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Q39101

- FRI1_ARATH

UniProt

Q39101 - FRI1_ARATH

Protein

Ferritin-1, chloroplastic

Gene

FER1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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 bindingi105 – 1051Iron 1PROSITE-ProRule annotation
    Metal bindingi140 – 1401Iron 1PROSITE-ProRule annotation
    Metal bindingi140 – 1401Iron 2PROSITE-ProRule annotation
    Metal bindingi143 – 1431Iron 1PROSITE-ProRule annotation
    Metal bindingi189 – 1891Iron 2PROSITE-ProRule annotation
    Metal bindingi223 – 2231Iron 2PROSITE-ProRule annotation

    GO - Molecular functioni

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

    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 bacterium Source: TAIR
    8. response to cold Source: TAIR
    9. response to hydrogen peroxide Source: TAIR
    10. response to iron ion Source: TAIR
    11. response to reactive oxygen species Source: TAIR
    12. response to zinc ion Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Iron storage

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT5G01600-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferritin-1, chloroplastic (EC:1.16.3.1)
    Short name:
    AtFer1
    Gene namesi
    Name:FER1
    Ordered Locus Names:At5g01600
    ORF Names:F7A7.120
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G01600.

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast stroma Source: TAIR
    3. chloroplast thylakoid membrane Source: TAIR
    4. membrane Source: TAIR
    5. mitochondrion Source: TAIR
    6. thylakoid Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4848ChloroplastBy similarityAdd
    BLAST
    Chaini49 – 255207Ferritin-1, chloroplasticPRO_0000008854Add
    BLAST

    Proteomic databases

    PaxDbiQ39101.
    PRIDEiQ39101.

    Expressioni

    Inductioni

    By iron overload treatment, and by H2O2.1 Publication

    Gene expression databases

    GenevestigatoriQ39101.

    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

    BioGridi16996. 8 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ39101.
    SMRiQ39101. Positions 82-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini88 – 241154Ferritin-like diironPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 8739Extension 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.
    InParanoidiQ39101.
    KOiK00522.
    OMAiASENNDP.
    PhylomeDBiQ39101.

    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.

    Q39101-1 [UniParc]FASTAAdd to Basket

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    MASNALSSFT AANPALSPKP LLPHGSASPS VSLGFSRKVG GGRAVVVAAA    50
    TVDTNNMPMT GVVFQPFEEV KKADLAIPIT SHASLARQRF ADASEAVINE 100
    QINVEYNVSY VYHSMYAYFD RDNVAMKGLA KFFKESSEEE RGHAEKFMEY 150
    QNQRGGRVKL HPIVSPISEF EHAEKGDALY AMELALSLEK LTNEKLLNVH 200
    KVASENNDPQ LADFVESEFL GEQIEAIKKI SDYITQLRMI GKGHGVWHFD 250
    QMLLN 255
    Length:255
    Mass (Da):28,178
    Last modified:November 1, 1996 - v1
    Checksum:iC40E89CA4548FCB0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421G → S in AAM61077. 1 PublicationCurated
    Sequence conflicti67 – 671F → L in AAM61077. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS71880.
    RefSeqiNP_195780.1. NM_120238.4.
    UniGeneiAt.23533.
    At.73124.
    At.75488.

    Genome annotation databases

    EnsemblPlantsiAT5G01600.1; AT5G01600.1; AT5G01600.
    GeneIDi831720.
    KEGGiath:AT5G01600.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S71880.
    RefSeqi NP_195780.1. NM_120238.4.
    UniGenei At.23533.
    At.73124.
    At.75488.

    3D structure databases

    ProteinModelPortali Q39101.
    SMRi Q39101. Positions 82-255.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 16996. 8 interactions.

    Proteomic databases

    PaxDbi Q39101.
    PRIDEi Q39101.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G01600.1 ; AT5G01600.1 ; AT5G01600 .
    GeneIDi 831720.
    KEGGi ath:AT5G01600.

    Organism-specific databases

    TAIRi AT5G01600.

    Phylogenomic databases

    eggNOGi COG1528.
    HOGENOMi HOG000223383.
    InParanoidi Q39101.
    KOi K00522.
    OMAi ASENNDP.
    PhylomeDBi Q39101.

    Enzyme and pathway databases

    BioCyci ARA:AT5G01600-MONOMER.

    Gene expression databases

    Genevestigatori Q39101.

    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. "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.
      , 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.
      , 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.

    Entry informationi

    Entry nameiFRI1_ARATH
    AccessioniPrimary (citable) accession number: Q39101
    Secondary accession number(s): Q8LG19
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 11, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 120 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