FRI1_ARATH
ID FRI1_ARATH Reviewed; 255 AA.
AC Q39101; Q8LG19;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Ferritin-1, chloroplastic {ECO:0000303|PubMed:8761454};
DE Short=AtFer1 {ECO:0000303|PubMed:8761454};
DE EC=1.16.3.1 {ECO:0000305};
DE Flags: Precursor;
GN Name=FER1 {ECO:0000303|PubMed:8761454};
GN OrderedLocusNames=At5g01600 {ECO:0000312|Araport:AT5G01600};
GN ORFNames=F7A7.120 {ECO:0000312|EMBL:CAB82276.1};
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].
RX PubMed=8761454; DOI=10.1042/bj3180067;
RA Gaymard F., Boucherez J., Briat J.-F.;
RT "Characterization of a ferritin mRNA from Arabidopsis thaliana accumulated
RT in response to iron through an oxidative pathway independent of abscisic
RT acid.";
RL Biochem. J. 318:67-73(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Petit J.-M., van Wuytswinkel O., Briat J.-F., Lobreaux S.;
RT "Characterization of an iron-dependent regulatory sequence (IDRS) involved
RT in AtFer1 and ZmFer1 plant ferritin gene transcriptional control by iron.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION.
RX PubMed=11672431; DOI=10.1042/0264-6021:3590575;
RA Petit J.-M., Briat J.-F., Lobreaux S.;
RT "Structure and differential expression of the four members of the
RT Arabidopsis thaliana ferritin gene family.";
RL Biochem. J. 359:575-582(2001).
RN [8]
RP INDUCTION BY PHR1.
RX PubMed=23788639; DOI=10.1074/jbc.m113.482281;
RA Bournier M., Tissot N., Mari S., Boucherez J., Lacombe E., Briat J.F.,
RA Gaymard F.;
RT "Arabidopsis ferritin 1 (AtFer1) gene regulation by the phosphate
RT starvation response 1 (AtPHR1) transcription factor reveals a direct
RT molecular link between iron and phosphate homeostasis.";
RL J. Biol. Chem. 288:22670-22680(2013).
CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form.
CC Important for iron homeostasis. Has ferroxidase activity. Iron is taken
CC up in the ferrous form and deposited as ferric hydroxides after
CC oxidation (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: L
CC (light) chain and H (heavy) chain. The major chain can be light or
CC heavy, depending on the species and tissue type. The functional
CC molecule forms a roughly spherical shell with a diameter of 12 nm and
CC contains a central cavity into which the insoluble mineral iron core is
CC deposited (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q39101; Q9SX22: At1g68590; NbExp=3; IntAct=EBI-25513208, EBI-4424705;
CC Q39101; Q39101: FER1; NbExp=5; IntAct=EBI-25513208, EBI-25513208;
CC Q39101; Q9LYN2: FER3; NbExp=3; IntAct=EBI-25513208, EBI-21138118;
CC Q39101; F4JL11: IMPA2; NbExp=3; IntAct=EBI-25513208, EBI-1253508;
CC Q39101; O04294: IMPA3; NbExp=3; IntAct=EBI-25513208, EBI-1644689;
CC Q39101; Q9FWY7: IMPA6; NbExp=3; IntAct=EBI-25513208, EBI-4431755;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- INDUCTION: Up-regulated by iron overload treatment, and by H(2)O(2)
CC (PubMed:11672431). Up-regulated by the phosphate starvation response
CC transcription factor PHR1 (PubMed:23788639).
CC {ECO:0000269|PubMed:11672431, ECO:0000269|PubMed:23788639}.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; X94248; CAA63932.1; -; mRNA.
DR EMBL; AF229850; AAF73918.1; -; Genomic_DNA.
DR EMBL; AL161946; CAB82276.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90364.1; -; Genomic_DNA.
DR EMBL; AF326869; AAG41451.1; -; mRNA.
DR EMBL; AF339691; AAK00373.1; -; mRNA.
DR EMBL; AF412065; AAL06518.1; -; mRNA.
DR EMBL; AY084509; AAM61077.1; -; mRNA.
DR PIR; S71880; S71880.
DR RefSeq; NP_195780.1; NM_120238.4.
DR AlphaFoldDB; Q39101; -.
DR SMR; Q39101; -.
DR BioGRID; 16996; 15.
DR IntAct; Q39101; 5.
DR STRING; 3702.AT5G01600.1; -.
DR iPTMnet; Q39101; -.
DR PaxDb; Q39101; -.
DR PRIDE; Q39101; -.
DR ProteomicsDB; 230546; -.
DR EnsemblPlants; AT5G01600.1; AT5G01600.1; AT5G01600.
DR GeneID; 831720; -.
DR Gramene; AT5G01600.1; AT5G01600.1; AT5G01600.
DR KEGG; ath:AT5G01600; -.
DR Araport; AT5G01600; -.
DR TAIR; locus:2149755; AT5G01600.
DR eggNOG; KOG2332; Eukaryota.
DR HOGENOM; CLU_065681_0_0_1; -.
DR InParanoid; Q39101; -.
DR OMA; EQRNDAH; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; Q39101; -.
DR BioCyc; ARA:AT5G01600-MON; -.
DR PRO; PR:Q39101; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39101; baseline and differential.
DR Genevisible; Q39101; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; TAS:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0009908; P:flower development; IGI:TAIR.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; IGI:TAIR.
DR GO; GO:0006826; P:iron ion transport; IGI:TAIR.
DR GO; GO:0048366; P:leaf development; IGI:TAIR.
DR GO; GO:0015979; P:photosynthesis; IGI:TAIR.
DR GO; GO:0009617; P:response to bacterium; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR GO; GO:0010039; P:response to iron ion; IEP:TAIR.
DR GO; GO:0000302; P:response to reactive oxygen species; IGI:TAIR.
DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR001519; Ferritin.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR014034; Ferritin_CS.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR PANTHER; PTHR11431; PTHR11431; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00204; FERRITIN_2; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Iron; Iron storage; Metal-binding; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 49..255
FT /note="Ferritin-1, chloroplastic"
FT /id="PRO_0000008854"
FT DOMAIN 88..241
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT REGION 49..87
FT /note="Extension peptide (EP)"
FT BINDING 105
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 143
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT CONFLICT 42
FT /note="G -> S (in Ref. 6; AAM61077)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="F -> L (in Ref. 6; AAM61077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28178 MW; C40E89CA4548FCB0 CRC64;
MASNALSSFT AANPALSPKP LLPHGSASPS VSLGFSRKVG GGRAVVVAAA TVDTNNMPMT
GVVFQPFEEV KKADLAIPIT SHASLARQRF ADASEAVINE QINVEYNVSY VYHSMYAYFD
RDNVAMKGLA KFFKESSEEE RGHAEKFMEY QNQRGGRVKL HPIVSPISEF EHAEKGDALY
AMELALSLEK LTNEKLLNVH KVASENNDPQ LADFVESEFL GEQIEAIKKI SDYITQLRMI
GKGHGVWHFD QMLLN
