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P19975

- FRI1_PEA

UniProt

P19975 - FRI1_PEA

Protein

Ferritin-1, chloroplastic

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (01 Oct 1993)
      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.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi98 – 981Iron 1PROSITE-ProRule annotation
    Metal bindingi136 – 1361Iron 1PROSITE-ProRule annotation
    Metal bindingi182 – 1821Iron 2PROSITE-ProRule annotation
    Metal bindingi216 – 2161Iron 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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Iron storage

    Keywords - Ligandi

    Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferritin-1, chloroplastic (EC:1.16.3.1)
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4747Chloroplast1 PublicationAdd
    BLAST
    Chaini48 – 253206Ferritin-1, chloroplasticPRO_0000008862Add
    BLAST

    Proteomic databases

    PRIDEiP19975.

    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.

    Structurei

    3D structure databases

    ProteinModelPortaliP19975.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 234154Ferritin-like diironPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni48 – 8033Extension 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

    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.
    PROSITEiPS00540. FERRITIN_1. 1 hit.
    PS00204. 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.

    P19975-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALSSSKFSS FSGFSLSPVS GNGVQKPCFC DLRVGEKWGS RKFRVSATTA    50
    PLTGVIFEPF EEVKKDYLAV PSVPLVSLAR QNFADECESV INEQINVEYN 100
    ASYVYHSLFA YFDRDNVALK GFAKFFKESS EEHREHAEKL MKYQNTRGGR 150
    VVLHPIKDVP SEFEHVEKGD ALYAMELALS LEKLTNEKLL NVHSVAERNN 200
    DLEMTHFIEG EYLAEQVEAI KKISEYVAQL RRVGKGHGVW HFDQRLLHGV 250
    HGA 253
    Length:253
    Mass (Da):28,619
    Last modified:October 1, 1993 - v2
    Checksum:i9C754BCBDBC926F7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461S → C in CAA51786. (PubMed:7826338)Curated
    Sequence conflicti101 – 1011A → V in CAA51786. (PubMed:7826338)Curated
    Sequence conflicti108 – 1081L → M in CAA51786. (PubMed:7826338)Curated
    Sequence conflicti133 – 1331H → E in CAA51786. (PubMed:7826338)Curated
    Sequence conflicti173 – 1731Y → H in CAA51786. (PubMed:7826338)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64417 mRNA. Translation: CAA45763.1.
    X73369 mRNA. Translation: CAA51786.1.
    PIRiS27358.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64417 mRNA. Translation: CAA45763.1 .
    X73369 mRNA. Translation: CAA51786.1 .
    PIRi S27358.

    3D structure databases

    ProteinModelPortali P19975.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P19975.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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 PS00540. FERRITIN_1. 1 hit.
    PS00204. FERRITIN_2. 1 hit.
    PS50905. FERRITIN_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin."
      Lobreaux S., Yewdall S.J., Briat J.-F., Harrison P.M.
      Biochem. J. 288:931-939(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Purification and characterization of recombinant pea-seed ferritins expressed in Escherichia coli: influence of N-terminus deletions on protein solubility and core formation in vitro."
      Van Wuytswinkel O., Savino G., Briat J.-F.
      Biochem. J. 305:253-261(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Mechanism of the transition from plant ferritin to phytosiderin."
      Laulhere J.-P., Laboure A.M., Briat J.-F.
      J. Biol. Chem. 264:3629-3635(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 48-82.
      Tissue: Seed.

    Entry informationi

    Entry nameiFRI1_PEA
    AccessioniPrimary (citable) accession number: P19975
    Secondary accession number(s): Q43080
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3