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P19130

- FRIH_PIG

UniProt

P19130 - FRIH_PIG

Protein

Ferritin heavy chain

Gene

FTH1

Organism
Sus scrofa (Pig)
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. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney By similarity.By similarity

    Catalytic activityi

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

    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 (EC:1.16.3.1)
    Short name:
    Ferritin H subunit
    Cleaved into the following chain:
    Gene namesi
    Name:FTH1
    Synonyms:FTH
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 181181Ferritin heavy chainPRO_0000201051Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 181180Ferritin heavy chain, N-terminally processedPRO_0000424475Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei2 – 21N-acetylthreonine; in Ferritin heavy chain, N-terminally processedBy similarity
    Modified residuei179 – 1791PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Interactioni

    Subunit structurei

    Oligomer of 24 subunits. There are two types of subunits: L (light) chain and H (heavy) chain. The major chain can be light or heavy, depending on the species and tissue type. 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 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP19130.
    SMRiP19130. Positions 6-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 160150Ferritin-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.
    PROSITEiPS00204. 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.

    P19130-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTSCSSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK    50
    NFAKYFLHQS HGGRGHAEKL MKLQTQRGAR IFLQDIMKPE RDDWENGLTA 100
    MEFALHVVKN VYQSLLELHK LATDKNDPHL CDFIETHYLH EQVKAIKELG 150
    DHITNLHRMG APEYGMAEYL FDKHTLGSSE S 181
    Length:181
    Mass (Da):21,045
    Last modified:January 23, 2007 - v3
    Checksum:i8E6D9710CC57F757
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1031F → C AA sequence (PubMed:3688879)Curated
    Sequence conflicti107 – 1082VV → LE AA sequence (PubMed:3688879)Curated
    Sequence conflicti112 – 1121Y → N AA sequence (PubMed:3688879)Curated
    Sequence conflicti140 – 1401H → D AA sequence (PubMed:3688879)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti111 – 1111V → M.
    Natural varianti116 – 1161L → H.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D15071 mRNA. Translation: BAA03666.1.
    PIRiS06279.
    RefSeqiNP_999140.1. NM_213975.1.
    UniGeneiSsc.23940.
    Ssc.42834.
    Ssc.61.

    Genome annotation databases

    GeneIDi397030.
    KEGGissc:397030.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D15071 mRNA. Translation: BAA03666.1 .
    PIRi S06279.
    RefSeqi NP_999140.1. NM_213975.1.
    UniGenei Ssc.23940.
    Ssc.42834.
    Ssc.61.

    3D structure databases

    ProteinModelPortali P19130.
    SMRi P19130. Positions 6-177.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397030.
    KEGGi ssc:397030.

    Organism-specific databases

    CTDi 2495.

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

    Publicationsi

    1. Hamasima N., Suzuki H., Fujii H., Ito T., Murakami Y., Yamada R., Yazawa T., Yasue H.
      Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Isolation and partial amino acid sequence of three subunit species of porcine spleen ferritin: evidence of multiple H subunits."
      Collawn J.F. Jr., Gowan L.K., Crow H., Schwabe C., Fish W.W.
      Arch. Biochem. Biophys. 259:105-113(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 102-181.
      Tissue: Spleen.

    Entry informationi

    Entry nameiFRIH_PIG
    AccessioniPrimary (citable) accession number: P19130
    Secondary accession number(s): P19131
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 91 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3