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Protein

Ferritin

Gene

FTN

Organism
Pseudo-nitzschia multiseries
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64Iron 1Combined sources1
Metal bindingi64Iron 2Combined sources1
Metal bindingi65Iron 1Combined sources1
Metal bindingi68Iron 2Combined sources1
Metal bindingi77Iron 3Combined sources1
Metal bindingi77Zinc 1Combined sources1
Metal bindingi102Iron 4Combined sources1
Metal bindingi106Iron 12Combined sources1
Metal bindingi106Iron 4Combined sources1
Metal bindingi106Iron 5Combined sources1
Metal bindingi106Iron 6Combined sources1
Metal bindingi106Iron 7Combined sources1
Metal bindingi106Iron 8Combined sources1
Metal bindingi106Iron 9Combined sources1
Metal bindingi106Zinc 2Combined sources1
Metal bindingi109Iron 10Combined sources1
Metal bindingi109Iron 11Combined sources1
Metal bindingi109Iron 6Combined sources1
Metal bindingi109Iron 7Combined sources1
Metal bindingi109Iron 9Combined sources1
Metal bindingi109Zinc 2Combined sources1
Metal bindingi110Iron 12Combined sources1
Metal bindingi110Iron 3Combined sources1
Metal bindingi110Iron 8Combined sources1
Metal bindingi110Zinc 1Combined sources1
Metal bindingi110Zinc 3Combined sources1
Metal bindingi110Zinc 4Combined sources1
Metal bindingi113Iron 3; via pros nitrogenCombined sources1
Metal bindingi113Zinc 1; via pros nitrogenCombined sources1
Metal bindingi156Iron 12Combined sources1
Metal bindingi156Iron 8Combined sources1
Metal bindingi156Zinc 3Combined sources1
Metal bindingi156Zinc 4Combined sources1
Metal bindingi159Iron 3Combined sources1
Metal bindingi192Iron 4Combined sources1
Metal bindingi192Iron 6Combined sources1
Metal bindingi192Iron 7Combined sources1
Metal bindingi192Iron 8Combined sources1
Metal bindingi192Iron 9Combined sources1
Metal bindingi192Zinc 2Combined sources1
Metal bindingi192Zinc 4Combined sources1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

Iron storageUniRule annotation

Keywords - Ligandi

Iron, Metal-bindingUniRule annotationCombined sources, ZincCombined sources

Names & Taxonomyi

Protein namesi
Recommended name:
FerritinUniRule annotation (EC:1.16.3.1UniRule annotation)
Gene namesi
Name:FTNImported
OrganismiPseudo-nitzschia multiseriesImported
Taxonomic identifieri37319 [NCBI]
Taxonomic lineageiEukaryotaStramenopilesBacillariophytaBacillariophyceaeBacillariophycidaeBacillarialesBacillariaceaePseudo-nitzschia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_500284193221 – 230FerritinSequence analysisAdd BLAST210

Interactioni

Protein-protein interaction databases

DIPiDIP-59728N.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3E6RX-ray2.40A/B/C/D/E/F63-229[»]
3E6SX-ray1.95A/B/C/D/E/F63-229[»]
4ISMX-ray2.00A/B/C/D/E/F/G/H63-229[»]
4ISPX-ray2.20A/B/C/D/E/F/G/H63-229[»]
4ITTX-ray2.10A/B/C/D/E/F/G/H63-229[»]
4ITWX-ray2.00A/B/C/D/E/F/G/H63-229[»]
4IWJX-ray1.95A/B/C/D/E/F/G/H63-229[»]
4IWKX-ray1.65A/B/C/D/E/F63-229[»]
4IXKX-ray2.10A/B/C/D/E/F/G/H63-229[»]
4ZKHX-ray1.90A/B/C/D/E/F/G/H63-230[»]
4ZKWX-ray1.80A/B/C/D/E/F/G/H63-230[»]
4ZKXX-ray1.80A/B/C/D/E/F/G/H63-230[»]
4ZL5X-ray1.85A/B/C/D/E/F63-230[»]
4ZL6X-ray1.90A/B/C/D/E/F63-230[»]
4ZLWX-ray2.00A/B/C/D/E/F/G/H63-229[»]
4ZMCX-ray1.90A/B/C/D/E/F/G/H63-229[»]
SMRiB6DMH6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiB6DMH6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini60 – 207Ferritin-like diironInterPro annotationAdd BLAST148

Sequence similaritiesi

Belongs to the ferritin family.UniRule annotation
Contains 1 ferritin-like diiron domain.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

B6DMH6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSPFFFLSA LALTLRDSSP SFATAFRLAV TRCARQGIHA PSSSSSSSSR
60 70 80 90 100
CLVASASALA GPSEELLDLF NRQVTQEFTA SQVYLSASIW FDQNDWEGMA
110 120 130 140 150
AYMLAESAEE REHGLGFVDF ANKRNIPIEL QAVPAPVSCA EWSSPEDVWQ
160 170 180 190 200
SILELEQANT RSLLNLAEAA STCHDFAVMA FLNPFHLQQV NEEDKIGSIL
210 220 230
AKVTDENRTP GLLRSLDVVS FLGPCLFRSV
Length:230
Mass (Da):25,199
Last modified:November 25, 2008 - v1
Checksum:i56107F9680350575
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei230Imported1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ004953 mRNA. Translation: ACI30660.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ004953 mRNA. Translation: ACI30660.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3E6RX-ray2.40A/B/C/D/E/F63-229[»]
3E6SX-ray1.95A/B/C/D/E/F63-229[»]
4ISMX-ray2.00A/B/C/D/E/F/G/H63-229[»]
4ISPX-ray2.20A/B/C/D/E/F/G/H63-229[»]
4ITTX-ray2.10A/B/C/D/E/F/G/H63-229[»]
4ITWX-ray2.00A/B/C/D/E/F/G/H63-229[»]
4IWJX-ray1.95A/B/C/D/E/F/G/H63-229[»]
4IWKX-ray1.65A/B/C/D/E/F63-229[»]
4IXKX-ray2.10A/B/C/D/E/F/G/H63-229[»]
4ZKHX-ray1.90A/B/C/D/E/F/G/H63-230[»]
4ZKWX-ray1.80A/B/C/D/E/F/G/H63-230[»]
4ZKXX-ray1.80A/B/C/D/E/F/G/H63-230[»]
4ZL5X-ray1.85A/B/C/D/E/F63-230[»]
4ZL6X-ray1.90A/B/C/D/E/F63-230[»]
4ZLWX-ray2.00A/B/C/D/E/F/G/H63-229[»]
4ZMCX-ray1.90A/B/C/D/E/F/G/H63-229[»]
SMRiB6DMH6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59728N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiB6DMH6.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiB6DMH6_9STRA
AccessioniPrimary (citable) accession number: B6DMH6
Entry historyi
Integrated into UniProtKB/TrEMBL: November 25, 2008
Last sequence update: November 25, 2008
Last modified: November 2, 2016
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.