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P07229 (FRI1_LITCT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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, higher subunit

Short name=Ferritin H
EC=1.16.3.1
OrganismLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifier8400 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

Protein attributes

Sequence length176 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. Ref.3

Catalytic activity

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

Subunit structure

Oligomer of 24 subunits. The functional molecule is roughly spherical and contains a central cavity into which the polymeric mineral iron core is deposited.

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.

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
   Biological processIron storage
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellular iron ion homeostasis

Inferred from electronic annotation. Source: UniProtKB-KW

iron ion transport

Inferred from electronic annotation. Source: InterPro

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

ferroxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 176175Ferritin, higher subunit
PRO_0000201072

Regions

Domain7 – 156150Ferritin-like diiron

Sites

Metal binding241Iron 1 By similarity
Metal binding581Iron By similarity
Metal binding591Iron 1 By similarity
Metal binding591Iron 2 By similarity
Metal binding621Iron 1 By similarity
Metal binding1041Iron 2 By similarity
Metal binding1381Iron 2 By similarity

Experimental info

Mutagenesis831K → Q: Improves crystallization.
Mutagenesis1351L → P: Reduces initial rate of ferroxidation and accelerates iron release. Ref.3
Sequence conflict831K → E in AAA49532. Ref.2

Secondary structure

............... 176
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07229 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 81EF7F13362ED5DE

FASTA17620,533
        10         20         30         40         50         60 
MDSQVRQNFH RDCEAAINRM VNMELYASYT YLSMAFYFDR DDIALHNVAK FFKEQSHEER 

        70         80         90        100        110        120 
EHAEKLMKDQ NKRGGRIVLQ DVKKPERDEW GNTLEAMQAA LQLEKTVNQA LLDLHKVGSD 

       130        140        150        160        170 
KVDPHLCDFL ETEYLEEQVK SIKQLGDYIT NLKRLGLPQN GMGEYLFDKH TMGESS 

« Hide

References

[1]"Differences in the regulation of messenger RNA for housekeeping and specialized-cell ferritin. A comparison of three distinct ferritin complementary DNAs, the corresponding subunits, and identification of the first processed in amphibia."
Dickey L.F., Sreedharan S., Theil E.C., Didsbury J.R., Wang Y.-H., Kaufman R.E.
J. Biol. Chem. 262:7901-7907(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Multiple red cell ferritin mRNAs, which code for an abundant protein in the embryonic cell type, analyzed by cDNA sequence and by primer extension of the 5'-untranslated regions."
Didsbury J.R., Theil E.C., Kaufman R.E., Dickey L.F.
J. Biol. Chem. 261:949-955(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Erythrocyte.
[3]"Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release?"
Takagi H., Shi D., Ha Y., Allewell N.M., Theil E.C.
J. Biol. Chem. 273:18685-18688(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT GLN-84, FUNCTION, MUTAGENESIS OF LEU-135.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15655 mRNA. Translation: AAA49523.1.
M12120 mRNA. Translation: AAA49532.1.
PIRFRFGL. A25627.
A27805.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG7X-ray1.85A1-176[»]
ProteinModelPortalP07229.
SMRP07229. Positions 3-172.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000410.

Enzyme and pathway databases

SABIO-RKP07229.

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

EvolutionaryTraceP07229.

Entry information

Entry nameFRI1_LITCT
AccessionPrimary (citable) accession number: P07229
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 89 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references