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P19975

- FRI1_PEA

UniProt

P19975 - FRI1_PEA

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Protein
Ferritin-1, chloroplastic
Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed - 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 1 By similarity
Metal bindingi136 – 1361Iron 1 By similarity
Metal bindingi182 – 1821Iron 2 By similarity
Metal bindingi216 – 2161Iron 2 By similarity

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 Publication
Add
BLAST
Chaini48 – 253206Ferritin-1, chloroplastic
PRO_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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 234154Ferritin-like diiron
Add
BLAST

Region

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

Sequence similaritiesi

Belongs to the ferritin family.

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

MALSSSKFSS FSGFSLSPVS GNGVQKPCFC DLRVGEKWGS RKFRVSATTA    50
PLTGVIFEPF EEVKKDYLAV PSVPLVSLAR QNFADECESV INEQINVEYN 100
ASYVYHSLFA YFDRDNVALK GFAKFFKESS EEHREHAEKL MKYQNTRGGR 150
VVLHPIKDVP SEFEHVEKGD ALYAMELALS LEKLTNEKLL NVHSVAERNN 200
DLEMTHFIEG EYLAEQVEAI KKISEYVAQL RRVGKGHGVW HFDQRLLHGV 250
HGA 253
Length:253
Mass (Da):28,619
Last modified:October 1, 1993 - v2
Checksum:i9C754BCBDBC926F7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461S → C in CAA51786. 1 Publication
Sequence conflicti101 – 1011A → V in CAA51786. 1 Publication
Sequence conflicti108 – 1081L → M in CAA51786. 1 Publication
Sequence conflicti133 – 1331H → E in CAA51786. 1 Publication
Sequence conflicti173 – 1731Y → H in CAA51786. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64417 mRNA. Translation: CAA45763.1.
X73369 mRNA. Translation: CAA51786.1.
PIRiS27358.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64417 mRNA. Translation: CAA45763.1 .
X73369 mRNA. Translation: CAA51786.1 .
PIRi S27358.

3D structure databases

ProteinModelPortali P19975.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P19975.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.20.1260.10. 1 hit.
InterProi IPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view ]
PANTHERi PTHR11431. PTHR11431. 1 hit.
Pfami PF00210. Ferritin. 1 hit.
[Graphical view ]
SUPFAMi SSF47240. SSF47240. 1 hit.
PROSITEi PS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: February 19, 2014
This is version 86 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

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