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Protein

Ferritin light chain 1

Gene

Ftl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi54IronPROSITE-ProRule annotation1
Metal bindingi57IronPROSITE-ProRule annotation1
Metal bindingi58IronPROSITE-ProRule annotation1
Metal bindingi61IronPROSITE-ProRule annotation1
Metal bindingi64IronPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-3000480. Scavenging by Class A Receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin light chain 1
Alternative name(s):
Ferritin L subunit 1
Gene namesi
Name:Ftl1
Synonyms:Ftl, Ftl-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:95589. Ftl1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002010611 – 183Ferritin light chain 1Add BLAST183

Proteomic databases

EPDiP29391.
MaxQBiP29391.
PaxDbiP29391.
PeptideAtlasiP29391.
PRIDEiP29391.

2D gel databases

COMPLUYEAST-2DPAGEP29391.
SWISS-2DPAGEP29391.

PTM databases

iPTMnetiP29391.
PhosphoSitePlusiP29391.
SwissPalmiP29391.

Expressioni

Gene expression databases

CleanExiMM_FTL1.

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.

GO - Molecular functioni

Protein-protein interaction databases

IntActiP29391. 5 interactors.
MINTiMINT-1856732.
STRINGi10090.ENSMUSP00000092002.

Structurei

Secondary structure

1183
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 38Combined sources28
Turni41 – 43Combined sources3
Helixi46 – 73Combined sources28
Helixi93 – 120Combined sources28
Helixi124 – 133Combined sources10
Helixi135 – 155Combined sources21
Helixi170 – 178Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H96X-ray1.60A2-183[»]
1LB3X-ray1.21A2-183[»]
ProteinModelPortaliP29391.
SMRiP29391.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29391.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 156Ferritin-like diironPROSITE-ProRule annotationAdd BLAST150

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2332. Eukaryota.
COG1528. LUCA.
HOGENOMiHOG000223383.
HOVERGENiHBG000410.
InParanoidiP29391.
PhylomeDBiP29391.

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.

P29391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSQIRQNYS TEVEAAVNRL VNLHLRASYT YLSLGFFFDR DDVALEGVGH
60 70 80 90 100
FFRELAEEKR EGAERLLEFQ NDRGGRALFQ DVQKPSQDEW GKTQEAMEAA
110 120 130 140 150
LAMEKNLNQA LLDLHALGSA RTDPHLCDFL ESHYLDKEVK LIKKMGNHLT
160 170 180
NLRRVAGPQP AQTGAPQGSL GEYLFERLTL KHD
Length:183
Mass (Da):20,802
Last modified:January 23, 2007 - v2
Checksum:iF15598CCBAAF4C0B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25L → V in AAH19840 (PubMed:15489334).Curated1
Sequence conflicti122T → A in AAH19840 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04716 mRNA. Translation: AAA37614.1.
L39879 Genomic DNA. Translation: AAA62259.1.
BC019840 mRNA. Translation: AAH19840.1.
CCDSiCCDS39952.1.
PIRiB33355.
UniGeneiMm.30357.
Mm.348374.
Mm.431913.
Mm.491102.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04716 mRNA. Translation: AAA37614.1.
L39879 Genomic DNA. Translation: AAA62259.1.
BC019840 mRNA. Translation: AAH19840.1.
CCDSiCCDS39952.1.
PIRiB33355.
UniGeneiMm.30357.
Mm.348374.
Mm.431913.
Mm.491102.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H96X-ray1.60A2-183[»]
1LB3X-ray1.21A2-183[»]
ProteinModelPortaliP29391.
SMRiP29391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP29391. 5 interactors.
MINTiMINT-1856732.
STRINGi10090.ENSMUSP00000092002.

PTM databases

iPTMnetiP29391.
PhosphoSitePlusiP29391.
SwissPalmiP29391.

2D gel databases

COMPLUYEAST-2DPAGEP29391.
SWISS-2DPAGEP29391.

Proteomic databases

EPDiP29391.
MaxQBiP29391.
PaxDbiP29391.
PeptideAtlasiP29391.
PRIDEiP29391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:95589. Ftl1.

Phylogenomic databases

eggNOGiKOG2332. Eukaryota.
COG1528. LUCA.
HOGENOMiHOG000223383.
HOVERGENiHBG000410.
InParanoidiP29391.
PhylomeDBiP29391.

Enzyme and pathway databases

ReactomeiR-MMU-3000480. Scavenging by Class A Receptors.

Miscellaneous databases

ChiTaRSiFtl1. mouse.
EvolutionaryTraceiP29391.
PROiP29391.
SOURCEiSearch...

Gene expression databases

CleanExiMM_FTL1.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiFRIL1_MOUSE
AccessioniPrimary (citable) accession number: P29391
Secondary accession number(s): Q8WUQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.