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P85839

- FRIMS_TREBE

UniProt

P85839 - FRIMS_TREBE

Protein

Ferritin, spleen middle subunit

Gene
N/A
Organism
Trematomus bernacchii (Emerald rockcod) (Pagothenia bernacchii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 28 (01 Oct 2014)
      Sequence version 1 (01 Jul 2008)
      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.2 Publications

    pH dependencei

    Stable at acidic pHs.1 Publication

    Temperature dependencei

    Thermostable.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi24 – 241Iron 1By similarityPROSITE-ProRule annotation
    Metal bindingi59 – 591Iron 1By similarityPROSITE-ProRule annotation
    Metal bindingi59 – 591Iron 2By similarityPROSITE-ProRule annotation
    Metal bindingi62 – 621Iron 1By similarityPROSITE-ProRule annotation
    Metal bindingi104 – 1041Iron 2By similarityPROSITE-ProRule annotation
    Metal bindingi138 – 1381Iron 2By similarityPROSITE-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, spleen middle subunit2 Publications (EC:1.16.3.1)
    Short name:
    Ferritin M2 Publications
    OrganismiTrematomus bernacchii (Emerald rockcod) (Pagothenia bernacchii)
    Taxonomic identifieri40690 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataPercomorphariaPerciformesNotothenioideiNototheniidaeTrematomus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 176176Ferritin, spleen middle subunitPRO_0000343460Add
    BLAST

    Expressioni

    Tissue specificityi

    Spleen (at protein level).2 Publications

    Interactioni

    Subunit structurei

    In spleen, forms a homopolymer. 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.2 PublicationsCurated

    Structurei

    3D structure databases

    ProteinModelPortaliP85839.
    SMRiP85839. Positions 3-172.
    ModBaseiSearch...
    MobiDBiSearch...

    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.Sequence Analysis
    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.
    PROSITEiPS00204. FERRITIN_2. 1 hit.
    PS50905. FERRITIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P85839-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSQVRQNYH RDCEAAVNRM INMELFASYS YTSMAFYFSR DDVALPGFAH    50
    FFKENSDEER EHADKLLTFQ NSRGGRIFLQ DIKKPERDEW GNGVDVMQCA 100
    LQLEKNVNQA LLDLHKIASG KVDPHMCDFL ETHYLNEQVE SIKKLGDFIT 150
    NLSRMDAVKN KMAEYLFDKH TMGGKN 176
    Length:176
    Mass (Da):20,426
    Last modified:July 1, 2008 - v1
    Checksum:i014A34B79B94411C
    GO

    Cross-referencesi

    3D structure databases

    ProteinModelPortali P85839.
    SMRi P85839. Positions 3-172.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG000410.

    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. "Ferritin from the spleen of the Antarctic teleost Trematomus bernacchii is an M-type homopolymer."
      Mignogna G., Chiaraluce R., Consalvi V., Cavallo S., Stefanini S., Chiancone E.
      Eur. J. Biochem. 269:1600-1606(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY.
      Tissue: Spleen1 Publication.
    2. "The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi."
      Giorgi A., Mignogna G., Bellapadrona G., Gattoni M., Chiaraluce R., Consalvi V., Chiancone E., Stefanini S.
      Arch. Biochem. Biophys. 478:69-74(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY.
      Tissue: Spleen1 Publication.

    Entry informationi

    Entry nameiFRIMS_TREBE
    AccessioniPrimary (citable) accession number: P85839
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 2008
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 28 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3