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Ferric reduction oxidase 8, mitochondrial (AtFRO8) (EC 1.16.1.7) (Ferric-chelate reductase 8)

 FRO8_ARATH              Reviewed;         728 AA.
Q8VY13; Q9FGS9;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
07-NOV-2018, entry version 102.
RecName: Full=Ferric reduction oxidase 8, mitochondrial;
Short=AtFRO8;
EC=1.16.1.7;
AltName: Full=Ferric-chelate reductase 8;
Flags: Precursor;
Name=FRO8; OrderedLocusNames=At5g50160; ORFNames=K6A12.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INDUCTION BY IRON.
PubMed=16006655; DOI=10.1093/pcp/pci163;
Wu H., Li L., Du J., Yuan Y., Cheng X., Ling H.Q.;
"Molecular and biochemical characterization of the Fe(III) chelate
reductase gene family in Arabidopsis thaliana.";
Plant Cell Physiol. 46:1505-1514(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10718197; DOI=10.1093/dnares/7.1.31;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
features of the regions of 3,076,755 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:31-63(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=14671022; DOI=10.1105/tpc.016055;
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome
highlights signaling and regulatory components, provides assessment of
targeting prediction programs, and indicates plant-specific
mitochondrial proteins.";
Plant Cell 16:241-256(2004).
[6]
TISSUE SPECIFICITY, AND INDUCTION BY IRON AND COPPER.
PubMed=16362328; DOI=10.1007/s00425-005-0165-0;
Mukherjee I., Campbell N.H., Ash J.S., Connolly E.L.;
"Expression profiling of the Arabidopsis ferric chelate reductase
(FRO) gene family reveals differential regulation by iron and
copper.";
Planta 223:1178-1190(2006).
[7]
GENE FAMILY, NOMENCLATURE, AND SUBCELLULAR LOCATION.
DOI=10.1016/j.plantsci.2009.02.011;
Jeong J., Connolly E.L.;
"Iron uptake mechanisms in plants: Functions of the FRO family of
ferric reductases.";
Plant Sci. 176:709-714(2009).
-!- FUNCTION: Ferric chelate reductase probably involved in iron
reduction in leaf veins for transport. May participate in the
transport of electrons to a Fe(3+) ion via FAD and heme
intermediates. {ECO:0000269|PubMed:16006655}.
-!- CATALYTIC ACTIVITY: 2 Fe(II)-siderophore + NAD(+) + H(+) = 2
Fe(III)-siderophore + NADH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
-!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-
pass membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in shoots. Detected in roots,
pedicels, flowers, siliques and leaf veins.
{ECO:0000269|PubMed:16006655, ECO:0000269|PubMed:16362328}.
-!- INDUCTION: Down-regulated in shoots by copper deficiency. Not
regulated by iron availability. {ECO:0000269|PubMed:16006655,
ECO:0000269|PubMed:16362328}.
-!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB09387.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB024031; BAB09387.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED95905.1; -; Genomic_DNA.
EMBL; AY074287; AAL66984.1; -; mRNA.
EMBL; BT003007; AAO22815.1; -; mRNA.
RefSeq; NP_199827.2; NM_124395.5.
UniGene; At.43265; -.
ProteinModelPortal; Q8VY13; -.
SMR; Q8VY13; -.
STRING; 3702.AT5G50160.1; -.
TCDB; 5.B.1.4.1; the phagocyte (gp91(phox)) nadph oxidase family.
PaxDb; Q8VY13; -.
EnsemblPlants; AT5G50160.1; AT5G50160.1; AT5G50160.
GeneID; 835081; -.
Gramene; AT5G50160.1; AT5G50160.1; AT5G50160.
KEGG; ath:AT5G50160; -.
Araport; AT5G50160; -.
TAIR; locus:2157697; AT5G50160.
eggNOG; KOG0039; Eukaryota.
eggNOG; ENOG410XNZY; LUCA.
HOGENOM; HOG000006154; -.
InParanoid; Q8VY13; -.
KO; K00521; -.
OMA; LKPTQLW; -.
OrthoDB; EOG093603NP; -.
PhylomeDB; Q8VY13; -.
BioCyc; ARA:AT5G50160-MONOMER; -.
Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:Q8VY13; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q8VY13; baseline and differential.
Genevisible; Q8VY13; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0000293; F:ferric-chelate reductase activity; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
Gene3D; 3.40.50.80; -; 2.
InterPro; IPR000778; Cyt_b245_heavy_chain.
InterPro; IPR013112; FAD-bd_8.
InterPro; IPR017927; FAD-bd_FR_type.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR013121; Fe_red_NAD-bd_6.
InterPro; IPR039261; FNR_nucleotide-bd.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF08022; FAD_binding_8; 1.
Pfam; PF01794; Ferric_reduct; 1.
Pfam; PF08030; NAD_binding_6; 1.
PRINTS; PR00466; GP91PHOX.
SUPFAM; SSF52343; SSF52343; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
Complete proteome; Electron transport; FAD; Flavoprotein; Heme;
Ion transport; Iron; Membrane; Metal-binding; Mitochondrion; NAD;
Oxidoreductase; Reference proteome; Transit peptide; Transmembrane;
Transmembrane helix; Transport.
TRANSIT 1 24 Mitochondrion. {ECO:0000255}.
CHAIN 25 728 Ferric reduction oxidase 8,
mitochondrial.
/FTId=PRO_0000413206.
TRANSMEM 56 74 Helical. {ECO:0000250}.
TRANSMEM 104 127 Helical. {ECO:0000250}.
TRANSMEM 194 217 Helical. {ECO:0000250}.
TRANSMEM 269 293 Helical. {ECO:0000250}.
TRANSMEM 316 336 Helical. {ECO:0000250}.
TRANSMEM 537 559 Helical. {ECO:0000250}.
TRANSMEM 595 616 Helical. {ECO:0000250}.
DOMAIN 159 281 Ferric oxidoreductase.
DOMAIN 300 418 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 358 361 FAD. {ECO:0000255}.
NP_BIND 410 413 NAD. {ECO:0000255}.
COMPBIAS 364 367 Poly-Ser.
METAL 195 195 Iron (heme axial ligand). {ECO:0000250}.
METAL 209 209 Iron (heme axial ligand). {ECO:0000250}.
METAL 270 270 Iron (heme axial ligand). {ECO:0000250}.
METAL 283 283 Iron (heme axial ligand). {ECO:0000250}.
SEQUENCE 728 AA; 83230 MW; A1E5BFD18FB1D2B0 CRC64;
MAKVLTLLVL RLLMNLLLIG WISLWIIKPT TIWIQSWRQA EDTARHTFFG YYGLNFAVFS
FPPIALSIVG LIYLSLLPQH HHPTRGGRGA AITVSRPAII NSFIGIVSCF EILALLLFLL
FLAWNFYARV SNDFKKLMPV KTMNLNLWQL KYYRVATRFG LLAEACLSLL LFPVLRGLSM
FRLLNIEFAA SVKYHVWFGT GLIFFSLVHG GSTLFIWTIT HHIEEEIWKW QRTGRVYVAG
LISLVTGLLM WITSLPQIRR KNFEVFYYTH HLYIVFLVAF LFHAGDRHFY WVLPGMFLFG
LDKILRIVQS RSESCILSAN LFSCKAIELV LPKDPMLNYA PSSFIFLNIP LVSRFQWHPF
SIISSSSVDK HSLSIMMKCE GDWTNSVYNK IEEAANCENK INNIIVRVEG PYGPASVDFL
RYDNLFLVAG GIGITPFLSI LKELASKNRL KSPKRVQLVF AVRTFQDLNM LLPIASIIFN
PIYNLNLKLK VFVTQEKKPS NGTTTLQEFL AQSQVQSIHL GTDEDYSRFP IRGPESFRWL
ATLVLITVLT FLGFLIGLSH FFIPSEHKNH SGVMKLAASG AMKTAKEKVP SWVPDLIIIV
SYVIAISVGG FAATILQRRR KHKEAPRMSK EVVIKPEERN FTELKPIPIT EEHEIHIGER
PKLEEIMSEF EKNLRGWSSV GVLVCGPESV KEAVASMCRQ WPQCFGVEDL RRSRMKMNLN
FHSLNFNL


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