(data stored in ACNUC13479 zone)

SWISSPROT: 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   07-JUN-2017, entry version 140.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   accumulated in response to iron through an oxidative pathway
RT   independent of abscisic 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)
RT   involved in AtFer1 and ZmFer1 plant ferritin gene transcriptional
RT   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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
CC       form. Important for iron homeostasis. Has ferroxidase activity.
CC       Iron is taken up in the ferrous form and deposited as ferric
CC       hydroxides after oxidation (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits:
CC       L (light) chain and H (heavy) chain. The major chain can be light
CC       or heavy, depending on the species and tissue type. The functional
CC       molecule forms a roughly spherical shell with a diameter of 12 nm
CC       and contains a central cavity into which the insoluble mineral
CC       iron core is deposited (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- INDUCTION: Up-regulated by iron overload treatment, and by
CC       H(2)O(2) (PubMed:11672431). Up-regulated by the phosphate
CC       starvation response transcription factor PHR1 (PubMed:23788639).
CC       {ECO:0000269|PubMed:11672431, ECO:0000269|PubMed:23788639}.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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   UniGene; At.23533; -.
DR   UniGene; At.73124; -.
DR   UniGene; At.75488; -.
DR   ProteinModelPortal; Q39101; -.
DR   SMR; Q39101; -.
DR   BioGrid; 16996; 8.
DR   STRING; 3702.AT5G01600.1; -.
DR   iPTMnet; Q39101; -.
DR   PaxDb; Q39101; -.
DR   PRIDE; Q39101; -.
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   eggNOG; COG1528; LUCA.
DR   HOGENOM; HOG000223383; -.
DR   InParanoid; Q39101; -.
DR   KO; K00522; -.
DR   OMA; ECGLRAM; -.
DR   OrthoDB; EOG09360PX4; -.
DR   PhylomeDB; Q39101; -.
DR   BioCyc; ARA:AT5G01600-MONOMER; -.
DR   Reactome; R-ATH-6798695; Neutrophil degranulation.
DR   Reactome; R-ATH-917937; Iron uptake and transport.
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; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
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:0009735; P:response to cytokinin; IDA: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; IPR009040; Ferritin-like_diiron.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012347; Ferritin-rel.
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;
DR   PRODOM; Q39101.
DR   SWISS-2DPAGE; Q39101.
KW   Chloroplast; Complete proteome; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT       1     48       Chloroplast. {ECO:0000250}.
FT   CHAIN        49    255       Ferritin-1, chloroplastic.
FT                                /FTId=PRO_0000008854.
FT   DOMAIN       88    241       Ferritin-like diiron.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00085}.
FT   REGION       49     87       Extension peptide (EP).
FT   METAL       105    105       Iron 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   METAL       140    140       Iron 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   METAL       140    140       Iron 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   METAL       143    143       Iron 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   METAL       189    189       Iron 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   METAL       223    223       Iron 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   CONFLICT     42     42       G -> S (in Ref. 6; AAM61077).
FT                                {ECO:0000305}.
FT   CONFLICT     67     67       F -> L (in Ref. 6; AAM61077).
FT                                {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
//

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