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Q7SXA6

- FRIH3_XENLA

UniProt

Q7SXA6 - FRIH3_XENLA

Protein

Ferritin heavy chain, oocyte isoform

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      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 bindingi24 – 241Iron 1PROSITE-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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferritin heavy chain, oocyte isoform (EC:1.16.3.1)
    Alternative name(s):
    A-ferritin
    GV-HCH
    XeAF
    OrganismiXenopus laevis (African clawed frog)Imported
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-955508. ftmt.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 177177Ferritin heavy chain, oocyte isoformPRO_0000201079Add
    BLAST

    Proteomic databases

    PRIDEiQ7SXA6.

    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 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ7SXA6.
    SMRiQ7SXA6. Positions 3-173.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Belongs to the ferritin family.Curated
    Contains 1 ferritin-like diiron domain.CuratedPROSITE-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.

    Q7SXA6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSQIRQNFH QECEAAINRQ VNMELYASYV YLSMSYYFDR DDVALKNFAK    50
    YFLHQSHEER EHAEKLMKMQ NQRGGRLFLQ DIKKPERDEW ANGLEALECS 100
    LQLEKNVNQS ILELHKLSTD HNDPHLCDFL ESHYLDEQVK SMKELGDHIT 150
    NLRRMGAPSN GLAEYLFDKH TLGEDHE 177
    Length:177
    Mass (Da):20,918
    Last modified:October 1, 2003 - v1
    Checksum:iEC490899B62B0C7B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 821I → L AA sequence (PubMed:14509834)Curated
    Sequence conflicti111 – 1111I → L AA sequence (PubMed:14509834)Curated
    Sequence conflicti149 – 1502IT → LA AA sequence (PubMed:14509834)Curated
    Sequence conflicti173 – 1742GE → W AA sequence (PubMed:14509834)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF538970 mRNA. Translation: AAQ10928.1.
    UniGeneiXl.5269.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF538970 mRNA. Translation: AAQ10928.1 .
    UniGenei Xl.5269.

    3D structure databases

    ProteinModelPortali Q7SXA6.
    SMRi Q7SXA6. Positions 3-173.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q7SXA6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Xenbasei XB-GENE-955508. ftmt.

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

    Publicationsi

    1. "Two types of new ferritin cDNA sequences from Xenopus laevis germinal vesicle oocytes."
      Huang W.-H., Guo H.-B., Huang X.-Y., Sun F.-Z.
      DNA Seq. 14:211-214(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 77-83; 106-116; 144-153 AND 155-177.
      Tissue: Oocyte1 Publication.

    Entry informationi

    Entry nameiFRIH3_XENLA
    AccessioniPrimary (citable) accession number: Q7SXA6
    Secondary accession number(s): P83457
    , P83460, P83462, P83463
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 52 of the entry and version 1 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 By similarity.By similarity

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3