Skip Header

Contribute Send feedback
Read comments (?) or add your own

P85837 (FRIH_TRENE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 20. 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
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 subunit
Short name=Ferritin H
EC=1.16.3.1
OrganismTrematomus newnesi (Dusky notothen)
Taxonomic identifier35730 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Perciformes › Notothenioidei › Nototheniidae › Trematomus

Protein attributes

Sequence length174 AA.
Sequence statusComplete.
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. UniProtKB P02794

Catalytic activity

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O. Ref.1

Subunit structure

In liver, forms a heteropolymer consisting of middle and heavy subunits. 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. Ref.1

Tissue specificity

Liver (at protein level). Ref.1

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
   Biological processIron storage
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 174174Ferritin, heavy subunit
PRO_0000352781

Regions

Domain7 – 156150Ferritin-like diiron

Sites

Metal binding241Iron 1 By similarity UniProtKB P02794
Metal binding591Iron 1 By similarity UniProtKB P02794
Metal binding591Iron 2 By similarity UniProtKB P02794
Metal binding621Iron 1 By similarity UniProtKB P02794
Metal binding1041Iron 2 By similarity UniProtKB P02794
Metal binding1381Iron 2 By similarity UniProtKB P02794

Sequences

Sequence LengthMass (Da)Tools
P85837 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 2A0C1B99353515E6

FASTA17420,379
        10         20         30         40         50         60 
MESQVRQNFH KDCEAAINRQ INLELYASYS YLSMAYYFDR DDVALPGFAH FFKHQSEEER 

        70         80         90        100        110        120 
EHAEKLMKQQ NQRGGRIFLQ DVKKPDRDEW GSGLDALECA LQLEKNVNQS LLDLHKVCSE 

       130        140        150        160        170 
HNDPHMCDFL ETHYLDEQVK SIKELGDWVT NLRRLGAPQN GMAEYLFDKH TLGK

« Hide

References

[1]"The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi."
Giorgi A., Mignogna G., Bellapadrona G., Gattoni M., Chiaraluce R., Consalvi V., Chiancone E., Stefanini S.
Arch. Biochem. Biophys. 478:69-74(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY.
Tissue: Liver.

Cross-references

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000410.

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. Ferritin/RR_like. 1 hit.
PROSITEPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRIH_TRENE
AccessionPrimary (citable) accession number: P85837
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: October 14, 2008
Last modified: May 1, 2013
This is version 20 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents