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Protein

Ferritin, higher subunit

Gene
N/A
Organism
Lithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Status
Reviewed-Annotation score: Annotation score: 3 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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi24 – 241Iron 1PROSITE-ProRule annotation
Metal bindingi58 – 581IronPROSITE-ProRule annotation
Metal bindingi59 – 591Iron 1PROSITE-ProRule annotation
Metal bindingi59 – 591Iron 2PROSITE-ProRule annotation
Metal bindingi62 – 621Iron 1PROSITE-ProRule annotation
Metal bindingi104 – 1041Iron 2PROSITE-ProRule annotation
Metal bindingi138 – 1381Iron 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. iron ion transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

SABIO-RKP07229.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin, higher subunit (EC:1.16.3.1)
Short name:
Ferritin H
OrganismiLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifieri8400 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi83 – 831K → Q: Improves crystallization.
Mutagenesisi135 – 1351L → P: Reduces initial rate of ferroxidation and accelerates iron release. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 176175Ferritin, higher subunitPRO_0000201072Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 3828Combined sources
Turni41 – 433Combined sources
Helixi46 – 7328Combined sources
Helixi93 – 11321Combined sources
Helixi138 – 15417Combined sources
Turni155 – 1595Combined sources
Helixi161 – 17010Combined sources
Turni171 – 1733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG7X-ray1.85A1-176[»]
ProteinModelPortaliP07229.
SMRiP07229. Positions 3-172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07229.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 156150Ferritin-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.

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.

P07229-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSQVRQNFH RDCEAAINRM VNMELYASYT YLSMAFYFDR DDIALHNVAK
60 70 80 90 100
FFKEQSHEER EHAEKLMKDQ NKRGGRIVLQ DVKKPERDEW GNTLEAMQAA
110 120 130 140 150
LQLEKTVNQA LLDLHKVGSD KVDPHLCDFL ETEYLEEQVK SIKQLGDYIT
160 170
NLKRLGLPQN GMGEYLFDKH TMGESS
Length:176
Mass (Da):20,533
Last modified:January 23, 2007 - v3
Checksum:i81EF7F13362ED5DE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831K → E in AAA49532 (PubMed:3484480).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15655 mRNA. Translation: AAA49523.1.
M12120 mRNA. Translation: AAA49532.1.
PIRiA25627. FRFGL.
A27805.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15655 mRNA. Translation: AAA49523.1.
M12120 mRNA. Translation: AAA49532.1.
PIRiA25627. FRFGL.
A27805.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG7X-ray1.85A1-176[»]
ProteinModelPortaliP07229.
SMRiP07229. Positions 3-172.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000410.

Enzyme and pathway databases

SABIO-RKP07229.

Miscellaneous databases

EvolutionaryTraceiP07229.

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

  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.

Entry informationi

Entry nameiFRI1_LITCT
AccessioniPrimary (citable) accession number: P07229
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 26, 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

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.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.