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Protein

Ferritin-1, chloroplastic

Gene

FER1

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 5 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 bindingi101 – 1011Iron 1PROSITE-ProRule annotation
Metal bindingi136 – 1361Iron 1PROSITE-ProRule annotation
Metal bindingi136 – 1361Iron 2PROSITE-ProRule annotation
Metal bindingi139 – 1391Iron 1PROSITE-ProRule annotation
Metal bindingi185 – 1851Iron 2PROSITE-ProRule annotation
Metal bindingi219 – 2191Iron 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. ferric iron binding Source: EnsemblPlants/Gramene
  2. ferroxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular iron ion homeostasis Source: UniProtKB-KW
  2. flower development Source: EnsemblPlants/Gramene
  3. iron ion transport Source: EnsemblPlants/Gramene
  4. leaf development Source: EnsemblPlants/Gramene
  5. photosynthesis Source: EnsemblPlants/Gramene
  6. response to reactive oxygen species Source: EnsemblPlants/Gramene
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)
Alternative name(s):
ZmFer1
Gene namesi
Name:FER1
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
ProteomesiUP000007305 Componenti: Unplaced

Organism-specific databases

GrameneiP29036.
MaizeGDBi25278.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast stroma Source: EnsemblPlants/Gramene
  2. chloroplast thylakoid membrane Source: EnsemblPlants/Gramene
  3. mitochondrion Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646Chloroplast1 PublicationAdd
BLAST
Chaini47 – 254208Ferritin-1, chloroplasticPRO_0000008859Add
BLAST

Proteomic databases

PRIDEiP29036.

Expressioni

Tissue specificityi

Ferritins accumulate in seed during maturation. Then, they are degraded during the first days of germination. Present in roots and leaves after iron treatment.

Inductioni

By iron.

Gene expression databases

ExpressionAtlasiP29036. baseline.

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

ProteinModelPortaliP29036.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 237154Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 8337Extension 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

Phylogenomic databases

HOGENOMiHOG000223383.
KOiK00522.

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.

P29036-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLRVSPSPA AAVPTQLSGA PATPAPVVRV AAPRGVASPS AGAACRAAGK
60 70 80 90 100
GKEVLSGVVF QPFEEIKGEL ALVPQSPDKS LARHKFVDDC EAALNEQINV
110 120 130 140 150
EYNASYAYHS LFAYFDRDNV ALKGFAKFFK ESSDEEREHA EKLMEYQNKR
160 170 180 190 200
GGRVRLQSIV TPLTEFDHPE KGDALYAMEL ALALEKLVNE KLHNLHGVAT
210 220 230 240 250
RCNDPQLTDF IESEFLEEQG EAINKISKYV AQLRRVGKGH GVWHFDQMLL

EEEA
Length:254
Mass (Da):28,025
Last modified:April 10, 2003 - v2
Checksum:i7B74EBB843DBA28D
GO

Sequence cautioni

The sequence CAA43663.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321Missing in CAA58146 (PubMed:7649160).Curated
Sequence conflicti214 – 2141E → D in CAA58146 (PubMed:7649160).Curated
Sequence conflicti220 – 2201G → V in CAA58146 (PubMed:7649160).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61391 mRNA. Translation: CAA43663.1. Different initiation.
X83076 Genomic DNA. Translation: CAA58146.1.
PIRiS22498.
RefSeqiNP_001105563.1. NM_001112093.1.
UniGeneiZm.99.

Genome annotation databases

GeneIDi542553.
KEGGizma:542553.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61391 mRNA. Translation: CAA43663.1. Different initiation.
X83076 Genomic DNA. Translation: CAA58146.1.
PIRiS22498.
RefSeqiNP_001105563.1. NM_001112093.1.
UniGeneiZm.99.

3D structure databases

ProteinModelPortaliP29036.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP29036.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi542553.
KEGGizma:542553.

Organism-specific databases

GrameneiP29036.
MaizeGDBi25278.

Phylogenomic databases

HOGENOMiHOG000223383.
KOiK00522.

Gene expression databases

ExpressionAtlasiP29036. baseline.

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. "Iron induces ferritin synthesis in maize plantlets."
    Lobreaux S., Massenet O., Briat J.-F.
    Plant Mol. Biol. 19:563-575(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-75.
    Strain: cv. Missouri 17.
    Tissue: Root and Seed.
  2. "Structure and differential expression of two maize ferritin genes in response to iron and abscisic acid."
    Fobis-Loisy I., Loridon K., Lobreaux S., Lebrun M., Briat J.-F.
    Eur. J. Biochem. 231:609-619(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Wisconsin 22.
    Tissue: Seedling.

Entry informationi

Entry nameiFRI1_MAIZE
AccessioniPrimary (citable) accession number: P29036
Secondary accession number(s): Q43258
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 1992
Last sequence update: April 10, 2003
Last modified: February 3, 2015
This is version 100 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

Complete proteome, Direct protein sequencing, Reference proteome

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.