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Protein

Ferritin-1, chloroplastic

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi98 – 981Iron 1PROSITE-ProRule annotation
Metal bindingi136 – 1361Iron 1PROSITE-ProRule annotation
Metal bindingi182 – 1821Iron 2PROSITE-ProRule annotation
Metal bindingi216 – 2161Iron 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin-1, chloroplastic (EC:1.16.3.1)
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4747Chloroplast1 PublicationAdd
BLAST
Chaini48 – 253206Ferritin-1, chloroplasticPRO_0000008862Add
BLAST

Proteomic databases

PRIDEiP19975.

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.

Structurei

3D structure databases

ProteinModelPortaliP19975.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 234154Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 8033Extension peptide (EP)Add
BLAST

Sequence similaritiesi

Belongs to the ferritin family.Curated
Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19975-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSSSKFSS FSGFSLSPVS GNGVQKPCFC DLRVGEKWGS RKFRVSATTA
60 70 80 90 100
PLTGVIFEPF EEVKKDYLAV PSVPLVSLAR QNFADECESV INEQINVEYN
110 120 130 140 150
ASYVYHSLFA YFDRDNVALK GFAKFFKESS EEHREHAEKL MKYQNTRGGR
160 170 180 190 200
VVLHPIKDVP SEFEHVEKGD ALYAMELALS LEKLTNEKLL NVHSVAERNN
210 220 230 240 250
DLEMTHFIEG EYLAEQVEAI KKISEYVAQL RRVGKGHGVW HFDQRLLHGV

HGA
Length:253
Mass (Da):28,619
Last modified:October 1, 1993 - v2
Checksum:i9C754BCBDBC926F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461S → C in CAA51786 (PubMed:7826338).Curated
Sequence conflicti101 – 1011A → V in CAA51786 (PubMed:7826338).Curated
Sequence conflicti108 – 1081L → M in CAA51786 (PubMed:7826338).Curated
Sequence conflicti133 – 1331H → E in CAA51786 (PubMed:7826338).Curated
Sequence conflicti173 – 1731Y → H in CAA51786 (PubMed:7826338).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64417 mRNA. Translation: CAA45763.1.
X73369 mRNA. Translation: CAA51786.1.
PIRiS27358.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64417 mRNA. Translation: CAA45763.1.
X73369 mRNA. Translation: CAA51786.1.
PIRiS27358.

3D structure databases

ProteinModelPortaliP19975.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP19975.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiFRI1_PEA
AccessioniPrimary (citable) accession number: P19975
Secondary accession number(s): Q43080
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1993
Last modified: January 7, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.