Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ferric reduction oxidase 2 (AtFRO2) (EC 1.16.1.7) (Ferric-chelate reductase 2) (Protein FERRIC CHELATE REDUCTASE DEFECTIVE 1)

 FRO2_ARATH              Reviewed;         725 AA.
P92949; Q9LMM3;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 2.
23-MAY-2018, entry version 123.
RecName: Full=Ferric reduction oxidase 2;
Short=AtFRO2;
EC=1.16.1.7;
AltName: Full=Ferric-chelate reductase 2;
AltName: Full=Protein FERRIC CHELATE REDUCTASE DEFECTIVE 1;
Name=FRO2; Synonyms=FRD1; OrderedLocusNames=At1g01580;
ORFNames=F22L4.12;
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 [GENOMIC DNA / MRNA], FUNCTION, MUTAGENESIS OF
THR-384, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY
IRON.
STRAIN=cv. Landsberg erecta;
PubMed=10067892; DOI=10.1038/17800;
Robinson N.J., Procter C.M., Connolly E.L., Guerinot M.L.;
"A ferric-chelate reductase for iron uptake from soils.";
Nature 397:694-697(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Root;
Yang J.H., Liu Y.J., Yang E.Q., Liu S.W., Liu Y.D., Li J.K., Wu C.X.;
"Molecular Cloning of the FRO2 Gene from Arabidopsis roots.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[5]
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).
[6]
INDUCTION.
PubMed=12805609; DOI=10.1104/pp.102.016089;
Vert G.A., Briat J.F., Curie C.;
"Dual regulation of the Arabidopsis high-affinity root iron uptake
system by local and long-distance signals.";
Plant Physiol. 132:796-804(2003).
[7]
FUNCTION, INDUCTION BY IRON; CADMIUM AND ZINC, AND TISSUE SPECIFICITY.
PubMed=14526117; DOI=10.1104/pp.103.025122;
Connolly E.L., Campbell N.H., Grotz N., Prichard C.L., Guerinot M.L.;
"Overexpression of the FRO2 ferric chelate reductase confers tolerance
to growth on low iron and uncovers posttranscriptional control.";
Plant Physiol. 133:1102-1110(2003).
[8]
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).
[9]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16813577; DOI=10.1111/j.1365-313X.2006.02803.x;
Durrett T.P., Connolly E.L., Rogers E.E.;
"Arabidopsis cpFtsY mutants exhibit pleiotropic defects including an
inability to increase iron deficiency-inducible root Fe(III) chelate
reductase activity.";
Plant J. 47:467-479(2006).
[10]
TOPOLOGY.
PubMed=16845482; DOI=10.1007/s11103-006-9015-0;
Schagerloef U., Wilson G., Hebert H., Al-Karadaghi S., Haegerhaell C.;
"Transmembrane topology of FRO2, a ferric chelate reductase from
Arabidopsis thaliana.";
Plant Mol. Biol. 62:215-221(2006).
[11]
INDUCTION BY CYTOKININ.
PubMed=18397377; DOI=10.1111/j.1365-313X.2008.03502.x;
Seguela M., Briat J.-F., Vert G., Curie C.;
"Cytokinins negatively regulate the root iron uptake machinery in
Arabidopsis through a growth-dependent pathway.";
Plant J. 55:289-300(2008).
[12]
FUNCTION, AND INDUCTION BY GLYCINE BETAINE.
PubMed=18513375; DOI=10.1111/j.1399-3054.2008.01141.x;
Einset J., Winge P., Bones A.M., Connolly E.L.;
"The FRO2 ferric reductase is required for glycine betaine's effect on
chilling tolerance in Arabidopsis roots.";
Physiol. Plantarum 134:334-341(2008).
[13]
GENE FAMILY, AND NOMENCLATURE.
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).
[14]
INDUCTION BY CARBON MONOXIDE.
PubMed=20055961; DOI=10.1111/j.1467-7652.2009.00469.x;
Kong W.W., Zhang L.P., Guo K., Liu Z.P., Yang Z.M.;
"Carbon monoxide improves adaptation of Arabidopsis to iron
deficiency.";
Plant Biotechnol. J. 8:88-99(2010).
-!- FUNCTION: Flavocytochrome that transfers electrons across the
plasma membrane to reduce ferric iron chelates to form soluble
ferrous iron in the rhizosphere. May be involved in the delivery
of iron to developing pollen grains. Acts also as a copper-chelate
reductase. Involved in glycine betaine-mediated chilling tolerance
and reactive oxygen species accumulation.
{ECO:0000269|PubMed:10067892, ECO:0000269|PubMed:14526117,
ECO:0000269|PubMed:16006655, ECO:0000269|PubMed:18513375}.
-!- 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: Cell membrane {ECO:0000269|PubMed:16813577};
Multi-pass membrane protein {ECO:0000269|PubMed:16813577}.
-!- TISSUE SPECIFICITY: Expressed in the epidermal cells of the roots.
High expression in lateral roots and root hairs. Detected in
leaves, stems, siliques and in flowers in anthers and styles.
{ECO:0000269|PubMed:10067892, ECO:0000269|PubMed:14526117,
ECO:0000269|PubMed:16006655, ECO:0000269|PubMed:16362328,
ECO:0000269|PubMed:16813577}.
-!- INDUCTION: Circadian-regulation. Up-regulated in roots by iron
deficiency, carbon monoxide and by treatment with glycine betaine.
Down-regulated by zinc, cadmium and cytokinin. Not regulated by
copper. {ECO:0000269|PubMed:10067892, ECO:0000269|PubMed:12805609,
ECO:0000269|PubMed:14526117, ECO:0000269|PubMed:16362328,
ECO:0000269|PubMed:18397377, ECO:0000269|PubMed:18513375,
ECO:0000269|PubMed:20055961}.
-!- DOMAIN: The C-terminus is probably located inside the membrane.
{ECO:0000269|PubMed:16845482}.
-!- DISRUPTION PHENOTYPE: Impaired growth on media with no added iron.
No response to glycine betaine in chilling assays.
{ECO:0000269|PubMed:10067892}.
-!- MISCELLANEOUS: Post-transcriptionally regulated by iron.
Coordinately regulated with the iron transport protein IRT1.
-!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF81316.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y09581; CAA70770.1; -; Genomic_DNA.
EMBL; AY302057; AAP51420.1; -; mRNA.
EMBL; AC061957; AAF81316.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE27308.1; -; Genomic_DNA.
PIR; E86146; E86146.
RefSeq; NP_171664.1; NM_100040.3.
UniGene; At.42640; -.
ProteinModelPortal; P92949; -.
SMR; P92949; -.
BioGrid; 24646; 1.
IntAct; P92949; 1.
STRING; 3702.AT1G01580.1; -.
TCDB; 5.B.1.4.4; the phagocyte (gp91(phox)) nadph oxidase family.
iPTMnet; P92949; -.
PaxDb; P92949; -.
PRIDE; P92949; -.
EnsemblPlants; AT1G01580.1; AT1G01580.1; AT1G01580.
EnsemblPlants; AT1G01580.2; AT1G01580.2; AT1G01580.
GeneID; 839411; -.
Gramene; AT1G01580.1; AT1G01580.1; AT1G01580.
Gramene; AT1G01580.2; AT1G01580.2; AT1G01580.
KEGG; ath:AT1G01580; -.
Araport; AT1G01580; -.
TAIR; locus:2025351; AT1G01580.
eggNOG; KOG0039; Eukaryota.
eggNOG; ENOG410XNZY; LUCA.
HOGENOM; HOG000006154; -.
InParanoid; P92949; -.
KO; K00521; -.
OMA; KIKTLWF; -.
OrthoDB; EOG093603NP; -.
PhylomeDB; P92949; -.
BioCyc; ARA:AT1G01580-MONOMER; -.
Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:P92949; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; P92949; differential.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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.
GO; GO:0015688; P:iron chelate transport; IMP:TAIR.
GO; GO:0055072; P:iron ion homeostasis; IMP:TAIR.
GO; GO:0009617; P:response to bacterium; IEP:TAIR.
InterPro; IPR013112; FAD-bd_8.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR013121; Fe_red_NAD-bd_6.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF08022; FAD_binding_8; 1.
Pfam; PF01794; Ferric_reduct; 1.
Pfam; PF08030; NAD_binding_6; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Electron transport; FAD;
Flavoprotein; Heme; Ion transport; Iron; Membrane; Metal-binding; NAD;
Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 725 Ferric reduction oxidase 2.
/FTId=PRO_0000413200.
TOPO_DOM 1 28 Cytoplasmic.
{ECO:0000269|PubMed:16845482}.
TRANSMEM 29 48 Helical.
TOPO_DOM 49 74 Extracellular.
{ECO:0000269|PubMed:16845482}.
TRANSMEM 75 93 Helical.
TOPO_DOM 94 125 Cytoplasmic.
{ECO:0000269|PubMed:16845482}.
TRANSMEM 126 149 Helical.
TOPO_DOM 150 217 Extracellular.
{ECO:0000269|PubMed:16845482}.
TRANSMEM 218 241 Helical.
TOPO_DOM 242 291 Cytoplasmic.
{ECO:0000269|PubMed:16845482}.
TRANSMEM 292 316 Helical.
TOPO_DOM 317 338 Extracellular.
{ECO:0000269|PubMed:16845482}.
TRANSMEM 339 359 Helical.
TOPO_DOM 360 554 Cytoplasmic.
{ECO:0000269|PubMed:16845482}.
TRANSMEM 555 577 Helical.
TOPO_DOM 578 597 Extracellular.
{ECO:0000269|PubMed:16845482}.
TRANSMEM 598 619 Helical.
TOPO_DOM 620 725 Cytoplasmic.
{ECO:0000269|PubMed:16845482}.
DOMAIN 183 303 Ferric oxidoreductase.
DOMAIN 332 437 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 381 384 FAD. {ECO:0000255}.
NP_BIND 429 432 NAD. {ECO:0000255}.
COMPBIAS 285 330 Phe-rich.
COMPBIAS 568 609 Ile-rich.
METAL 219 219 Iron (heme axial ligand). {ECO:0000305}.
METAL 233 233 Iron (heme axial ligand). {ECO:0000305}.
METAL 293 293 Iron (heme axial ligand). {ECO:0000305}.
METAL 306 306 Iron (heme axial ligand). {ECO:0000305}.
MUTAGEN 384 384 T->M: In frd1-3; loss of induced ferric-
chelate reductase activity.
{ECO:0000269|PubMed:10067892}.
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


Related products :

Catalog number Product name Quantity
FRRS1_HUMAN Human ELISA Kit FOR Ferric-chelate reductase 1 96T
E12435h Human Ferric Chelate Reductase 1 ELISA Kit 96T
FRS3 FRRS1 Gene ferric-chelate reductase 1
FRRS1_MOUSE Mouse ELISA Kit FOR Ferric-chelate reductase 1 96T
FRRS1_BOVIN Bovine ELISA Kit FOR Ferric-chelate reductase 1 96T
CSB-EL009003BO Bovine Ferric-chelate reductase 1(FRRS1) ELISA kit 96T
CSB-EL009003HU Human Ferric-chelate reductase 1(FRRS1) ELISA kit 96T
CSB-EL009003MO Mouse Ferric-chelate reductase 1(FRRS1) ELISA kit 96T
CSB-EL009003BO Bovine Ferric-chelate reductase 1(FRRS1) ELISA kit SpeciesBovine 96T
CSB-EL009003HU Human Ferric-chelate reductase 1(FRRS1) ELISA kit SpeciesHuman 96T
CSB-EL009003MO Mouse Ferric-chelate reductase 1(FRRS1) ELISA kit SpeciesMouse 96T
EIAAB10258 CYBRD1,Cytochrome b reductase 1,DCYTB,Duodenal cytochrome b,Ferric-chelate reductase 3,FRRS3,Homo sapiens,Human
FRRS1_MOUSE ELISA Kit FOR Ferric-chelate reductase 1; organism: Mouse; gene name: FRRS1 96T
CSB-EL009003MO Mouse ferric-chelate reductase 1 (FRRS1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL009003HU Human ferric-chelate reductase 1 (FRRS1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL009003BO Bovine ferric-chelate reductase 1 (FRRS1) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
orb81128 E.coli Ferric Uptake Regulator protein Ferric Uptake Regulator Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 148 amino acids and having a molecular mass of 5
E-03815/110 Ethylene Diamine Tetra Acetic Acid Ferric Sodium Salt (EDTA Ferric Sodium Salt) CAS: 1578-42-6 500 gm
E-03815/110 Ethylene Diamine Tetra Acetic Acid Ferric Sodium Salt (EDTA Ferric Sodium Salt) CAS: 1578-42-6 100 gm
14221-47-7 Ammonium ferric oxalate Ammonium ferric oxala 1g
13268-42-3 Ammonium ferric oxalate Ammonium ferric oxala 1g
25869-00-5 Ammonium Ferric Ferrocyanide Ammonium Ferric Ferr 1g
111687-36-6 Ferric ammoniom 1,3_propylenediamine Ferric ammoniom 1,3_p 1g
F-03982 FERRIC AMMONIUM CITRATE (Brown) (Ammonium Ferric Citrate) CAS: 1185-57-5 500 gm
F-03993 FERRIC AMMONIUM SULPHATE (Ammonium Ferric Sulphate) CAS: 7783-83-7 500 gm


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur