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Q9SRL5 (FRI2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. 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-2, chloroplastic

EC=1.16.3.1
Gene names
Name:FER2
Ordered Locus Names:At3g11050
ORF Names:F11B9.26, F9F8.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length253 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 abscisic acid (ABA). 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 – 4545Chloroplast Potential
Chain46 – 253208Ferritin-2, chloroplastic
PRO_0000008855

Regions

Domain83 – 236154Ferritin-like diiron
Region46 – 8237Extension peptide (EP)

Sites

Metal binding1001Iron 1 By similarity
Metal binding1351Iron 1 By similarity
Metal binding1351Iron 2 By similarity
Metal binding1381Iron 1 By similarity
Metal binding1841Iron 2 By similarity
Metal binding2181Iron 2 By similarity

Experimental info

Sequence conflict31H → L in AAM65872. Ref.5
Sequence conflict161Y → S in AAM65872. Ref.5
Sequence conflict321L → R in AAM65872. Ref.5
Sequence conflict401R → K in AAM65872. Ref.5
Sequence conflict69 – 702ME → LD in AAM65872. Ref.5
Sequence conflict891S → A in AAM65872. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9SRL5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 92A59DCA3B8EBE3A

FASTA25328,378
        10         20         30         40         50         60 
MLHKASPALS LLSSGYTGGG NLFPPSRNSS NLLFSPSGSR FSVQAAKGTN TKSLTGVVFE 

        70         80         90        100        110        120 
PFEEVKKEME LVPTTPFVSL ARHKFSDDSE SAINDQINVE YNVSYVYHAL YAYFDRDNVG 

       130        140        150        160        170        180 
LKGFAKFFND SSLEERGHAE MFMEYQNKRG GRVKLQSILM PVSEFDHEEK GDALHAMELA 

       190        200        210        220        230        240 
LSLEKLTNEK LLKLQSVGVK NNDVQLVDFV ESEFLGEQVE AIKKISEYVA QLRRIGKGHG 

       250 
VWHFDQMLLN DEV 

« 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]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs."
Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C., Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R., Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J. expand/collapse author list , Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.
Plant J. 9:101-124(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-212.
Strain: cv. Columbia.
Tissue: Leaf.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ312192 mRNA. Translation: CAC85498.1.
AC009991 Genomic DNA. Translation: AAF01516.1.
AC073395 Genomic DNA. Translation: AAG50984.1.
CP002686 Genomic DNA. Translation: AEE74997.1.
AK175807 mRNA. Translation: BAD43570.1.
AK175899 mRNA. Translation: BAD43662.1.
AK175901 mRNA. Translation: BAD43664.1.
AK175910 mRNA. Translation: BAD43673.1.
AY088333 mRNA. Translation: AAM65872.1.
Z34949 mRNA. Translation: CAA84408.1.
RefSeqNP_187716.1. NM_111942.3.
UniGeneAt.17409.

3D structure databases

ProteinModelPortalQ9SRL5.
SMRQ9SRL5. Positions 56-251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid5610. 1 interaction.
STRING3702.AT3G11050.1-P.

Proteomic databases

PaxDbQ9SRL5.
PRIDEQ9SRL5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G11050.1; AT3G11050.1; AT3G11050.
GeneID820276.
KEGGath:AT3G11050.

Organism-specific databases

TAIRAT3G11050.

Phylogenomic databases

eggNOGCOG1528.
HOGENOMHOG000223383.
InParanoidQ9SRL5.
KOK00522.
OMASASHAYM.
PhylomeDBQ9SRL5.

Enzyme and pathway databases

BioCycARA:AT3G11050-MONOMER.

Gene expression databases

ArrayExpressQ9SRL5.
GenevestigatorQ9SRL5.

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 nameFRI2_ARATH
AccessionPrimary (citable) accession number: Q9SRL5
Secondary accession number(s): Q42288, Q8L9N6, Q8WHW4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 98 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