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O65100

- FRI3_VIGUN

UniProt

O65100 - FRI3_VIGUN

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Protein

Ferritin-3, chloroplastic

Gene
N/A
Organism
Vigna unguiculata (Cowpea)
Status
Reviewed - Annotation score: 3 out of 5- 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi105 – 1051Iron 1PROSITE-ProRule annotation
Metal bindingi140 – 1401Iron 1PROSITE-ProRule annotation
Metal bindingi140 – 1401Iron 2PROSITE-ProRule annotation
Metal bindingi143 – 1431Iron 1PROSITE-ProRule annotation
Metal bindingi189 – 1891Iron 2PROSITE-ProRule annotation
Metal bindingi223 – 2231Iron 2PROSITE-ProRule annotation

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-3, chloroplastic (EC:1.16.3.1)
OrganismiVigna unguiculata (Cowpea)
Taxonomic identifieri3917 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

Subcellular locationi

Plastidchloroplast By similarity

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5454ChloroplastSequence AnalysisAdd
BLAST
Chaini55 – 256202Ferritin-3, chloroplasticPRO_0000008871Add
BLAST

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

ProteinModelPortaliO65100.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 241154Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 8733Extension 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

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.

O65100-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALSCSKVLT FSLSSVVGGD DAKKKLSLCS SSSLSASVNG GGSRNMRVCA
60 70 80 90 100
AASNAPAPLT GVIFEPFQEL KKDYLAVPIA PNVSLSRQNY SDEAEAAINE
110 120 130 140 150
QINVEYNVSY VYHSLFAYFD RDNIALKGLA KFFKESSEEE REHAEKLIKY
160 170 180 190 200
QNIRGGRVVL HPITSPPSEF EHPEKGDALY AMELALSLEK LTNEKLLYVH
210 220 230 240 250
SVADRNNDAQ LADFIESEFL NEQVESIKKI AEYVTQLRLV GKGHGVWHFD

QRLLHD
Length:256
Mass (Da):28,444
Last modified:August 1, 1998 - v1
Checksum:i8B913652C017822B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052057 mRNA. Translation: AAC06026.1.
PIRiT08123.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052057 mRNA. Translation: AAC06026.1 .
PIRi T08123.

3D structure databases

ProteinModelPortali O65100.
ModBasei Search...
MobiDBi Search...

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. "Occurrence and expression of members of the ferritin gene family in cowpeas."
    Wardrop A.J., Wicks R.E., Entsch B.
    Biochem. J. 337:523-530(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. N41.
    Tissue: Leaf.

Entry informationi

Entry nameiFRI3_VIGUN
AccessioniPrimary (citable) accession number: O65100
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: August 1, 1998
Last modified: October 29, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3