P07229 (FRI1_LITCT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Ferritin, higher subunit Short name=Ferritin H EC=1.16.3.1
Organism	Lithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifier	8400 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Rana › Aquarana

Protein attributes

Sequence length	176 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Ref.3
Catalytic activity	4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.
Subunit structure	Oligomer of 24 subunits. The functional molecule is roughly spherical and contains a central cavity into which the polymeric mineral iron core is deposited.
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.
Sequence similarities	Belongs to the ferritin family. Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
Biological process	Iron storage
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	cellular iron ion homeostasis Inferred from electronic annotation. Source: UniProtKB-KW iron ion transport Inferred from electronic annotation. Source: InterPro
Molecular_function	ferric iron binding Inferred from electronic annotation. Source: InterPro ferroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 176

175

Ferritin, higher subunit

PRO_0000201072

Regions

Domain

7 – 156

150

Ferritin-like diiron

Sites

Metal binding

24

1

Iron 1 By similarity

Metal binding

58

1

Iron By similarity

Metal binding

59

1

Iron 1 By similarity

Metal binding

59

1

Iron 2 By similarity

Metal binding

62

1

Iron 1 By similarity

Metal binding

104

1

Iron 2 By similarity

Metal binding

138

1

Iron 2 By similarity

Experimental info

Mutagenesis

83

1

K → Q: Improves crystallization.

Mutagenesis

135

1

L → P: Reduces initial rate of ferroxidation and accelerates iron release. Ref.3

Sequence conflict

83

1

K → E in AAA49532. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

176

Helix Strand Turn

Details...

Helix

11 – 38

28

Turn

41 – 43

3

Helix

46 – 73

28

Helix

93 – 113

21

Helix

138 – 154

17

Turn

155 – 159

5

Helix

161 – 170

10

Turn

171 – 173

3

Sequences

	Sequence		Length	Mass (Da)
	P07229 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 81EF7F13362ED5DE	FASTA	176	20,533
	10 20 30 40 50 60 MDSQVRQNFH RDCEAAINRM VNMELYASYT YLSMAFYFDR DDIALHNVAK FFKEQSHEER 70 80 90 100 110 120 EHAEKLMKDQ NKRGGRIVLQ DVKKPERDEW GNTLEAMQAA LQLEKTVNQA LLDLHKVGSD 130 140 150 160 170 KVDPHLCDFL ETEYLEEQVK SIKQLGDYIT NLKRLGLPQN GMGEYLFDKH TMGESS

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M15655 mRNA. Translation: AAA49523.1.
M12120 mRNA. Translation: AAA49532.1.

PIR

FRFGL. A25627.
A27805.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BG7	X-ray	1.85	A	1-176	[»]

ProteinModelPortal

P07229.

SMR

P07229. Positions 3-172.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG000410.

Enzyme and pathway databases

SABIO-RK

P07229.

Family and domain databases

Gene3D

1.20.1260.10. 1 hit.

InterPro

IPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]

PANTHER

PTHR11431. PTHR11431. 1 hit.

Pfam

PF00210. Ferritin. 1 hit.
[Graphical view]

SUPFAM

SSF47240. Ferritin/RR_like. 1 hit.

PROSITE

PS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07229.

Entry information

Entry name

FRI1_LITCT

Accession

Primary (citable) accession number: P07229

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program