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Q9S756 (FRI4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ferritin-4, chloroplastic

EC=1.16.3.1
Gene names
Name:FER4
Ordered Locus Names:At2g40300
ORF Names:T07M07.18, T3G21.7
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.

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 – 5757Chloroplast Potential
Chain58 – 259202Ferritin-4, chloroplastic
PRO_0000008857

Regions

Domain91 – 244154Ferritin-like diiron
Region58 – 9033Extension peptide (EP)

Sites

Metal binding1081Iron 1 By similarity
Metal binding1431Iron 1 By similarity
Metal binding1431Iron 2 By similarity
Metal binding1461Iron 1 By similarity
Metal binding1921Iron 2 By similarity
Metal binding2261Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9S756 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CFEC3BA233BAAAA3

FASTA25929,029
        10         20         30         40         50         60 
MLLKTVSSSS SSALSLVNFH GVKKDVSPLL PSISSNLRVS SGKSGNLTFS FRASKSSTTD 

        70         80         90        100        110        120 
ALSGVVFEPF KEVKKELDLV PTSSHLSLAR QKYSDECEAA INEQINVEYN VSYVYHAMYA 

       130        140        150        160        170        180 
YFDRDNIALK GLAKFFKESS LEEREHAEKL MEYQNKRGGR VKLQSIVMPL SEFEHVDKGD 

       190        200        210        220        230        240 
ALYGMELALS LEKLVNEKLL NLHSVASKNN DVHLADFIES EFLTEQVEAI KLISEYVAQL 

       250 
RRVGKGHGTW HFNQMLLEG 

« 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].
Strain: cv. Columbia.
[2]"A cluster of ABA-regulated genes on Arabidopsis thaliana BAC T07M07."
Wang M.L., Belmonte S., Kim U., Dolan M., Morris J.W., Goodman H.M.
Genome Res. 9:325-333(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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
AJ312191 mRNA. Translation: CAC85400.1.
AF085279 Genomic DNA. Translation: AAD25945.1.
AC007020 Genomic DNA. Translation: AAD25665.1.
CP002685 Genomic DNA. Translation: AEC09810.1.
AY062795 mRNA. Translation: AAL32873.1.
AY081615 mRNA. Translation: AAM10177.1.
PIRG84827.
RefSeqNP_181559.1. NM_129588.4.
UniGeneAt.27228.
At.69019.

3D structure databases

ProteinModelPortalQ9S756.
SMRQ9S756. Positions 67-257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid3960. 1 interaction.

Proteomic databases

PaxDbQ9S756.
PRIDEQ9S756.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G40300.1; AT2G40300.1; AT2G40300.
GeneID818622.
KEGGath:AT2G40300.

Organism-specific databases

TAIRAT2G40300.

Phylogenomic databases

eggNOGCOG1528.
HOGENOMHOG000223383.
InParanoidQ9S756.
KOK00522.
OMAAMAYHFD.
PhylomeDBQ9S756.
ProtClustDBCLSN2683400.

Enzyme and pathway databases

BioCycARA:AT2G40300-MONOMER.

Gene expression databases

GenevestigatorQ9S756.

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.
PROSITEPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRI4_ARATH
AccessionPrimary (citable) accession number: Q9S756
Secondary accession number(s): Q8WHW5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 102 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