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Protein

Ferritin, higher subunit

Gene
N/A
Organism
Lithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Status
Reviewed-Annotation score: Annotation score: 4 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)DescriptionActionsGraphical viewLength
Metal bindingi24Iron 1PROSITE-ProRule annotation1
Metal bindingi58IronPROSITE-ProRule annotation1
Metal bindingi59Iron 1PROSITE-ProRule annotation1
Metal bindingi59Iron 2PROSITE-ProRule annotation1
Metal bindingi62Iron 1PROSITE-ProRule annotation1
Metal bindingi104Iron 2PROSITE-ProRule annotation1
Metal bindingi138Iron 2PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi83K → Q: Improves crystallization. 1
Mutagenesisi135L → P: Reduces initial rate of ferroxidation and accelerates iron release. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002010722 – 176Ferritin, higher subunitAdd BLAST175

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

1176
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 38Combined sources28
Turni41 – 43Combined sources3
Helixi46 – 73Combined sources28
Helixi93 – 113Combined sources21
Helixi138 – 154Combined sources17
Turni155 – 159Combined sources5
Helixi161 – 170Combined sources10
Turni171 – 173Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP07229.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 156Ferritin-like diironPROSITE-ProRule annotationAdd BLAST150

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)DescriptionActionsGraphical viewLength
Sequence conflicti83K → E in AAA49532 (PubMed:3484480).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BG7X-ray1.85A1-176[»]
ProteinModelPortaliP07229.
SMRiP07229.
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...

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 2, 2016
This is version 96 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

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 one 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.