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Protein

Ferritin-4, chloroplastic

Gene
N/A
Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi91Iron 1PROSITE-ProRule annotation1
Metal bindingi126Iron 1PROSITE-ProRule annotation1
Metal bindingi126Iron 2PROSITE-ProRule annotation1
Metal bindingi129Iron 1PROSITE-ProRule annotation1
Metal bindingi175Iron 2PROSITE-ProRule annotation1
Metal bindingi209Iron 2PROSITE-ProRule annotation1

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-4, chloroplastic (EC:1.16.3.1)
Alternative name(s):
SFerH-4
OrganismiGlycine max (Soybean) (Glycine hispida)
Taxonomic identifieri3847 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
Proteomesi
  • UP000008827 Componenti: Chromosome 14

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 40ChloroplastSequence analysisAdd BLAST40
ChainiPRO_000000886741 – 247Ferritin-4, chloroplasticAdd BLAST207

Proteomic databases

PRIDEiQ948P5.

Expressioni

Gene expression databases

GenevisibleiQ948P5. GM.

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

Protein-protein interaction databases

STRINGi3847.GLYMA14G06160.1.

Structurei

Secondary structure

1247
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi52 – 56Combined sources5
Turni57 – 62Combined sources6
Helixi78 – 105Combined sources28
Turni108 – 110Combined sources3
Helixi113 – 140Combined sources28
Turni159 – 161Combined sources3
Helixi163 – 191Combined sources29
Helixi195 – 204Combined sources10
Helixi206 – 226Combined sources21
Helixi230 – 240Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A68X-ray1.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X36-247[»]
3A9QX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X36-247[»]
SMRiQ948P5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ948P5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini74 – 227Ferritin-like diironPROSITE-ProRule annotationAdd BLAST154

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni41 – 73Extension peptide (EP)Add BLAST33

Sequence similaritiesi

Belongs to the ferritin family.Curated
Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IU11. Eukaryota.
ENOG410Y5ZV. LUCA.
InParanoidiQ948P5.
KOiK00522.
OMAiDLHKLCS.
OrthoDBiEOG09360PX4.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
PROSITEiPS00204. 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.

Q948P5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLRTAAASA SSLSLFSPNA EPPRSVPARG LVVRAAKGST NHRALTGVIF
60 70 80 90 100
EPFEEVKKEL DLVPTVPQAS LARQKYVDES ESAVNEQINV EYNVSYVYHA
110 120 130 140 150
MFAYFDRDNV ALRGLAKFFK ESSEEEREHA EKLMEYQNKR GGKVKLQSIV
160 170 180 190 200
MPLSDFDHAD KGDALHAMEL ALSLEKLTNE KLLNLHSVAT KNGDVQLADF
210 220 230 240
VETEYLGEQV EAIKRISEYV AQLRRVGKGH GVWHFDQMLL HEGGDAA
Length:247
Mass (Da):27,559
Last modified:September 22, 2009 - v2
Checksum:i9A643DDFB5DDEDE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB062756 mRNA. Translation: BAB64537.2.
RefSeqiNP_001237049.1. NM_001250120.1.
UniGeneiGma.18301.

Genome annotation databases

EnsemblPlantsiGLYMA14G06160.1; GLYMA14G06160.1; GLYMA14G06160.
GeneIDi547477.
GrameneiGLYMA14G06160.1; GLYMA14G06160.1; GLYMA14G06160.
KEGGigmx:547477.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB062756 mRNA. Translation: BAB64537.2.
RefSeqiNP_001237049.1. NM_001250120.1.
UniGeneiGma.18301.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A68X-ray1.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X36-247[»]
3A9QX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X36-247[»]
SMRiQ948P5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3847.GLYMA14G06160.1.

Proteomic databases

PRIDEiQ948P5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiGLYMA14G06160.1; GLYMA14G06160.1; GLYMA14G06160.
GeneIDi547477.
GrameneiGLYMA14G06160.1; GLYMA14G06160.1; GLYMA14G06160.
KEGGigmx:547477.

Phylogenomic databases

eggNOGiENOG410IU11. Eukaryota.
ENOG410Y5ZV. LUCA.
InParanoidiQ948P5.
KOiK00522.
OMAiDLHKLCS.
OrthoDBiEOG09360PX4.

Miscellaneous databases

EvolutionaryTraceiQ948P5.

Gene expression databases

GenevisibleiQ948P5. GM.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
PROSITEiPS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFRI4_SOYBN
AccessioniPrimary (citable) accession number: Q948P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: September 22, 2009
Last modified: November 30, 2016
This is version 84 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.