Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9SRL5

- FRI2_ARATH

UniProt

Q9SRL5 - FRI2_ARATH

Protein

Ferritin-2, chloroplastic

Gene

FER2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi100 – 1001Iron 1PROSITE-ProRule annotation
    Metal bindingi135 – 1351Iron 1PROSITE-ProRule annotation
    Metal bindingi135 – 1351Iron 2PROSITE-ProRule annotation
    Metal bindingi138 – 1381Iron 1PROSITE-ProRule annotation
    Metal bindingi184 – 1841Iron 2PROSITE-ProRule annotation
    Metal bindingi218 – 2181Iron 2PROSITE-ProRule annotation

    GO - Molecular functioni

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

    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

    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

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4545ChloroplastSequence AnalysisAdd
    BLAST
    Chaini46 – 253208Ferritin-2, chloroplasticPRO_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.By similarity

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SRL5.
    SMRiQ9SRL5. Positions 56-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini83 – 236154Ferritin-like diironPROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Sequence similaritiesi

    Belongs to the ferritin family.Curated
    Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

    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

    Experimental Info

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

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 99 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