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P19975 (FRI1_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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

Names and origin

Protein namesRecommended name:
Ferritin-1, chloroplastic

EC=1.16.3.1
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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.

Subcellular location

Plastidchloroplast. Plastid.

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
   Biological processIron storage
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   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

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

ferroxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4747Chloroplast Ref.3
Chain48 – 253206Ferritin-1, chloroplastic
PRO_0000008862

Regions

Domain81 – 234154Ferritin-like diiron
Region48 – 8033Extension peptide (EP)

Sites

Metal binding981Iron 1 By similarity
Metal binding1361Iron 1 By similarity
Metal binding1821Iron 2 By similarity
Metal binding2161Iron 2 By similarity

Experimental info

Sequence conflict461S → C in CAA51786. Ref.2
Sequence conflict1011A → V in CAA51786. Ref.2
Sequence conflict1081L → M in CAA51786. Ref.2
Sequence conflict1331H → E in CAA51786. Ref.2
Sequence conflict1731Y → H in CAA51786. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P19975 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 9C754BCBDBC926F7

FASTA25328,619
        10         20         30         40         50         60 
MALSSSKFSS FSGFSLSPVS GNGVQKPCFC DLRVGEKWGS RKFRVSATTA PLTGVIFEPF 

        70         80         90        100        110        120 
EEVKKDYLAV PSVPLVSLAR QNFADECESV INEQINVEYN ASYVYHSLFA YFDRDNVALK 

       130        140        150        160        170        180 
GFAKFFKESS EEHREHAEKL MKYQNTRGGR VVLHPIKDVP SEFEHVEKGD ALYAMELALS 

       190        200        210        220        230        240 
LEKLTNEKLL NVHSVAERNN DLEMTHFIEG EYLAEQVEAI KKISEYVAQL RRVGKGHGVW 

       250 
HFDQRLLHGV HGA 

« Hide

References

[1]"Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin."
Lobreaux S., Yewdall S.J., Briat J.-F., Harrison P.M.
Biochem. J. 288:931-939(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Purification and characterization of recombinant pea-seed ferritins expressed in Escherichia coli: influence of N-terminus deletions on protein solubility and core formation in vitro."
Van Wuytswinkel O., Savino G., Briat J.-F.
Biochem. J. 305:253-261(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Mechanism of the transition from plant ferritin to phytosiderin."
Laulhere J.-P., Laboure A.M., Briat J.-F.
J. Biol. Chem. 264:3629-3635(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 48-82.
Tissue: Seed.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64417 mRNA. Translation: CAA45763.1.
X73369 mRNA. Translation: CAA51786.1.
PIRS27358.

3D structure databases

ProteinModelPortalP19975.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP19975.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. SSF47240. 1 hit.
PROSITEPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRI1_PEA
AccessionPrimary (citable) accession number: P19975
Secondary accession number(s): Q43080
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1993
Last modified: February 19, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families