FRI2_ARATH
ID FRI2_ARATH Reviewed; 253 AA.
AC Q9SRL5; Q42288; Q8L9N6; Q8WHW4;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ferritin-2, chloroplastic;
DE EC=1.16.3.1;
DE Flags: Precursor;
GN Name=FER2; OrderedLocusNames=At3g11050; ORFNames=F11B9.26, F9F8.13;
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], AND INDUCTION.
RC STRAIN=cv. Columbia;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-212.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
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 -!- 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- INDUCTION: By abscisic acid (ABA). {ECO:0000269|PubMed:11672431}.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ312192; CAC85498.1; -; mRNA.
DR EMBL; AC009991; AAF01516.1; -; Genomic_DNA.
DR EMBL; AC073395; AAG50984.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74997.1; -; Genomic_DNA.
DR EMBL; AK175807; BAD43570.1; -; mRNA.
DR EMBL; AK175899; BAD43662.1; -; mRNA.
DR EMBL; AK175901; BAD43664.1; -; mRNA.
DR EMBL; AK175910; BAD43673.1; -; mRNA.
DR EMBL; AY088333; AAM65872.1; -; mRNA.
DR EMBL; Z34949; CAA84408.1; -; mRNA.
DR RefSeq; NP_187716.1; NM_111942.4.
DR AlphaFoldDB; Q9SRL5; -.
DR SMR; Q9SRL5; -.
DR BioGRID; 5610; 1.
DR STRING; 3702.AT3G11050.1; -.
DR PaxDb; Q9SRL5; -.
DR PRIDE; Q9SRL5; -.
DR ProteomicsDB; 230610; -.
DR EnsemblPlants; AT3G11050.1; AT3G11050.1; AT3G11050.
DR GeneID; 820276; -.
DR Gramene; AT3G11050.1; AT3G11050.1; AT3G11050.
DR KEGG; ath:AT3G11050; -.
DR Araport; AT3G11050; -.
DR TAIR; locus:2074683; AT3G11050.
DR eggNOG; KOG2332; Eukaryota.
DR HOGENOM; CLU_065681_0_0_1; -.
DR InParanoid; Q9SRL5; -.
DR OMA; FRSQSHE; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; Q9SRL5; -.
DR BioCyc; ARA:AT3G11050-MON; -.
DR PRO; PR:Q9SRL5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRL5; baseline and differential.
DR Genevisible; Q9SRL5; AT.
DR GO; GO:0009507; C:chloroplast; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP: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 2: Evidence at transcript level;
KW Chloroplast; Iron; Iron storage; Metal-binding; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..253
FT /note="Ferritin-2, chloroplastic"
FT /id="PRO_0000008855"
FT DOMAIN 83..236
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT REGION 46..82
FT /note="Extension peptide (EP)"
FT BINDING 100
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 138
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT CONFLICT 3
FT /note="H -> L (in Ref. 5; AAM65872)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="Y -> S (in Ref. 5; AAM65872)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="L -> R (in Ref. 5; AAM65872)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="R -> K (in Ref. 5; AAM65872)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..70
FT /note="ME -> LD (in Ref. 5; AAM65872)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="S -> A (in Ref. 5; AAM65872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 28378 MW; 92A59DCA3B8EBE3A CRC64;
MLHKASPALS LLSSGYTGGG NLFPPSRNSS NLLFSPSGSR FSVQAAKGTN TKSLTGVVFE
PFEEVKKEME LVPTTPFVSL ARHKFSDDSE SAINDQINVE YNVSYVYHAL YAYFDRDNVG
LKGFAKFFND SSLEERGHAE MFMEYQNKRG GRVKLQSILM PVSEFDHEEK GDALHAMELA
LSLEKLTNEK LLKLQSVGVK NNDVQLVDFV ESEFLGEQVE AIKKISEYVA QLRRIGKGHG
VWHFDQMLLN DEV
