FRO3_ARATH
ID FRO3_ARATH Reviewed; 717 AA.
AC F4I4K7; F4I4K6; O23122;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Ferric reduction oxidase 3, mitochondrial;
DE Short=AtFRO3;
DE EC=1.16.1.7;
DE AltName: Full=Ferric-chelate reductase 3;
DE Flags: Precursor;
GN Name=FRO3; Synonyms=FROHC; OrderedLocusNames=At1g23020; ORFNames=F19G10.4;
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, TISSUE SPECIFICITY, AND INDUCTION BY
RP IRON.
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=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 [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 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 [5]
RP TISSUE SPECIFICITY, AND INDUCTION BY IRON.
RX PubMed=18436742; DOI=10.1126/science.1153795;
RA Dinneny J.R., Long T.A., Wang J.Y., Jung J.W., Mace D., Pointer S.,
RA Barron C., Brady S.M., Schiefelbein J., Benfey P.N.;
RT "Cell identity mediates the response of Arabidopsis roots to abiotic
RT stress.";
RL Science 320:942-945(2008).
RN [6]
RP GENE FAMILY, NOMENCLATURE, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Ferric chelate reductase involved in iron reduction in roots.
CC May participate in the transport of electrons to a Fe(3+) ion via FAD
CC and heme intermediates. {ECO:0000269|PubMed:16006655}.
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: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=F4I4K7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4I4K7-2; Sequence=VSP_041873;
CC Name=3;
CC IsoId=F4I4K7-3; Sequence=VSP_041872, VSP_041873;
CC -!- TISSUE SPECIFICITY: Expressed in root steele. Detected in shoots,
CC leaves, stems, siliques, flowers and cotyledons.
CC {ECO:0000269|PubMed:16006655, ECO:0000269|PubMed:16362328,
CC ECO:0000269|PubMed:18436742}.
CC -!- INDUCTION: Up-regulated in roots and shoots by iron deficiency and
CC copper deficiency. {ECO:0000269|PubMed:16006655,
CC ECO:0000269|PubMed:16362328, ECO:0000269|PubMed:18436742}.
CC -!- MISCELLANEOUS: It is not clear whether or not FRO3 functions in iron
CC import to mitochondria or is involved in iron efflux to the cytosol.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
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DR EMBL; AF000657; AAB72168.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30322.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30323.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59873.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59874.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59875.1; -; Genomic_DNA.
DR PIR; C86364; C86364.
DR RefSeq; NP_001185067.1; NM_001198138.1. [F4I4K7-1]
DR RefSeq; NP_001319065.1; NM_001332575.1. [F4I4K7-2]
DR RefSeq; NP_001322197.1; NM_001332576.1. [F4I4K7-3]
DR RefSeq; NP_001322198.1; NM_001332577.1. [F4I4K7-3]
DR RefSeq; NP_173715.2; NM_102150.4. [F4I4K7-2]
DR AlphaFoldDB; F4I4K7; -.
DR SMR; F4I4K7; -.
DR STRING; 3702.AT1G23020.2; -.
DR PaxDb; F4I4K7; -.
DR PRIDE; F4I4K7; -.
DR ProteomicsDB; 248553; -. [F4I4K7-1]
DR EnsemblPlants; AT1G23020.1; AT1G23020.1; AT1G23020. [F4I4K7-2]
DR EnsemblPlants; AT1G23020.2; AT1G23020.2; AT1G23020. [F4I4K7-1]
DR EnsemblPlants; AT1G23020.3; AT1G23020.3; AT1G23020. [F4I4K7-3]
DR EnsemblPlants; AT1G23020.4; AT1G23020.4; AT1G23020. [F4I4K7-3]
DR EnsemblPlants; AT1G23020.5; AT1G23020.5; AT1G23020. [F4I4K7-2]
DR GeneID; 838910; -.
DR Gramene; AT1G23020.1; AT1G23020.1; AT1G23020. [F4I4K7-2]
DR Gramene; AT1G23020.2; AT1G23020.2; AT1G23020. [F4I4K7-1]
DR Gramene; AT1G23020.3; AT1G23020.3; AT1G23020. [F4I4K7-3]
DR Gramene; AT1G23020.4; AT1G23020.4; AT1G23020. [F4I4K7-3]
DR Gramene; AT1G23020.5; AT1G23020.5; AT1G23020. [F4I4K7-2]
DR KEGG; ath:AT1G23020; -.
DR Araport; AT1G23020; -.
DR TAIR; locus:2017789; AT1G23020.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; F4I4K7; -.
DR OMA; GMFTHID; -.
DR OrthoDB; 190356at2759; -.
DR BRENDA; 1.16.1.10; 399.
DR PRO; PR:F4I4K7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I4K7; baseline and differential.
DR Genevisible; F4I4K7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
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; 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 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 PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Electron transport; FAD; Flavoprotein; Heme;
KW Ion transport; Iron; Membrane; Metal-binding; Mitochondrion; NAD;
KW Oxidoreductase; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..717
FT /note="Ferric reduction oxidase 3, mitochondrial"
FT /id="PRO_0000413201"
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 140..163
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 232..255
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 306..330
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 564..586
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 606..627
FT /note="Helical"
FT /evidence="ECO:0000250"
FT DOMAIN 198..317
FT /note="Ferric oxidoreductase"
FT DOMAIN 346..451
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
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 247
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 307
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 320
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 395..398
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 443..446
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..27
FT /note="MAARGRLVVARGNRSFSSIIRKYSLKR -> MVLG (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_041872"
FT VAR_SEQ 117
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_041873"
SQ SEQUENCE 717 AA; 80934 MW; 9213B93C8E99F6A1 CRC64;
MAARGRLVVA RGNRSFSSII RKYSLKRETN KKVIKNVIKL LTMVILMGTV VIWIMMPTST
YKKIWLKSMR AKLGKSIYFG KPGVNLLVYM FPMILLASLG SIYLHLKKQT RVNQFNSRMD
RKKIDKFGAL KRPMLVKAGL GIVTVTEVMF LMMFMALLLW SLANYFYHTF VTITPQSLPT
DGDNLWQARL DSIAVRLGLT GNICLGFLFY PVARGSSLLA AVGLTSESST KYHIWLGNLV
MTLFTSHGLC YCIYWISTNQ VSQMLEWDRT GISHLAGEIA LVAGLLMWAT TFPAIRRRFF
EVFFYTHYLY MVFMLFFVFH VGISYALISF PGFYIFMVDR FLRFLQSRNN VKLVSARVLP
CETVELNFSK NPMLMYSPTS ILFVNIPSIS KLQWHPFTIT SSSKLEPKKL SVMIKSQGKW
SSKLHHMLAS SNQIDHLAVS VEGPYGPAST DYLRHDSLVM VSGGSGITPF ISIIRDLLYV
SSTNAYKTPK ITLICAFKNS SDLSMLNLIL PNSTEISSFI DIQIKAFVTR EKVSTCNMNI
IKTLSFKPYV SDQPISPILG PNSWLWLATI LSSSFMIFII IIAIISRYHI YPIDQSSKEY
TSAYTSLIYL LAISISVVAT STVAMLCNKK SYFKGLYQNV DALSPLMIES SPDQLLPEFT
NIHYGERPNL NKLLVGLKGS SVGVLVCGPR KMREEVAKIC SFGSAANLQF ESISFNW
