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Ferritin-1, chloroplastic (AtFer1) (EC 1.16.3.1)

 FRI1_ARATH              Reviewed;         255 AA.
Q39101; Q8LG19;
11-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 141.
RecName: Full=Ferritin-1, chloroplastic {ECO:0000303|PubMed:8761454};
Short=AtFer1 {ECO:0000303|PubMed:8761454};
EC=1.16.3.1 {ECO:0000305};
Flags: Precursor;
Name=FER1 {ECO:0000303|PubMed:8761454};
OrderedLocusNames=At5g01600 {ECO:0000312|Araport:AT5G01600};
ORFNames=F7A7.120 {ECO:0000312|EMBL:CAB82276.1};
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].
PubMed=8761454; DOI=10.1042/bj3180067;
Gaymard F., Boucherez J., Briat J.-F.;
"Characterization of a ferritin mRNA from Arabidopsis thaliana
accumulated in response to iron through an oxidative pathway
independent of abscisic acid.";
Biochem. J. 318:67-73(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
Petit J.-M., van Wuytswinkel O., Briat J.-F., Lobreaux S.;
"Characterization of an iron-dependent regulatory sequence (IDRS)
involved in AtFer1 and ZmFer1 plant ferritin gene transcriptional
control by iron.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
INDUCTION.
PubMed=11672431; DOI=10.1042/0264-6021:3590575;
Petit J.-M., Briat J.-F., Lobreaux S.;
"Structure and differential expression of the four members of the
Arabidopsis thaliana ferritin gene family.";
Biochem. J. 359:575-582(2001).
[8]
INDUCTION BY PHR1.
PubMed=23788639; DOI=10.1074/jbc.M113.482281;
Bournier M., Tissot N., Mari S., Boucherez J., Lacombe E., Briat J.F.,
Gaymard F.;
"Arabidopsis ferritin 1 (AtFer1) gene regulation by the phosphate
starvation response 1 (AtPHR1) transcription factor reveals a direct
molecular link between iron and phosphate homeostasis.";
J. Biol. Chem. 288:22670-22680(2013).
-!- FUNCTION: Stores iron in a soluble, non-toxic, readily available
form. Important for iron homeostasis. Has ferroxidase activity.
Iron is taken up in the ferrous form and deposited as ferric
hydroxides after oxidation (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
{ECO:0000305}.
-!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits:
L (light) chain and H (heavy) chain. The major chain can be light
or heavy, depending on the species and tissue type. The functional
molecule forms a roughly spherical shell with a diameter of 12 nm
and contains a central cavity into which the insoluble mineral
iron core is deposited (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast.
-!- INDUCTION: Up-regulated by iron overload treatment, and by
H(2)O(2) (PubMed:11672431). Up-regulated by the phosphate
starvation response transcription factor PHR1 (PubMed:23788639).
{ECO:0000269|PubMed:11672431, ECO:0000269|PubMed:23788639}.
-!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X94248; CAA63932.1; -; mRNA.
EMBL; AF229850; AAF73918.1; -; Genomic_DNA.
EMBL; AL161946; CAB82276.1; -; Genomic_DNA.
EMBL; CP002688; AED90364.1; -; Genomic_DNA.
EMBL; AF326869; AAG41451.1; -; mRNA.
EMBL; AF339691; AAK00373.1; -; mRNA.
EMBL; AF412065; AAL06518.1; -; mRNA.
EMBL; AY084509; AAM61077.1; -; mRNA.
PIR; S71880; S71880.
RefSeq; NP_195780.1; NM_120238.4.
UniGene; At.23533; -.
UniGene; At.73124; -.
UniGene; At.75488; -.
ProteinModelPortal; Q39101; -.
SMR; Q39101; -.
BioGrid; 16996; 8.
STRING; 3702.AT5G01600.1; -.
iPTMnet; Q39101; -.
PaxDb; Q39101; -.
PRIDE; Q39101; -.
EnsemblPlants; AT5G01600.1; AT5G01600.1; AT5G01600.
GeneID; 831720; -.
Gramene; AT5G01600.1; AT5G01600.1; AT5G01600.
KEGG; ath:AT5G01600; -.
Araport; AT5G01600; -.
TAIR; locus:2149755; AT5G01600.
eggNOG; KOG2332; Eukaryota.
eggNOG; COG1528; LUCA.
HOGENOM; HOG000223383; -.
InParanoid; Q39101; -.
KO; K00522; -.
OMA; ECGLRAM; -.
OrthoDB; EOG09360PX4; -.
PhylomeDB; Q39101; -.
BioCyc; ARA:AT5G01600-MONOMER; -.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-917937; Iron uptake and transport.
PRO; PR:Q39101; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q39101; baseline and differential.
Genevisible; Q39101; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
GO; GO:0005506; F:iron ion binding; TAS:TAIR.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0009908; P:flower development; IGI:TAIR.
GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
GO; GO:0055072; P:iron ion homeostasis; IGI:TAIR.
GO; GO:0006826; P:iron ion transport; IGI:TAIR.
GO; GO:0048366; P:leaf development; IGI:TAIR.
GO; GO:0015979; P:photosynthesis; IGI:TAIR.
GO; GO:0009617; P:response to bacterium; IMP:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
GO; GO:0010039; P:response to iron ion; IEP:TAIR.
GO; GO:0000302; P:response to reactive oxygen species; IGI:TAIR.
GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
Gene3D; 1.20.1260.10; -; 1.
InterPro; IPR001519; Ferritin.
InterPro; IPR012347; Ferritin-like.
InterPro; IPR009040; Ferritin-like_diiron.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR014034; Ferritin_CS.
InterPro; IPR008331; Ferritin_DPS_dom.
PANTHER; PTHR11431; PTHR11431; 1.
Pfam; PF00210; Ferritin; 1.
SUPFAM; SSF47240; SSF47240; 1.
PROSITE; PS00204; FERRITIN_2; 1.
PROSITE; PS50905; FERRITIN_LIKE; 1.
2: Evidence at transcript level;
Chloroplast; Complete proteome; Iron; Iron storage; Metal-binding;
Oxidoreductase; Plastid; Reference proteome; Transit peptide.
TRANSIT 1 48 Chloroplast. {ECO:0000250}.
CHAIN 49 255 Ferritin-1, chloroplastic.
/FTId=PRO_0000008854.
DOMAIN 88 241 Ferritin-like diiron.
{ECO:0000255|PROSITE-ProRule:PRU00085}.
REGION 49 87 Extension peptide (EP).
METAL 105 105 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
METAL 140 140 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
METAL 140 140 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
METAL 143 143 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
METAL 189 189 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
METAL 223 223 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
CONFLICT 42 42 G -> S (in Ref. 6; AAM61077).
{ECO:0000305}.
CONFLICT 67 67 F -> L (in Ref. 6; AAM61077).
{ECO:0000305}.
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


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