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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541IronPROSITE-ProRule annotation
Metal bindingi57 – 571IronPROSITE-ProRule annotation
Metal bindingi58 – 581IronPROSITE-ProRule annotation
Metal bindingi61 – 611IronPROSITE-ProRule annotation
Metal bindingi64 – 641IronPROSITE-ProRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 183183Ferritin light chain 1PRO_0000201061Add
BLAST

Proteomic databases

EPDiP29391.
MaxQBiP29391.
PaxDbiP29391.
PeptideAtlasiP29391.
PRIDEiP29391.

2D gel databases

COMPLUYEAST-2DPAGEP29391.
SWISS-2DPAGEP29391.

PTM databases

iPTMnetiP29391.
PhosphoSiteiP29391.
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 interactions.
MINTiMINT-1856732.
STRINGi10090.ENSMUSP00000092002.

Structurei

Secondary structure

1
183
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 3828Combined sources
Turni41 – 433Combined sources
Helixi46 – 7328Combined sources
Helixi93 – 12028Combined sources
Helixi124 – 13310Combined sources
Helixi135 – 15521Combined sources
Helixi170 – 1789Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H96X-ray1.60A2-183[»]
1LB3X-ray1.21A2-183[»]
ProteinModelPortaliP29391.
SMRiP29391. Positions 3-180.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29391.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 156150Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251L → V in AAH19840 (PubMed:15489334).Curated
Sequence conflicti122 – 1221T → A in AAH19840 (PubMed:15489334).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1H96X-ray1.60A2-183[»]
1LB3X-ray1.21A2-183[»]
ProteinModelPortaliP29391.
SMRiP29391. Positions 3-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP29391.
PhosphoSiteiP29391.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Transcriptional regulation of ferritin H and L subunits in adult erythroid and liver cells from the mouse. Unambiguous identification of mouse ferritin subunits and in vitro formation of the ferritin shells."
    Beaumont C., Dugast I., Renaudie F., Souroujon M., Grandchamp B.
    J. Biol. Chem. 264:7498-7504(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning, characterization and expression of mouse ferritin L subunit gene."
    Renaudie F., Boulanger L., Grandchamp B., Beaumont C.
    C. R. Acad. Sci. III, Sci. Vie 318:431-437(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 106-121 AND 155-177, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  5. Cited for: FUNCTION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

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: July 6, 2016
This is version 146 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.