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Q39101 (FRI1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. 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
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-1, chloroplastic
Short name=AtFer1
EC=1.16.3.1
Gene names
Name:FER1
Ordered Locus Names:At5g01600
ORF Names:F7A7.120
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length255 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

Plastid › chloroplast.

Induction

By iron overload treatment, and by H2O2. Ref.7

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
   Biological processIron storage
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular iron ion homeostasis

Inferred from electronic annotation. Source: UniProtKB-KW

flower development

Inferred from genetic interaction PubMed 18826427. Source: TAIR

iron ion homeostasis

Inferred from genetic interaction PubMed 18826427. Source: TAIR

iron ion transport

Inferred from genetic interaction PubMed 18826427. Source: TAIR

leaf development

Inferred from genetic interaction PubMed 18826427. Source: TAIR

photosynthesis

Inferred from genetic interaction PubMed 18826427. Source: TAIR

response to bacterium

Inferred from expression pattern PubMed 15998312PubMed 19121106. Source: TAIR

response to cold

Inferred from expression pattern PubMed 14535880. Source: TAIR

response to hydrogen peroxide

Inferred from expression pattern Ref.7. Source: TAIR

response to iron ion

Inferred from expression pattern Ref.7. Source: TAIR

response to zinc ion

Inferred from expression pattern PubMed 19880396. Source: TAIR

   Cellular_componentchloroplast stroma

Inferred from direct assay PubMed 18633119PubMed 20061580. Source: TAIR

chloroplast thylakoid membrane

Inferred from direct assay PubMed 14729914. Source: TAIR

mitochondrion

Inferred from direct assay PubMed 22923678. Source: TAIR

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

ferroxidase activity

Inferred from electronic annotation. Source: EC

iron ion binding

Traceable author statement Ref.7. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4848Chloroplast By similarity
Chain49 – 255207Ferritin-1, chloroplastic
PRO_0000008854

Regions

Domain88 – 241154Ferritin-like diiron
Region49 – 8739Extension peptide (EP)

Sites

Metal binding1051Iron 1 By similarity
Metal binding1401Iron 1 By similarity
Metal binding1401Iron 2 By similarity
Metal binding1431Iron 1 By similarity
Metal binding1891Iron 2 By similarity
Metal binding2231Iron 2 By similarity

Experimental info

Sequence conflict421G → S in AAM61077. Ref.6
Sequence conflict671F → L in AAM61077. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q39101 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C40E89CA4548FCB0

FASTA25528,178
        10         20         30         40         50         60 
MASNALSSFT AANPALSPKP LLPHGSASPS VSLGFSRKVG GGRAVVVAAA TVDTNNMPMT 

        70         80         90        100        110        120 
GVVFQPFEEV KKADLAIPIT SHASLARQRF ADASEAVINE QINVEYNVSY VYHSMYAYFD 

       130        140        150        160        170        180 
RDNVAMKGLA KFFKESSEEE RGHAEKFMEY QNQRGGRVKL HPIVSPISEF EHAEKGDALY 

       190        200        210        220        230        240 
AMELALSLEK LTNEKLLNVH KVASENNDPQ LADFVESEFL GEQIEAIKKI SDYITQLRMI 

       250 
GKGHGVWHFD QMLLN

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a ferritin mRNA from Arabidopsis thaliana accumulated in response to iron through an oxidative pathway independent of abscisic acid."
Gaymard F., Boucherez J., Briat J.-F.
Biochem. J. 318:67-73(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of an iron-dependent regulatory sequence (IDRS) involved in AtFer1 and ZmFer1 plant ferritin gene transcriptional control by iron."
Petit J.-M., van Wuytswinkel O., Briat J.-F., Lobreaux S.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Landsberg erecta.
[3]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 408:823-826(2000) [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.
[6]"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].
[7]"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: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X94248 mRNA. Translation: CAA63932.1.
AF229850 Genomic DNA. Translation: AAF73918.1.
AL161946 Genomic DNA. Translation: CAB82276.1.
CP002688 Genomic DNA. Translation: AED90364.1.
AF326869 mRNA. Translation: AAG41451.1.
AF339691 mRNA. Translation: AAK00373.1.
AF412065 mRNA. Translation: AAL06518.1.
AY084509 mRNA. Translation: AAM61077.1.
IPIIPI00519549.
PIRS71880.
RefSeqNP_195780.1. NM_120238.4.
UniGeneAt.23533.
At.73124.
At.75488.

3D structure databases

ProteinModelPortalQ39101.
SMRQ39101. Positions 82-255.
ModBaseSearch...

Proteomic databases

PaxDbQ39101.
PRIDEQ39101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G01600.1; AT5G01600.1; AT5G01600.
GeneID831720.
KEGGath:AT5G01600.

Organism-specific databases

TAIRAt5g01600.

Phylogenomic databases

eggNOGCOG1528.
HOGENOMHOG000223383.
InParanoidQ39101.
KOK00522.
OMAASENNDP.
PhylomeDBQ39101.
ProtClustDBCLSN2683400.

Gene expression databases

ArrayExpressQ39101.
GenevestigatorQ39101.
GermOnlineAT5G01600. Arabidopsis thaliana.

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. Ferritin/RR_like. 1 hit.
PROSITEPS00540. FERRITIN_1. False negative.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRI1_ARATH
AccessionPrimary (citable) accession number: Q39101
Secondary accession number(s): Q8LG19
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents