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Q9LYN2 (FRI3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferritin-3, chloroplastic

EC=1.16.3.1
Gene names
Name:FER3
Ordered Locus Names:At3g56090
ORF Names:F18O21_50
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Catalytic activity

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

Subunit structure

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.

Subcellular location

Plastidchloroplast By similarity.

Induction

By iron overload treatment. Ref.1

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4949Chloroplast Potential
Chain50 – 259210Ferritin-3, chloroplastic
PRO_0000008856

Regions

Domain89 – 242154Ferritin-like diiron
Region50 – 8839Extension peptide (EP)

Sites

Metal binding1061Iron 1 By similarity
Metal binding1411Iron 1 By similarity
Metal binding1411Iron 2 By similarity
Metal binding1441Iron 1 By similarity
Metal binding1901Iron 2 By similarity
Metal binding2241Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9LYN2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7E06E16761C2FB1B

FASTA25928,837
        10         20         30         40         50         60 
MLLKAASTFS LLNIHGEKKD ISPLFSSSSS ISSPVSSGKS GNLSFPLRAS KSSTTTTSTL 

        70         80         90        100        110        120 
SGVVFEPFEE VKKEMDLVPS GQQLSLARHL YSPECEAAVN EQINVEYNVS YVYHALYAYF 

       130        140        150        160        170        180 
DRDNVALKGL AKFFKESSVE EREHAELLME YQNKRGGRVK LQPMVLPQSE FDHPEKGDAL 

       190        200        210        220        230        240 
YAMELALSLE KLVNEKLLNL HSVASKNDDV QLADFIESVF LNEQVEAIKK ISEYVSQLRR 

       250 
LGKGHGTWHF DQELLGAAA 

« Hide

References

« Hide 'large scale' references
[1]"Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family."
Petit J.-M., Briat J.-F., Lobreaux S.
Biochem. J. 359:575-582(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ312190 mRNA. Translation: CAC85399.1.
AL163763 Genomic DNA. Translation: CAB87408.1.
CP002686 Genomic DNA. Translation: AEE79476.1.
AY072221 mRNA. Translation: AAL60042.1.
AY122951 mRNA. Translation: AAM67484.1.
PIRT47726.
RefSeqNP_191168.1. NM_115467.4.
UniGeneAt.20042.
At.67841.

3D structure databases

ProteinModelPortalQ9LYN2.
SMRQ9LYN2. Positions 62-255.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid10091. 1 interaction.
STRING3702.AT3G56090.1-P.

Proteomic databases

PaxDbQ9LYN2.
PRIDEQ9LYN2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G56090.1; AT3G56090.1; AT3G56090.
GeneID824775.
KEGGath:AT3G56090.

Organism-specific databases

TAIRAT3G56090.

Phylogenomic databases

eggNOGCOG1528.
HOGENOMHOG000223383.
InParanoidQ9LYN2.
KOK00522.
OMATHIDYLT.
PhylomeDBQ9LYN2.

Enzyme and pathway databases

BioCycARA:AT3G56090-MONOMER.

Gene expression databases

ArrayExpressQ9LYN2.
GenevestigatorQ9LYN2.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERPTHR11431. PTHR11431. 1 hit.
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRI3_ARATH
AccessionPrimary (citable) accession number: Q9LYN2
Secondary accession number(s): Q8WHW6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names