FRI4_ARATH
ID FRI4_ARATH Reviewed; 259 AA.
AC Q9S756; Q8WHW5;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ferritin-4, chloroplastic;
DE EC=1.16.3.1;
DE Flags: Precursor;
GN Name=FER4; OrderedLocusNames=At2g40300; ORFNames=T07M07.18, T3G21.7;
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].
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 [GENOMIC DNA].
RX PubMed=10207155;
RA Wang M.L., Belmonte S., Kim U., Dolan M., Morris J.W., Goodman H.M.;
RT "A cluster of ABA-regulated genes on Arabidopsis thaliana BAC T07M07.";
RL Genome Res. 9:325-333(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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).
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 -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; AJ312191; CAC85400.1; -; mRNA.
DR EMBL; AF085279; AAD25945.1; -; Genomic_DNA.
DR EMBL; AC007020; AAD25665.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09810.1; -; Genomic_DNA.
DR EMBL; AY062795; AAL32873.1; -; mRNA.
DR EMBL; AY081615; AAM10177.1; -; mRNA.
DR PIR; G84827; G84827.
DR RefSeq; NP_181559.1; NM_129588.5.
DR AlphaFoldDB; Q9S756; -.
DR SMR; Q9S756; -.
DR BioGRID; 3960; 1.
DR STRING; 3702.AT2G40300.1; -.
DR PaxDb; Q9S756; -.
DR PRIDE; Q9S756; -.
DR ProteomicsDB; 230529; -.
DR EnsemblPlants; AT2G40300.1; AT2G40300.1; AT2G40300.
DR GeneID; 818622; -.
DR Gramene; AT2G40300.1; AT2G40300.1; AT2G40300.
DR KEGG; ath:AT2G40300; -.
DR Araport; AT2G40300; -.
DR TAIR; locus:2063104; AT2G40300.
DR eggNOG; KOG2332; Eukaryota.
DR HOGENOM; CLU_065681_0_0_1; -.
DR InParanoid; Q9S756; -.
DR OMA; YLSMGYF; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; Q9S756; -.
DR BioCyc; ARA:AT2G40300-MON; -.
DR PRO; PR:Q9S756; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9S756; baseline and differential.
DR Genevisible; Q9S756; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA: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: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:0010039; P:response to iron ion; IEP:TAIR.
DR GO; GO:0000302; P:response to reactive oxygen species; IGI: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; PS00540; FERRITIN_1; 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..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..259
FT /note="Ferritin-4, chloroplastic"
FT /id="PRO_0000008857"
FT DOMAIN 91..244
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT REGION 58..90
FT /note="Extension peptide (EP)"
FT BINDING 108
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
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 143
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 146
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ SEQUENCE 259 AA; 29029 MW; CFEC3BA233BAAAA3 CRC64;
MLLKTVSSSS SSALSLVNFH GVKKDVSPLL PSISSNLRVS SGKSGNLTFS FRASKSSTTD
ALSGVVFEPF KEVKKELDLV PTSSHLSLAR QKYSDECEAA INEQINVEYN VSYVYHAMYA
YFDRDNIALK GLAKFFKESS LEEREHAEKL MEYQNKRGGR VKLQSIVMPL SEFEHVDKGD
ALYGMELALS LEKLVNEKLL NLHSVASKNN DVHLADFIES EFLTEQVEAI KLISEYVAQL
RRVGKGHGTW HFNQMLLEG
