P29390 (FRI2_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ferritin-2, chloroplastic
EC=1.16.3.1

Alternative name(s):
ZmFer2

Gene names

Name:

FER2

Organism

Zea mays (Maize)

Taxonomic identifier

4577 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.
Subunit structure	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.
Subcellular location	Plastid › chloroplast. Plastid.
Tissue specificity	Ferritins accumulate in seed during maturation. Then, they are degraded during the first days of germination. Present in roots and leaves after iron treatment.
Induction	By iron.
Sequence similarities	Belongs to the ferritin family. Contains 1 ferritin-like diiron domain.
Sequence caution	The sequence CAA43664.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Iron storage
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cellular iron ion homeostasis Inferred from electronic annotation. Source: UniProtKB-KW iron ion transport Inferred from electronic annotation. Source: InterPro
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ferric iron binding Inferred from electronic annotation. Source: InterPro ferroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 43	43	Chloroplast Ref.1
	Chain	44 – 252	209	Ferritin-2, chloroplastic		PRO_0000008860
Regions
	Domain	81 – 234	154	Ferritin-like diiron
	Region	44 – 80	37	Extension peptide (EP)
Sites
	Metal binding	98	1	Iron 1 By similarity
	Metal binding	133	1	Iron 1 By similarity
	Metal binding	133	1	Iron 2 By similarity
	Metal binding	136	1	Iron 1 By similarity
	Metal binding	182	1	Iron 2 By similarity
	Metal binding	216	1	Iron 2 By similarity
Experimental info
	Sequence conflict	217	1	G → V in CAA58147. Ref.2
	Sequence conflict	251	1	A → G in CAA58147. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P29390 [UniParc]. Last modified April 11, 2003. Version 2. Checksum: D181B4A8A86ADED0	FASTA	252	27,749
	10 20 30 40 50 60 MMLRVSSSPA AAVANHLSGG AAATTAPARV TAQRSGVSLS AAAAAGKGKE VLSGVVFQPF 70 80 90 100 110 120 EEIKGELALV PQSPDRSLAR HKFVDDCEAA INEQINVEYN ASYAYHSLFA YFDRDNVALK 130 140 150 160 170 180 GFAKFFKESS DEEREHAEKL MEYQNKRGGR VRLQSIVAPL TEFDHPEKGD ALYAMELTLA 190 200 210 220 230 240 LEKLVNEKLH SLHGVATRCN DPQLIDFIES EFLEEQGEAI NKVSKYVAQL RRVGNKGHGV 250 WHFDQMLLQE AA

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X61392 mRNA. Translation: CAA43664.1. Different initiation. X83077 Genomic DNA. Translation: CAA58147.1.
PIR	S24057.
RefSeq	NP_001105437.1. NM_001111967.1.
UniGene	Zm.72614.
3D structure databases
ProteinModelPortal	P29390.
ModBase	Search...
Proteomic databases
PRIDE	P29390.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	542392.
KEGG	zma:542392.
Organism-specific databases
Gramene	P29390.
MaizeGDB	25278.
Phylogenomic databases
KO	K00522.
Family and domain databases
Gene3D	1.20.1260.10. 1 hit.
InterPro	IPR001519. Ferritin. IPR009040. Ferritin-like_diiron. IPR009078. Ferritin-like_SF. IPR012347. Ferritin-rel. IPR014034. Ferritin_CS. IPR008331. Ferritin_DPS_dom. [Graphical view]
PANTHER	PTHR11431. PTHR11431. 1 hit.
Pfam	PF00210. Ferritin. 1 hit. [Graphical view]
SUPFAM	SSF47240. Ferritin/RR_like. 1 hit.
PROSITE	PS00540. FERRITIN_1. 1 hit. PS00204. FERRITIN_2. False negative. PS50905. FERRITIN_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FRI2_MAIZE

Accession

Primary (citable) accession number: P29390
Secondary accession number(s): Q43259

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	April 11, 2003
Last modified:	May 1, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program