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P09528

- FRIH_MOUSE

UniProt

P09528 - FRIH_MOUSE

Protein

Ferritin heavy chain

Gene

Fth1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi28 – 281Iron 1PROSITE-ProRule annotation
    Metal bindingi63 – 631Iron 1PROSITE-ProRule annotation
    Metal bindingi63 – 631Iron 2PROSITE-ProRule annotation
    Metal bindingi66 – 661Iron 1PROSITE-ProRule annotation
    Metal bindingi108 – 1081Iron 2PROSITE-ProRule annotation
    Metal bindingi142 – 1421Iron 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. immune response Source: UniProtKB
    3. iron ion transport Source: InterPro
    4. negative regulation of cell proliferation Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Iron storage

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196581. Scavenging by Class A Receptors.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:95588. Fth1.

    Subcellular locationi

    GO - Cellular componenti

    1. endocytic vesicle lumen Source: Reactome
    2. extracellular region Source: Reactome
    3. mitochondrion Source: MGI

    Pathology & Biotechi

    Disruption phenotypei

    Homozygous mutant embryos die in utero between 3.5 and 9.5 dpc (PubMed:10652280). Heterozygous animals are healthy and fertile and do not present any apparent abnormalities. They show slightly elevated tissue light chain ferritin content and 7- to 10-fold more light chain ferritin in the serum than normal mice, but their serum iron remains unchanged.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 182182Ferritin heavy chainPRO_0000201049Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 182181Ferritin heavy chain, N-terminally processedPRO_0000424473Add
    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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP09528.
    PaxDbiP09528.
    PRIDEiP09528.

    2D gel databases

    REPRODUCTION-2DPAGEP09528.

    PTM databases

    PhosphoSiteiP09528.

    Expressioni

    Developmental stagei

    At 9.5 dpc, detected at low levels in the developing heart and central nervous system. At later stages of development, widely expressed, predominantly in the heart and brown fat tissue.1 Publication

    Gene expression databases

    BgeeiP09528.
    CleanExiMM_FTH1.
    GenevestigatoriP09528.

    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.

    Protein-protein interaction databases

    IntActiP09528. 4 interactions.
    MINTiMINT-1856685.
    STRINGi10090.ENSMUSP00000025563.

    Structurei

    3D structure databases

    ProteinModelPortaliP09528.
    SMRiP09528. Positions 7-177.
    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

    eggNOGiCOG1528.
    GeneTreeiENSGT00700000104283.
    HOGENOMiHOG000223383.
    HOVERGENiHBG000410.
    InParanoidiP09528.
    KOiK00522.
    OMAiASENNDP.
    OrthoDBiEOG7DRJ49.
    PhylomeDBiP09528.
    TreeFamiTF313885.

    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.

    P09528-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTASPSQVR QNYHQDAEAA INRQINLELY ASYVYLSMSC YFDRDDVALK    50
    NFAKYFLHQS HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWESGLNA 100
    MECALHLEKS VNQSLLELHK LATDKNDPHL CDFIETYYLS EQVKSIKELG 150
    DHVTNLRKMG APEAGMAEYL FDKHTLGHGD ES 182
    Length:182
    Mass (Da):21,067
    Last modified:January 23, 2007 - v2
    Checksum:i129A8887A2BC650B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171A → S in AAA37612. (PubMed:2708374)Curated
    Sequence conflicti137 – 1371Y → H in AAA37612. (PubMed:2708374)Curated
    Sequence conflicti140 – 1401S → N in AAA37612. (PubMed:2708374)Curated
    Sequence conflicti164 – 1641A → S in AAA37612. (PubMed:2708374)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52561 Genomic DNA. Translation: CAA36795.1.
    X12812 mRNA. Translation: CAA31300.1.
    J03941 mRNA. Translation: AAA37611.1.
    M60170 Genomic DNA. Translation: AAA37613.1.
    M24509 mRNA. Translation: AAA37612.1.
    AK027998 mRNA. Translation: BAC25694.1.
    AK139622 mRNA. Translation: BAE24084.1.
    AK147082 mRNA. Translation: BAE27662.1.
    AK150262 mRNA. Translation: BAE29419.1.
    AK150508 mRNA. Translation: BAE29621.1.
    AK150628 mRNA. Translation: BAE29718.1.
    AK150679 mRNA. Translation: BAE29759.1.
    AK150693 mRNA. Translation: BAE29772.1.
    AK151192 mRNA. Translation: BAE30189.1.
    AK151241 mRNA. Translation: BAE30233.1.
    AK151399 mRNA. Translation: BAE30367.1.
    AK151609 mRNA. Translation: BAE30548.1.
    AK151675 mRNA. Translation: BAE30600.1.
    AK152071 mRNA. Translation: BAE30924.1.
    AK152542 mRNA. Translation: BAE31297.1.
    AK152702 mRNA. Translation: BAE31431.1.
    AK153017 mRNA. Translation: BAE31651.1.
    AK153195 mRNA. Translation: BAE31795.1.
    AK153199 mRNA. Translation: BAE31799.1.
    AK159243 mRNA. Translation: BAE34925.1.
    AK168601 mRNA. Translation: BAE40468.1.
    AK169004 mRNA. Translation: BAE40803.1.
    BC012314 mRNA. Translation: AAH12314.1.
    CCDSiCCDS29567.1.
    PIRiS06070.
    RefSeqiNP_034369.1. NM_010239.2.
    UniGeneiMm.1776.

    Genome annotation databases

    EnsembliENSMUST00000025563; ENSMUSP00000025563; ENSMUSG00000024661.
    GeneIDi14319.
    KEGGimmu:14319.
    UCSCiuc008got.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52561 Genomic DNA. Translation: CAA36795.1 .
    X12812 mRNA. Translation: CAA31300.1 .
    J03941 mRNA. Translation: AAA37611.1 .
    M60170 Genomic DNA. Translation: AAA37613.1 .
    M24509 mRNA. Translation: AAA37612.1 .
    AK027998 mRNA. Translation: BAC25694.1 .
    AK139622 mRNA. Translation: BAE24084.1 .
    AK147082 mRNA. Translation: BAE27662.1 .
    AK150262 mRNA. Translation: BAE29419.1 .
    AK150508 mRNA. Translation: BAE29621.1 .
    AK150628 mRNA. Translation: BAE29718.1 .
    AK150679 mRNA. Translation: BAE29759.1 .
    AK150693 mRNA. Translation: BAE29772.1 .
    AK151192 mRNA. Translation: BAE30189.1 .
    AK151241 mRNA. Translation: BAE30233.1 .
    AK151399 mRNA. Translation: BAE30367.1 .
    AK151609 mRNA. Translation: BAE30548.1 .
    AK151675 mRNA. Translation: BAE30600.1 .
    AK152071 mRNA. Translation: BAE30924.1 .
    AK152542 mRNA. Translation: BAE31297.1 .
    AK152702 mRNA. Translation: BAE31431.1 .
    AK153017 mRNA. Translation: BAE31651.1 .
    AK153195 mRNA. Translation: BAE31795.1 .
    AK153199 mRNA. Translation: BAE31799.1 .
    AK159243 mRNA. Translation: BAE34925.1 .
    AK168601 mRNA. Translation: BAE40468.1 .
    AK169004 mRNA. Translation: BAE40803.1 .
    BC012314 mRNA. Translation: AAH12314.1 .
    CCDSi CCDS29567.1.
    PIRi S06070.
    RefSeqi NP_034369.1. NM_010239.2.
    UniGenei Mm.1776.

    3D structure databases

    ProteinModelPortali P09528.
    SMRi P09528. Positions 7-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P09528. 4 interactions.
    MINTi MINT-1856685.
    STRINGi 10090.ENSMUSP00000025563.

    PTM databases

    PhosphoSitei P09528.

    2D gel databases

    REPRODUCTION-2DPAGE P09528.

    Proteomic databases

    MaxQBi P09528.
    PaxDbi P09528.
    PRIDEi P09528.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025563 ; ENSMUSP00000025563 ; ENSMUSG00000024661 .
    GeneIDi 14319.
    KEGGi mmu:14319.
    UCSCi uc008got.1. mouse.

    Organism-specific databases

    CTDi 2495.
    MGIi MGI:95588. Fth1.

    Phylogenomic databases

    eggNOGi COG1528.
    GeneTreei ENSGT00700000104283.
    HOGENOMi HOG000223383.
    HOVERGENi HBG000410.
    InParanoidi P09528.
    KOi K00522.
    OMAi ASENNDP.
    OrthoDBi EOG7DRJ49.
    PhylomeDBi P09528.
    TreeFami TF313885.

    Enzyme and pathway databases

    Reactomei REACT_196581. Scavenging by Class A Receptors.

    Miscellaneous databases

    ChiTaRSi FTH1. mouse.
    NextBioi 285759.
    PROi P09528.
    SOURCEi Search...

    Gene expression databases

    Bgeei P09528.
    CleanExi MM_FTH1.
    Genevestigatori P09528.

    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. "Nucleotide sequence of the mouse ferritin H chain gene."
      Yachaou A., Renaudie F., Grandchamp B., Beaumont C.
      Nucleic Acids Res. 17:8005-8005(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: BALB/c.
    2. "Nucleotide sequence of cDNA encoding the heavy subunit of mouse macrophage ferritin."
      Miyazaki Y., Setoguchi M., Higuchi Y., Yoshida S., Akizuki S., Yamamoto S.
      Nucleic Acids Res. 16:10373-10373(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ICR.
      Tissue: Macrophage.
    3. "The molecular cloning and characterization of murine ferritin heavy chain, a tumor necrosis factor-inducible gene."
      Torti S.V., Kwak E.L., Miller S.C., Miller L.L., Ringold G.M., Myambo K.B., Young A.P., Torti F.M.
      J. Biol. Chem. 263:12638-12644(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Murine ferritin heavy chain: isolation and characterization of a functional gene."
      Kwak E.L., Torti S.V., Torti F.M.
      Gene 94:255-261(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    5. "Transcriptional regulation of ferritin H and L subunits in adult erythroid and liver cells from the mouse. Unambiguous identification of mouse ferritin subunits and in vitro formation of the ferritin shells."
      Beaumont C., Dugast I., Renaudie F., Souroujon M., Grandchamp B.
      J. Biol. Chem. 264:7498-7504(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Amnion, Heart and Kidney.
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Mammary tumor.
    8. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 11-23 AND 55-64, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    9. Cited for: DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
    10. "H ferritin knockout mice: a model of hyperferritinemia in the absence of iron overload."
      Ferreira C., Santambrogio P., Martin M.E., Andrieu V., Feldmann G., Henin D., Beaumont C.
      Blood 98:525-532(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    11. Cited for: FUNCTION.

    Entry informationi

    Entry nameiFRIH_MOUSE
    AccessioniPrimary (citable) accession number: P09528
    Secondary accession number(s): Q3UI44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 141 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3