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P17663

- FRIHB_XENLA

UniProt

P17663 - FRIHB_XENLA

Protein

Ferritin heavy chain B

Gene

fth1-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 2 (01 Nov 1991)
      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 B
    Short name:
    Ferritin H subunit B
    Alternative name(s):
    Ferritin heavy chain 1 (EC:1.16.3.1)
    Gene namesi
    Name:fth1-b
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-6256345. fth1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 176176Ferritin heavy chain BPRO_0000201077Add
    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 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP17663.
    SMRiP17663. 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.Curated
    Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOVERGENiHBG000410.
    KOiK00522.

    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.

    P17663-1 [UniParc]FASTAAdd to Basket

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    MQSQVRQNFN SDCEAAINRM VNLEMYASYV YLSMSYYFDR DDVALHHVAK    50
    FFKEQSHEER EHAEKFLKYQ NKRGGRVVLQ DIKKPERDEW SNTLEAMQAA 100
    LQLEKTVNQA LLDLHKLASD KVDPQLCDFL ESEYLEEQVK AMKELGDYIT 150
    NLKRLGVPQN GMGEYLFDKH TLGESS 176
    Length:176
    Mass (Da):20,563
    Last modified:November 1, 1991 - v2
    Checksum:iC325E410FB3EC648
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61R → L in CAA35760. (PubMed:2336402)Curated
    Sequence conflicti15 – 151A → I in CAA35760. (PubMed:2336402)Curated
    Sequence conflicti157 – 1582VP → A in CAA35760. (PubMed:2336402)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51395 mRNA. Translation: CAA35760.1.
    M55010 mRNA. Translation: AAA49708.1.
    BC044961 mRNA. Translation: AAH44961.1.
    BC170380 mRNA. Translation: AAI70380.1.
    BC170382 mRNA. Translation: AAI70382.1.
    PIRiA37959. FRXL.
    RefSeqiNP_001079580.1. NM_001086111.1.
    UniGeneiXl.2168.

    Genome annotation databases

    GeneIDi379267.
    KEGGixla:379267.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51395 mRNA. Translation: CAA35760.1 .
    M55010 mRNA. Translation: AAA49708.1 .
    BC044961 mRNA. Translation: AAH44961.1 .
    BC170380 mRNA. Translation: AAI70380.1 .
    BC170382 mRNA. Translation: AAI70382.1 .
    PIRi A37959. FRXL.
    RefSeqi NP_001079580.1. NM_001086111.1.
    UniGenei Xl.2168.

    3D structure databases

    ProteinModelPortali P17663.
    SMRi P17663. Positions 3-172.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 379267.
    KEGGi xla:379267.

    Organism-specific databases

    CTDi 379267.
    Xenbasei XB-GENE-6256345. fth1.

    Phylogenomic databases

    HOVERGENi HBG000410.
    KOi K00522.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Xenopus liver ferritin H subunit: cDNA sequence and mRNA production in the liver following estrogen treatment."
      Holland L.J., Wall A.A., Bhattacharya A.
      Biochemistry 30:1965-1972(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. NIH - Xenopus Gene Collection (XGC) project
      Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo and Tail bud.

    Entry informationi

    Entry nameiFRIHB_XENLA
    AccessioniPrimary (citable) accession number: P17663
    Secondary accession number(s): B7ZS33, Q66LL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 88 of the entry and version 2 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3