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Q9SRL5

- FRI2_ARATH

UniProt

Q9SRL5 - FRI2_ARATH

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Protein
Ferritin-2, chloroplastic
Gene
FER2, At3g11050, F11B9.26, F9F8.13
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi100 – 1001Iron 1 By similarity
Metal bindingi135 – 1351Iron 1 By similarity
Metal bindingi135 – 1351Iron 2 By similarity
Metal bindingi138 – 1381Iron 1 By similarity
Metal bindingi184 – 1841Iron 2 By similarity
Metal bindingi218 – 2181Iron 2 By similarity

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. cellular iron ion homeostasis Source: UniProtKB-KW
  2. iron ion transport Source: InterPro
  3. response to abscisic acid Source: TAIR
  4. response to oxidative stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G11050-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin-2, chloroplastic (EC:1.16.3.1)
Gene namesi
Name:FER2
Ordered Locus Names:At3g11050
ORF Names:F11B9.26, F9F8.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G11050.

Subcellular locationi

Plastidchloroplast By similarity

GO - Cellular componenti

  1. chloroplast Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545Chloroplast Reviewed prediction
Add
BLAST
Chaini46 – 253208Ferritin-2, chloroplastic
PRO_0000008855Add
BLAST

Proteomic databases

PaxDbiQ9SRL5.
PRIDEiQ9SRL5.

Expressioni

Inductioni

By abscisic acid (ABA).1 Publication

Gene expression databases

ArrayExpressiQ9SRL5.
GenevestigatoriQ9SRL5.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi5610. 1 interaction.
STRINGi3702.AT3G11050.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9SRL5.
SMRiQ9SRL5. Positions 56-251.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini83 – 236154Ferritin-like diiron
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 8237Extension peptide (EP)
Add
BLAST

Sequence similaritiesi

Belongs to the ferritin family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1528.
HOGENOMiHOG000223383.
InParanoidiQ9SRL5.
KOiK00522.
OMAiSASHAYM.
PhylomeDBiQ9SRL5.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SRL5-1 [UniParc]FASTAAdd to Basket

« Hide

MLHKASPALS LLSSGYTGGG NLFPPSRNSS NLLFSPSGSR FSVQAAKGTN    50
TKSLTGVVFE PFEEVKKEME LVPTTPFVSL ARHKFSDDSE SAINDQINVE 100
YNVSYVYHAL YAYFDRDNVG LKGFAKFFND SSLEERGHAE MFMEYQNKRG 150
GRVKLQSILM PVSEFDHEEK GDALHAMELA LSLEKLTNEK LLKLQSVGVK 200
NNDVQLVDFV ESEFLGEQVE AIKKISEYVA QLRRIGKGHG VWHFDQMLLN 250
DEV 253
Length:253
Mass (Da):28,378
Last modified:May 1, 2000 - v1
Checksum:i92A59DCA3B8EBE3A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31H → L in AAM65872. 1 Publication
Sequence conflicti16 – 161Y → S in AAM65872. 1 Publication
Sequence conflicti32 – 321L → R in AAM65872. 1 Publication
Sequence conflicti40 – 401R → K in AAM65872. 1 Publication
Sequence conflicti69 – 702ME → LD in AAM65872. 1 Publication
Sequence conflicti89 – 891S → A in AAM65872. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_187716.1. NM_111942.3.
UniGeneiAt.17409.

Genome annotation databases

EnsemblPlantsiAT3G11050.1; AT3G11050.1; AT3G11050.
GeneIDi820276.
KEGGiath:AT3G11050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_187716.1. NM_111942.3.
UniGenei At.17409.

3D structure databases

ProteinModelPortali Q9SRL5.
SMRi Q9SRL5. Positions 56-251.
ModBasei Search...

Protein-protein interaction databases

BioGridi 5610. 1 interaction.
STRINGi 3702.AT3G11050.1-P.

Proteomic databases

PaxDbi Q9SRL5.
PRIDEi Q9SRL5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G11050.1 ; AT3G11050.1 ; AT3G11050 .
GeneIDi 820276.
KEGGi ath:AT3G11050.

Organism-specific databases

TAIRi AT3G11050.

Phylogenomic databases

eggNOGi COG1528.
HOGENOMi HOG000223383.
InParanoidi Q9SRL5.
KOi K00522.
OMAi SASHAYM.
PhylomeDBi Q9SRL5.

Enzyme and pathway databases

BioCyci ARA:AT3G11050-MONOMER.

Gene expression databases

ArrayExpressi Q9SRL5.
Genevestigatori Q9SRL5.

Family and domain databases

Gene3Di 1.20.1260.10. 1 hit.
InterProi IPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view ]
PANTHERi PTHR11431. PTHR11431. 1 hit.
Pfami PF00210. Ferritin. 1 hit.
[Graphical view ]
SUPFAMi SSF47240. SSF47240. 1 hit.
PROSITEi PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-212.
    Strain: cv. Columbia.
    Tissue: Leaf.

Entry informationi

Entry nameiFRI2_ARATH
AccessioniPrimary (citable) accession number: Q9SRL5
Secondary accession number(s): Q42288, Q8L9N6, Q8WHW4
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi