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P07798

- FRI2_LITCT

UniProt

P07798 - FRI2_LITCT

Protein

Ferritin, middle subunit

Gene
N/A
Organism
Lithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Status
Reviewed - Annotation score: 4 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.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi24 – 241Iron 1
    Metal bindingi59 – 591Iron 1
    Metal bindingi59 – 591Iron 2
    Metal bindingi62 – 621Iron 1
    Metal bindingi104 – 1041Iron 2
    Metal bindingi138 – 1381Iron 2
    Metal bindingi141 – 1411Iron 2

    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-RKP07798.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferritin, middle subunit (EC:1.16.3.1)
    Short name:
    Ferritin M
    Alternative name(s):
    Ferritin H'
    Ferritin X
    OrganismiLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
    Taxonomic identifieri8400 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 176175Ferritin, middle subunitPRO_0000201073Add
    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 – 12028
    Helixi124 – 13310
    Helixi135 – 15420
    Turni155 – 1595
    Helixi161 – 17010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MFRX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-176[»]
    3KA3X-ray1.40A1-176[»]
    3KA4X-ray1.40A1-176[»]
    3KA6X-ray1.40A1-176[»]
    3KA8X-ray1.35A1-176[»]
    3KA9X-ray1.45A1-176[»]
    3RBCX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-176[»]
    3RE7X-ray2.82A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-176[»]
    3RGDX-ray2.89A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-176[»]
    3SE1X-ray1.65A1-176[»]
    3SH6X-ray1.40A1-176[»]
    3SHXX-ray1.35A1-176[»]
    4DASX-ray2.56A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-176[»]
    ProteinModelPortaliP07798.
    SMRiP07798. Positions 2-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07798.

    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.

    P07798-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVSQVRQNYH SDCEAAVNRM LNLELYASYT YSSMYAFFDR DDVALHNVAE    50
    FFKEHSHEER EHAEKFMKYQ NKRGGRVVLQ DIKKPERDEW GNTLEAMQAA 100
    LQLEKTVNQA LLDLHKLATD KVDPHLCDFL ESEYLEEQVK DIKRIGDFIT 150
    NLKRLGLPEN GMGEYLFDKH SVKESS 176
    Length:176
    Mass (Da):20,592
    Last modified:January 23, 2007 - v3
    Checksum:iA9F0F5BEB8584D46
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02724 mRNA. Translation: AAA49525.1.
    PIRiC27805.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02724 mRNA. Translation: AAA49525.1 .
    PIRi C27805.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MFR X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-176 [» ]
    3KA3 X-ray 1.40 A 1-176 [» ]
    3KA4 X-ray 1.40 A 1-176 [» ]
    3KA6 X-ray 1.40 A 1-176 [» ]
    3KA8 X-ray 1.35 A 1-176 [» ]
    3KA9 X-ray 1.45 A 1-176 [» ]
    3RBC X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-176 [» ]
    3RE7 X-ray 2.82 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-176 [» ]
    3RGD X-ray 2.89 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-176 [» ]
    3SE1 X-ray 1.65 A 1-176 [» ]
    3SH6 X-ray 1.40 A 1-176 [» ]
    3SHX X-ray 1.35 A 1-176 [» ]
    4DAS X-ray 2.56 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-176 [» ]
    ProteinModelPortali P07798.
    SMRi P07798. Positions 2-172.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG000410.

    Enzyme and pathway databases

    SABIO-RK P07798.

    Miscellaneous databases

    EvolutionaryTracei P07798.

    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. "Crystal structure of bullfrog M ferritin at 2.8 A resolution: analysis of subunit interactions and the binuclear metal center."
      Ha Y., Shi D., Small G.W., Theil E.C., Allewell N.M.
      J. Biol. Inorg. Chem. 4:243-256(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiFRI2_LITCT
    AccessioniPrimary (citable) accession number: P07798
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 94 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