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P80145

- FRIH_ANAPL

UniProt

P80145 - FRIH_ANAPL

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Protein

Ferritin heavy chain

Gene
FTH
Organism
Anas platyrhynchos (Domestic duck) (Anas boschas)
Status
Reviewed - 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. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney By similarity.1 Publication
Inhibits translation of various mRNA species in vitro. Associates with a 35S prosome-like particle that contains non-translated mRNAs in a complex with proteins. May be involved in pre-translational regulation of some mRNA.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  1. ferroxidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular iron ion homeostasis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin heavy chain (EC:1.16.3.1)
Short name:
Ferritin H subunit
Alternative name(s):
Prosome-like particle
Short name:
PLP
RNP particle
Gene namesi
Name:FTH
OrganismiAnas platyrhynchos (Domestic duck) (Anas boschas)
Taxonomic identifieri8839 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnas
ProteomesiUP000016666: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 32›32Ferritin heavy chainPRO_0000201056Add
BLAST

Interactioni

Subunit structurei

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 By similarity.

Family & Domainsi

Sequence similaritiesi

Belongs to the ferritin family.

Sequencei

Sequence statusi: Fragments.

P80145-1 [UniParc]FASTAAdd to Basket

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NVNQSLLELH GAPKYGMAEY LFDKHTLGES DN                      32
Length:32
Mass (Da):3,592
Last modified:April 1, 1993 - v1
Checksum:iD7274FD4CB175252
GO

Non-adjacent residues

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi10 – 112

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

PIRiS24135.

Cross-referencesi

Sequence databases

PIRi S24135.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

Publicationsi

  1. "The protein of M(r) 21,000 constituting the prosome-like particle of duck erythroblasts is homologous to apoferritin."
    Coux O., Camoin L., Nothwang H.-G., Bey F., Silva-Pereira I., Keith G., Strosberg A.-D., Scherrer K.
    Eur. J. Biochem. 207:823-832(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION.
    Tissue: Erythroblast.

Entry informationi

Entry nameiFRIH_ANAPL
AccessioniPrimary (citable) accession number: P80145
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: February 19, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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