Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ferritin-2, chloroplastic

Gene

FER2

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 bindingi98 – 981Iron 1PROSITE-ProRule annotation
Metal bindingi133 – 1331Iron 1PROSITE-ProRule annotation
Metal bindingi133 – 1331Iron 2PROSITE-ProRule annotation
Metal bindingi136 – 1361Iron 1PROSITE-ProRule annotation
Metal bindingi182 – 1821Iron 2PROSITE-ProRule annotation
Metal bindingi216 – 2161Iron 2PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin-2, chloroplastic (EC:1.16.3.1)
Alternative name(s):
ZmFer2
Gene namesi
Name:FER2
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
ProteomesiUP000007305 Componenti: Unplaced

Organism-specific databases

GrameneiP29390.
MaizeGDBi25278.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343Chloroplast1 PublicationAdd
BLAST
Chaini44 – 252209Ferritin-2, chloroplasticPRO_0000008860Add
BLAST

Proteomic databases

PRIDEiP29390.

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.

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

ProteinModelPortaliP29390.
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
Regioni44 – 8037Extension 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

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.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P29390-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLRVSSSPA AAVANHLSGG AAATTAPARV TAQRSGVSLS AAAAAGKGKE
60 70 80 90 100
VLSGVVFQPF EEIKGELALV PQSPDRSLAR HKFVDDCEAA INEQINVEYN
110 120 130 140 150
ASYAYHSLFA YFDRDNVALK GFAKFFKESS DEEREHAEKL MEYQNKRGGR
160 170 180 190 200
VRLQSIVAPL TEFDHPEKGD ALYAMELTLA LEKLVNEKLH SLHGVATRCN
210 220 230 240 250
DPQLIDFIES EFLEEQGEAI NKVSKYVAQL RRVGNKGHGV WHFDQMLLQE

AA
Length:252
Mass (Da):27,749
Last modified:April 11, 2003 - v2
Checksum:iD181B4A8A86ADED0
GO

Sequence cautioni

The sequence CAA43664.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti217 – 2171G → V in CAA58147 (PubMed:7649160).Curated
Sequence conflicti251 – 2511A → G in CAA58147 (PubMed:7649160).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61392 mRNA. Translation: CAA43664.1. Different initiation.
X83077 Genomic DNA. Translation: CAA58147.1.
PIRiS24057.
UniGeneiZm.72614.

Genome annotation databases

KEGGizma:542392.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61392 mRNA. Translation: CAA43664.1. Different initiation.
X83077 Genomic DNA. Translation: CAA58147.1.
PIRiS24057.
UniGeneiZm.72614.

3D structure databases

ProteinModelPortaliP29390.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP29390.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGizma:542392.

Organism-specific databases

GrameneiP29390.
MaizeGDBi25278.

Phylogenomic databases

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.
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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-72.
    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(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. B73.
    Tissue: Seedling.

Entry informationi

Entry nameiFRI2_MAIZE
AccessioniPrimary (citable) accession number: P29390
Secondary accession number(s): Q43259
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: April 11, 2003
Last modified: July 22, 2015
This is version 97 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.