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P19132 (FRIH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferritin heavy chain

Short name=Ferritin H subunit
EC=1.16.3.1

Cleaved into the following chain:

  1. Ferritin heavy chain, N-terminally processed
Gene names
Name:Fth1
Synonyms:Fth
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length182 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

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.

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 182182Ferritin heavy chain
PRO_0000201053
Initiator methionine11Removed; alternate By similarity
Chain2 – 182181Ferritin heavy chain, N-terminally processed
PRO_0000424476

Regions

Domain11 – 160150Ferritin-like diiron

Sites

Metal binding281Iron 1 By similarity
Metal binding631Iron 1 By similarity
Metal binding631Iron 2 By similarity
Metal binding661Iron 1 By similarity
Metal binding1081Iron 2 By similarity
Metal binding1421Iron 2 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylthreonine; in Ferritin heavy chain, N-terminally processed By similarity

Experimental info

Sequence conflict1021R → E in AAB39890. Ref.2
Sequence conflict1821S → E AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P19132 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F27E105373235B43

FASTA18221,127
        10         20         30         40         50         60 
MTTASPSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSC YFDRDDVALK NFAKYFLHQS 

        70         80         90        100        110        120 
HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWESGLNA MRCALHLEKS VNQSLLELHK 

       130        140        150        160        170        180 
LATDKNDPHL CDFIETHYLN EQVKSIKELG DHVTNLRKMG APESGMAEYL FDKHTLGHGD 


ES 

« Hide

References

[1]"Conservation of ferritin heavy subunit gene structure: implications for the regulation of ferritin gene expression."
Murray M.T., White K., Munro H.N.
Proc. Natl. Acad. Sci. U.S.A. 84:7438-7442(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Wu C.G., Groenink M., Bosma A., Reitsma P.H., van Deventer J.H., Chamuleau R.A.F.M.
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
[3]Lubec G., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 81-87, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
[4]"TSH regulation of ferritin H chain messenger RNA levels in the rat thyroids."
Ursini M.V., de Franciscis V.
Biochem. Biophys. Res. Commun. 150:287-295(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 137-182.
[5]"Conservation in rat liver of light and heavy subunit sequences of mammalian ferritin. Presence of unique octopeptide in the light subunit."
Leibold E.A., Aziz N., Brown A.J.P., Munro H.N.
J. Biol. Chem. 259:4327-4334(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 159-182.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18053, M18051, M18052 Genomic DNA. Translation: AAA41153.1.
U58829 mRNA. Translation: AAB39890.1.
M29330 mRNA. Translation: AAA42300.1.
PIRA39884.
RefSeqNP_036980.1. NM_012848.2.
UniGeneRn.54447.

3D structure databases

ProteinModelPortalP19132.
SMRP19132. Positions 7-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247358. 1 interaction.
IntActP19132. 1 interaction.
MINTMINT-4567905.

PTM databases

PhosphoSiteP19132.

Proteomic databases

PaxDbP19132.
PRIDEP19132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25319.
KEGGrno:25319.
UCSCRGD:2635. rat.

Organism-specific databases

CTD2495.
RGD2635. Fth1.

Phylogenomic databases

eggNOGCOG1528.
HOVERGENHBG000410.
KOK00522.

Gene expression databases

GenevestigatorP19132.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERPTHR11431. PTHR11431. 1 hit.
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio606157.
PROP19132.

Entry information

Entry nameFRIH_RAT
AccessionPrimary (citable) accession number: P19132
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families