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Protein

Ferritin, chloroplastic

Gene

PFE

Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi99Iron 1PROSITE-ProRule annotation1
Metal bindingi134Iron 1PROSITE-ProRule annotation1
Metal bindingi134Iron 2PROSITE-ProRule annotation1
Metal bindingi137Iron 1PROSITE-ProRule annotation1
Metal bindingi183Iron 2PROSITE-ProRule annotation1
Metal bindingi217Iron 2PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processIron storage
LigandIron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin, chloroplastic (EC:1.16.3.1)
Gene namesi
Name:PFE
OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifieri3885 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeindigoferoid/millettioid cladePhaseoleaePhaseolus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 48ChloroplastAdd BLAST48
ChainiPRO_000000886349 – 254Ferritin, chloroplasticAdd BLAST206

Proteomic databases

ProMEXiP25699

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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP25699
SMRiP25699
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini82 – 235Ferritin-like diironPROSITE-ProRule annotationAdd BLAST154

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 81Extension peptide (EP)Add BLAST33

Sequence similaritiesi

Belongs to the ferritin family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK00522

Family and domain databases

Gene3Di1.20.1260.10, 1 hit
InterProiView protein in InterPro
IPR001519 Ferritin
IPR012347 Ferritin-like
IPR009040 Ferritin-like_diiron
IPR009078 Ferritin-like_SF
IPR014034 Ferritin_CS
IPR008331 Ferritin_DPS_dom
PANTHERiPTHR11431 PTHR11431, 1 hit
PfamiView protein in Pfam
PF00210 Ferritin, 1 hit
SUPFAMiSSF47240 SSF47240, 1 hit
PROSITEiView protein in PROSITE
PS00540 FERRITIN_1, 1 hit
PS00204 FERRITIN_2, 1 hit
PS50905 FERRITIN_LIKE, 1 hit

Sequencei

Sequence statusi: Complete.

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

P25699-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALAPSKVSP FSGFSLSDGV GAVRNPTCSV SLSFLNKKVG SRNLGVSAST
60 70 80 90 100
VPLTGVIFEP FEEVKKEELA VPTAGQVSLA RQYYADECES AINEQINVEY
110 120 130 140 150
NASYVYHSLF AYFDRDNVAL KGFARFFKES SEEEREHAEK LMKYQNTRGG
160 170 180 190 200
RVVLHPIKNV PSEFEHVEKG DALYAMELAL SLEKLVNEKL RSVHSVADRN
210 220 230 240 250
KDPQLADFIE SEFLSEQVEA IKKISEYVAQ LRMVGKGHGV WHFDQSLLHD

GHAA
Length:254
Mass (Da):28,304
Last modified:May 1, 1992 - v1
Checksum:i60B0E974D3F4435F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58274 mRNA Translation: CAA41213.1 Sequence problems.
PIRiS17426 FRFBH
RefSeqiXP_007140214.1, XM_007140152.1

Genome annotation databases

EnsemblPlantsiESW12208; ESW12208; PHAVU_008G093700g
GeneIDi18622338
GrameneiESW12208; ESW12208; PHAVU_008G093700g
KEGGipvu:PHAVU_008G093700g

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58274 mRNA Translation: CAA41213.1 Sequence problems.
PIRiS17426 FRFBH
RefSeqiXP_007140214.1, XM_007140152.1

3D structure databases

ProteinModelPortaliP25699
SMRiP25699
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

ProMEXiP25699

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiESW12208; ESW12208; PHAVU_008G093700g
GeneIDi18622338
GrameneiESW12208; ESW12208; PHAVU_008G093700g
KEGGipvu:PHAVU_008G093700g

Phylogenomic databases

KOiK00522

Family and domain databases

Gene3Di1.20.1260.10, 1 hit
InterProiView protein in InterPro
IPR001519 Ferritin
IPR012347 Ferritin-like
IPR009040 Ferritin-like_diiron
IPR009078 Ferritin-like_SF
IPR014034 Ferritin_CS
IPR008331 Ferritin_DPS_dom
PANTHERiPTHR11431 PTHR11431, 1 hit
PfamiView protein in Pfam
PF00210 Ferritin, 1 hit
SUPFAMiSSF47240 SSF47240, 1 hit
PROSITEiView protein in PROSITE
PS00540 FERRITIN_1, 1 hit
PS00204 FERRITIN_2, 1 hit
PS50905 FERRITIN_LIKE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiFRI_PHAVU
AccessioniPrimary (citable) accession number: P25699
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: September 12, 2018
This is version 89 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health

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