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Protein

Ferritin heavy chain

Gene

Fth1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. immune response Source: UniProtKB
  2. intracellular sequestering of iron ion Source: MGI
  3. iron ion transport Source: InterPro
  4. negative regulation of cell proliferation Source: UniProtKB
  5. negative regulation of fibroblast proliferation Source: MGI
Complete GO annotation...

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.
REACT_205755. Iron uptake and transport.
REACT_232671. Golgi Associated Vesicle Biogenesis.

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. extracellular vesicular exosome Source: MGI
  4. mitochondrion Source: MGI
  5. nucleus Source: MGI
Complete GO annotation...

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.
GeneTreeiENSGT00760000119129.
HOGENOMiHOG000223383.
HOVERGENiHBG000410.
InParanoidiP09528.
KOiK00522.
OMAiQALHNFA.
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

        10         20         30         40         50
MTTASPSQVR QNYHQDAEAA INRQINLELY ASYVYLSMSC YFDRDDVALK
60 70 80 90 100
NFAKYFLHQS HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWESGLNA
110 120 130 140 150
MECALHLEKS VNQSLLELHK LATDKNDPHL CDFIETYYLS EQVKSIKELG
160 170 180
DHVTNLRKMG APEAGMAEYL FDKHTLGHGD ES
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP09528.
SMRiP09528. Positions 7-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP09528.

2D gel databases

REPRODUCTION-2DPAGEP09528.

Proteomic databases

MaxQBiP09528.
PaxDbiP09528.
PRIDEiP09528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2495.
MGIiMGI:95588. Fth1.

Phylogenomic databases

eggNOGiCOG1528.
GeneTreeiENSGT00760000119129.
HOGENOMiHOG000223383.
HOVERGENiHBG000410.
InParanoidiP09528.
KOiK00522.
OMAiQALHNFA.
OrthoDBiEOG7DRJ49.
PhylomeDBiP09528.
TreeFamiTF313885.

Enzyme and pathway databases

ReactomeiREACT_196581. Scavenging by Class A Receptors.
REACT_205755. Iron uptake and transport.
REACT_232671. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiFth1. mouse.
NextBioi285759.
PROiP09528.
SOURCEiSearch...

Gene expression databases

BgeeiP09528.
CleanExiMM_FTH1.
GenevestigatoriP09528.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 145 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.