P80145 (FRIH_ANAPL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ferritin heavy chain
Short name=Ferritin H subunit
EC=1.16.3.1

Alternative name(s):
Prosome-like particle
Short name=PLP
RNP particle

Gene names

Name:

FTH

Organism

Anas platyrhynchos (Domestic duck) (Anas boschas)

Taxonomic identifier

8839 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Anas

Protein attributes

Sequence length	32 AA.
Sequence status	Fragments.
Protein existence	Evidence 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. Ref.1 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. Ref.1
Catalytic activity	4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.
Subunit structure	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.
Sequence similarities	Belongs to the ferritin family.

Ontologies

Keywords
Biological process	Iron storage
Ligand	Iron Metal-binding RNA-binding
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cellular iron ion homeostasis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW ferroxidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 32	›32	Ferritin heavy chain		PRO_0000201056
Experimental info
	Non-adjacent residues	10 – 11	2
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P80145 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: D7274FD4CB175252	FASTA	32	3,592
	10 20 30 NVNQSLLELH GAPKYGMAEY LFDKHTLGES DN

References

[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.

Cross-references

Sequence databases
PIR	S24135.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
PROSITE	PS00540. FERRITIN_1. Partial match. PS00204. FERRITIN_2. Partial match. PS50905. FERRITIN_LIKE. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FRIH_ANAPL

Accession

Primary (citable) accession number: P80145

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program