
FT TOPO_DOM 150..217
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16845482"
FT TRANSMEM 218..241
FT /note="Helical"
FT TOPO_DOM 242..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16845482"
FT TRANSMEM 292..316
FT /note="Helical"
FT TOPO_DOM 317..338
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16845482"
FT TRANSMEM 339..359
FT /note="Helical"
FT TOPO_DOM 360..554
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16845482"
FT TRANSMEM 555..577
FT /note="Helical"
FT TOPO_DOM 578..597
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16845482"
FT TRANSMEM 598..619
FT /note="Helical"
FT TOPO_DOM 620..725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16845482"
FT DOMAIN 183..303
FT /note="Ferric oxidoreductase"
FT DOMAIN 332..437
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 219
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:0000305"
FT BINDING 233
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:0000305"
FT BINDING 293
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:0000305"
FT BINDING 306
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:0000305"
FT BINDING 381..384
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 429..432
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MUTAGEN 384
FT /note="T->M: In frd1-3; loss of induced ferric-chelate
FT reductase activity."
FT /evidence="ECO:0000269|PubMed:10067892"
SQ SEQUENCE 725 AA; 81501 MW; 9589ABA88DD79512 CRC64;
MEIEKSNNGG SNPSAGEEFK DMIKGVTKFL MMVIFLGTIM LWIMMPTLTY RTKWLPHLRI
KFGTSTYFGA TGTTLFMYMF PMMVVACLGC VYLHFKNRKS PHHIDRETKG GVWSKLRKPM
LVKGPLGIVS VTEITFLAMF VALLLWCFIT YLRNSFATIT PKSAAAHDES LWQAKLESAA
LRLGLIGNIC LAFLFLPVAR GSSLLPAMGL TSESSIKYHI WLGHMVMALF TVHGLCYIIY
WASMHEISQM IMWDTKGVSN LAGEIALAAG LVMWATTYPK IRRRFFEVFF YTHYLYIVFM
LFFVLHVGIS FSFIALPGFY IFLVDRFLRF LQSRENVRLL AARILPSDTM ELTFSKNSKL
VYSPTSIMFV NIPSISKLQW HPFTITSSSK LEPEKLSIVI KKEGKWSTKL HQRLSSSDQI
DRLAVSVEGP YGPASADFLR HEALVMVCGG SGITPFISVI RDLIATSQKE TCKIPKITLI
CAFKKSSEIS MLDLVLPLSG LETELSSDIN IKIEAFITRD NDAGDEAKAG KIKTLWFKPS
LSDQSISSIL GPNSWLWLGA ILASSFLIFM IIIGIITRYY IYPIDHNTNK IYSLTSKTII
YILVISVSIM ATCSAAMLWN KKKYGKVESK QVQNVDRPSP TSSPTSSWGY NSLREIESTP
QESLVQRTNL HFGERPNLKK LLLDVEGSSV GVLVCGPKKM RQKVAEICSS GLAENLHFES
ISFSW
