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

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 bindingi64Iron 3Combined sources1
Metal bindingi65Iron 1Combined sources1
Metal bindingi68Iron 2Combined sources1
Metal bindingi77Iron 4Combined sources1
Metal bindingi77Iron 5Combined sources1
Metal bindingi102Iron 6Combined sources1
Metal bindingi102Iron 7Combined sources1
Metal bindingi106Iron 10Combined sources1
Metal bindingi106Iron 6Combined sources1
Metal bindingi106Iron 7Combined sources1
Metal bindingi106Iron 8Combined sources1
Metal bindingi106Iron 9Combined sources1
Metal bindingi109Iron 11Combined sources1
Metal bindingi109Iron 12Combined sources1
Metal bindingi109Iron 8Combined sources1
Metal bindingi109Iron 9Combined sources1
Metal bindingi110Iron 10Combined sources1
Metal bindingi110Iron 13Combined sources1
Metal bindingi110Iron 14Combined sources1
Metal bindingi110Iron 15Combined sources1
Metal bindingi110Iron 4Combined sources1
Metal bindingi110Iron 5Combined sources1
Metal bindingi113Iron 16; via tele nitrogenCombined sources1
Metal bindingi113Iron 4; via pros nitrogenCombined sources1
Metal bindingi156Iron 10Combined sources1
Metal bindingi156Iron 13Combined sources1
Metal bindingi156Iron 14Combined sources1
Metal bindingi156Iron 15Combined sources1
Metal bindingi159Iron 14Combined sources1
Metal bindingi159Iron 4Combined sources1
Metal bindingi188Iron 16Combined sources1
Metal bindingi189Iron 15Combined sources1
Metal bindingi192Iron 10Combined sources1
Metal bindingi192Iron 16Combined sources1
Metal bindingi192Iron 6Combined sources1
Metal bindingi192Iron 8Combined sources1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotation
Biological processIron storageUniRule annotation
LigandIron, Metal-bindingUniRule annotationCombined 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

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

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiView protein in InterPro
IPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiView protein in Pfam
PF00210. Ferritin. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiView protein in PROSITE
PS50905. FERRITIN_LIKE. 1 hit.

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.

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.

Entry informationi

Entry nameiB6DMH6_9STRA
AccessioniPrimary (citable) accession number: B6DMH6
Entry historyiIntegrated into UniProtKB/TrEMBL: November 25, 2008
Last sequence update: November 25, 2008
Last modified: July 5, 2017
This is version 50 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources