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P07229

- FRI1_LITCT

UniProt

P07229 - FRI1_LITCT

Protein

Ferritin, higher subunit

Gene
N/A
Organism
Lithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi24 – 241Iron 1PROSITE-ProRule annotation
    Metal bindingi58 – 581IronPROSITE-ProRule annotation
    Metal bindingi59 – 591Iron 1PROSITE-ProRule annotation
    Metal bindingi59 – 591Iron 2PROSITE-ProRule annotation
    Metal bindingi62 – 621Iron 1PROSITE-ProRule annotation
    Metal bindingi104 – 1041Iron 2PROSITE-ProRule annotation
    Metal bindingi138 – 1381Iron 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

    Enzyme and pathway databases

    SABIO-RKP07229.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferritin, higher subunit (EC:1.16.3.1)
    Short name:
    Ferritin H
    OrganismiLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
    Taxonomic identifieri8400 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi83 – 831K → Q: Improves crystallization.
    Mutagenesisi135 – 1351L → P: Reduces initial rate of ferroxidation and accelerates iron release. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 176175Ferritin, higher subunitPRO_0000201072Add
    BLAST

    Interactioni

    Subunit structurei

    Oligomer of 24 subunits. The functional molecule is roughly spherical and contains a central cavity into which the polymeric mineral iron core is deposited.

    Structurei

    Secondary structure

    1
    176
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 3828
    Turni41 – 433
    Helixi46 – 7328
    Helixi93 – 11321
    Helixi138 – 15417
    Turni155 – 1595
    Helixi161 – 17010
    Turni171 – 1733

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BG7X-ray1.85A1-176[»]
    ProteinModelPortaliP07229.
    SMRiP07229. Positions 3-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07229.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 156150Ferritin-like diironPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    HOVERGENiHBG000410.

    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.

    P07229-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSQVRQNFH RDCEAAINRM VNMELYASYT YLSMAFYFDR DDIALHNVAK    50
    FFKEQSHEER EHAEKLMKDQ NKRGGRIVLQ DVKKPERDEW GNTLEAMQAA 100
    LQLEKTVNQA LLDLHKVGSD KVDPHLCDFL ETEYLEEQVK SIKQLGDYIT 150
    NLKRLGLPQN GMGEYLFDKH TMGESS 176
    Length:176
    Mass (Da):20,533
    Last modified:January 23, 2007 - v3
    Checksum:i81EF7F13362ED5DE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831K → E in AAA49532. (PubMed:3484480)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15655 mRNA. Translation: AAA49523.1.
    M12120 mRNA. Translation: AAA49532.1.
    PIRiA25627. FRFGL.
    A27805.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15655 mRNA. Translation: AAA49523.1 .
    M12120 mRNA. Translation: AAA49532.1 .
    PIRi A25627. FRFGL.
    A27805.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BG7 X-ray 1.85 A 1-176 [» ]
    ProteinModelPortali P07229.
    SMRi P07229. Positions 3-172.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG000410.

    Enzyme and pathway databases

    SABIO-RK P07229.

    Miscellaneous databases

    EvolutionaryTracei P07229.

    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. "Differences in the regulation of messenger RNA for housekeeping and specialized-cell ferritin. A comparison of three distinct ferritin complementary DNAs, the corresponding subunits, and identification of the first processed in amphibia."
      Dickey L.F., Sreedharan S., Theil E.C., Didsbury J.R., Wang Y.-H., Kaufman R.E.
      J. Biol. Chem. 262:7901-7907(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Multiple red cell ferritin mRNAs, which code for an abundant protein in the embryonic cell type, analyzed by cDNA sequence and by primer extension of the 5'-untranslated regions."
      Didsbury J.R., Theil E.C., Kaufman R.E., Dickey L.F.
      J. Biol. Chem. 261:949-955(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Erythrocyte.
    3. "Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release?"
      Takagi H., Shi D., Ha Y., Allewell N.M., Theil E.C.
      J. Biol. Chem. 273:18685-18688(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT GLN-84, FUNCTION, MUTAGENESIS OF LEU-135.

    Entry informationi

    Entry nameiFRI1_LITCT
    AccessioniPrimary (citable) accession number: P07229
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 90 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are three types of ferritin subunits in amphibia: L, M and H chains. M and H chains are fast mineralizing; the L chain is very slow mineralizing.

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3