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)

Q9LYN2

- FRI3_ARATH

UniProt

Q9LYN2 - FRI3_ARATH

Protein

Ferritin-3, chloroplastic

Gene

FER3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Oct 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 bindingi106 – 1061Iron 1PROSITE-ProRule annotation
    Metal bindingi141 – 1411Iron 1PROSITE-ProRule annotation
    Metal bindingi141 – 1411Iron 2PROSITE-ProRule annotation
    Metal bindingi144 – 1441Iron 1PROSITE-ProRule annotation
    Metal bindingi190 – 1901Iron 2PROSITE-ProRule annotation
    Metal bindingi224 – 2241Iron 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. flower development Source: TAIR
    3. iron ion homeostasis Source: TAIR
    4. iron ion transport Source: TAIR
    5. leaf development Source: TAIR
    6. photosynthesis Source: TAIR
    7. response to iron ion Source: TAIR
    8. response to reactive oxygen species Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Iron storage

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT3G56090-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferritin-3, chloroplastic (EC:1.16.3.1)
    Gene namesi
    Name:FER3
    Ordered Locus Names:At3g56090
    ORF Names:F18O21_50
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G56090.

    Subcellular locationi

    Plastidchloroplast By similarity

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast envelope Source: TAIR
    3. chloroplast stroma Source: TAIR
    4. membrane Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4949ChloroplastSequence AnalysisAdd
    BLAST
    Chaini50 – 259210Ferritin-3, chloroplasticPRO_0000008856Add
    BLAST

    Proteomic databases

    PaxDbiQ9LYN2.
    PRIDEiQ9LYN2.

    Expressioni

    Inductioni

    By iron overload treatment.1 Publication

    Gene expression databases

    ArrayExpressiQ9LYN2.
    GenevestigatoriQ9LYN2.

    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

    BioGridi10091. 4 interactions.
    STRINGi3702.AT3G56090.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LYN2.
    SMRiQ9LYN2. Positions 62-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini89 – 242154Ferritin-like diironPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 8839Extension 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.
    InParanoidiQ9LYN2.
    KOiK00522.
    OMAiTHIDYLT.
    PhylomeDBiQ9LYN2.

    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.

    Q9LYN2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLKAASTFS LLNIHGEKKD ISPLFSSSSS ISSPVSSGKS GNLSFPLRAS    50
    KSSTTTTSTL SGVVFEPFEE VKKEMDLVPS GQQLSLARHL YSPECEAAVN 100
    EQINVEYNVS YVYHALYAYF DRDNVALKGL AKFFKESSVE EREHAELLME 150
    YQNKRGGRVK LQPMVLPQSE FDHPEKGDAL YAMELALSLE KLVNEKLLNL 200
    HSVASKNDDV QLADFIESVF LNEQVEAIKK ISEYVSQLRR LGKGHGTWHF 250
    DQELLGAAA 259
    Length:259
    Mass (Da):28,837
    Last modified:October 1, 2000 - v1
    Checksum:i7E06E16761C2FB1B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ312190 mRNA. Translation: CAC85399.1.
    AL163763 Genomic DNA. Translation: CAB87408.1.
    CP002686 Genomic DNA. Translation: AEE79476.1.
    AY072221 mRNA. Translation: AAL60042.1.
    AY122951 mRNA. Translation: AAM67484.1.
    PIRiT47726.
    RefSeqiNP_191168.1. NM_115467.4.
    UniGeneiAt.20042.
    At.67841.

    Genome annotation databases

    EnsemblPlantsiAT3G56090.1; AT3G56090.1; AT3G56090.
    GeneIDi824775.
    KEGGiath:AT3G56090.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ312190 mRNA. Translation: CAC85399.1 .
    AL163763 Genomic DNA. Translation: CAB87408.1 .
    CP002686 Genomic DNA. Translation: AEE79476.1 .
    AY072221 mRNA. Translation: AAL60042.1 .
    AY122951 mRNA. Translation: AAM67484.1 .
    PIRi T47726.
    RefSeqi NP_191168.1. NM_115467.4.
    UniGenei At.20042.
    At.67841.

    3D structure databases

    ProteinModelPortali Q9LYN2.
    SMRi Q9LYN2. Positions 62-255.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 10091. 4 interactions.
    STRINGi 3702.AT3G56090.1-P.

    Proteomic databases

    PaxDbi Q9LYN2.
    PRIDEi Q9LYN2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G56090.1 ; AT3G56090.1 ; AT3G56090 .
    GeneIDi 824775.
    KEGGi ath:AT3G56090.

    Organism-specific databases

    TAIRi AT3G56090.

    Phylogenomic databases

    eggNOGi COG1528.
    HOGENOMi HOG000223383.
    InParanoidi Q9LYN2.
    KOi K00522.
    OMAi THIDYLT.
    PhylomeDBi Q9LYN2.

    Enzyme and pathway databases

    BioCyci ARA:AT3G56090-MONOMER.

    Gene expression databases

    ArrayExpressi Q9LYN2.
    Genevestigatori Q9LYN2.

    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. "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.
      , 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.

    Entry informationi

    Entry nameiFRI3_ARATH
    AccessioniPrimary (citable) accession number: Q9LYN2
    Secondary accession number(s): Q8WHW6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 11, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 106 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