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Protein

Ferritin light chain

Gene

FTL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi54Iron1
Metal bindingi57Iron1
Metal bindingi58Iron1
Metal bindingi61Iron1
Metal bindingi64Iron1

GO - Molecular functioni

  • ferric iron binding Source: InterPro
  • identical protein binding Source: IntAct
  • iron ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000087086-MONOMER.
ReactomeiR-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-432722. Golgi Associated Vesicle Biogenesis.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-917937. Iron uptake and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin light chain
Short name:
Ferritin L subunit
Gene namesi
Name:FTL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:3999. FTL.

Subcellular locationi

GO - Cellular componenti

  • autolysosome Source: MGI
  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • intracellular ferritin complex Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Hereditary hyperferritinemia-cataract syndrome (HHCS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disease characterized by elevated level of ferritin in serum and tissues, and early-onset bilateral cataract.
See also OMIM:600886
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07094830T → I in HHCS. 1 PublicationCorresponds to variant rs397514540dbSNPEnsembl.1
Neurodegeneration with brain iron accumulation 3 (NBIA3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neurodegenerative disorder associated with iron accumulation in the brain, primarily in the basal ganglia. It is characterized by a variety of neurological signs including parkinsonism, ataxia, corticospinal signs, mild non-progressive cognitive deficit and episodic psychosis. It is linked with decreased serum ferritin levels.
See also OMIM:606159
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02663396A → T in NBIA3. 1 PublicationCorresponds to variant rs104894685dbSNPEnsembl.1
L-ferritin deficiency (LFTD)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition characterized by low levels of ferritin in serum and tissues in the absence of other hematological symptoms. Seizures and mild neuropsychologic impairment may manifest in individuals with complete ferritin deficiency.
See also OMIM:615604

Keywords - Diseasei

Cataract, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi2512.
MalaCardsiFTL.
MIMi600886. phenotype.
606159. phenotype.
615604. phenotype.
OpenTargetsiENSG00000087086.
Orphaneti254704. Genetic hyperferritinemia without iron overload.
163. Hereditary hyperferritinemia with congenital cataracts.
157846. Neuroferritinopathy.
PharmGKBiPA28412.

Chemistry databases

DrugBankiDB00893. Iron Dextran.

Polymorphism and mutation databases

BioMutaiFTL.
DMDMi120523.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002010602 – 175Ferritin light chainAdd BLAST174

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP02792.
MaxQBiP02792.
PaxDbiP02792.
PeptideAtlasiP02792.
PRIDEiP02792.
TopDownProteomicsiP02792.

PTM databases

iPTMnetiP02792.
PhosphoSitePlusiP02792.
SwissPalmiP02792.

Expressioni

Gene expression databases

BgeeiENSG00000087086.
CleanExiHS_FTL.
GenevisibleiP02792. HS.

Organism-specific databases

HPAiCAB020769.
HPA041602.

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. Iron enters the spherical protein shell through pores that are formed between subunits. Mutations leading to truncation or the addition of extra residues at the C-terminus interfere with normal pore formation and with iron accumulation.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-713279,EBI-713279
FTH1P027948EBI-713279,EBI-713259
FTH1Q6NZ445EBI-713279,EBI-10180219
HTTP428582EBI-713279,EBI-466029
KPNA3Q8IYQ93EBI-713279,EBI-742146
MYOGP151733EBI-713279,EBI-3906629
NAMPTP434903EBI-713279,EBI-2829310
PSENENQ9NZ424EBI-713279,EBI-998468
SDCBPO005605EBI-713279,EBI-727004
USHBP1Q8N6Y03EBI-713279,EBI-739895

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi108789. 47 interactors.
DIPiDIP-31248N.
IntActiP02792. 29 interactors.
MINTiMINT-1187221.
STRINGi9606.ENSP00000366525.

Structurei

Secondary structure

1175
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 5Combined sources3
Helixi11 – 39Combined sources29
Turni41 – 43Combined sources3
Helixi46 – 73Combined sources28
Helixi93 – 120Combined sources28
Helixi124 – 133Combined sources10
Helixi135 – 154Combined sources20
Helixi160 – 170Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FFXX-ray1.90J2-174[»]
2FG4X-ray2.10A2-175[»]
2FG8X-ray2.50A/B/C/D/E/F/G/H2-175[»]
3KXUX-ray1.85A1-166[»]
4V6BX-ray2.85A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x1-166[»]
ProteinModelPortaliP02792.
SMRiP02792.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02792.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 61Catalytic site for iron oxidation8

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410KDTV. Eukaryota.
ENOG4111WYH. LUCA.
GeneTreeiENSGT00760000119129.
HOVERGENiHBG000410.
InParanoidiP02792.
KOiK13625.
PhylomeDBiP02792.
TreeFamiTF313885.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02792-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQIRQNYS TDVEAAVNSL VNLYLQASYT YLSLGFYFDR DDVALEGVSH
60 70 80 90 100
FFRELAEEKR EGYERLLKMQ NQRGGRALFQ DIKKPAEDEW GKTPDAMKAA
110 120 130 140 150
MALEKKLNQA LLDLHALGSA RTDPHLCDFL ETHFLDEEVK LIKKMGDHLT
160 170
NLHRLGGPEA GLGEYLFERL TLKHD
Length:175
Mass (Da):20,020
Last modified:January 23, 2007 - v2
Checksum:i0DB98081FF976BC2
GO

Sequence cautioni

The sequence CAE11873 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti54E → Q AA sequence (PubMed:6653779).Curated1
Sequence conflicti87E → Q AA sequence (PubMed:6653779).Curated1
Sequence conflicti89E → W AA sequence (PubMed:8706699).Curated1
Sequence conflicti102A → T in AAA35831 (PubMed:3858810).Curated1
Sequence conflicti154R → A AA sequence (PubMed:8706699).Curated1
Sequence conflicti175D → N AA sequence (PubMed:6653779).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07094830T → I in HHCS. 1 PublicationCorresponds to variant rs397514540dbSNPEnsembl.1
Natural variantiVAR_02663396A → T in NBIA3. 1 PublicationCorresponds to variant rs104894685dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11147 mRNA. Translation: AAA52439.1.
M10119 mRNA. Translation: AAA35831.1.
M12938 mRNA. Translation: AAA52440.1.
AY207005 mRNA. Translation: AAO52739.1.
CR456715 mRNA. Translation: CAG32996.1.
AK311773 mRNA. Translation: BAG34716.1.
BX571748 mRNA. Translation: CAE11873.1. Different initiation.
AC026803 Genomic DNA. No translation available.
BC002991 mRNA. Translation: AAH02991.2.
BC004245 mRNA. Translation: AAH04245.1.
BC008439 mRNA. Translation: AAH08439.1.
BC013928 mRNA. Translation: AAH13928.1.
BC016715 mRNA. Translation: AAH16715.1.
BC016346 mRNA. Translation: AAH16346.1.
BC016354 mRNA. Translation: AAH16354.1.
BC018990 mRNA. Translation: AAH18990.1.
BC021670 mRNA. Translation: AAH21670.1.
BC058820 mRNA. Translation: AAH58820.1.
BC062708 mRNA. Translation: AAH62708.1.
X03742 Genomic DNA. Translation: CAA27382.1.
X03743 Genomic DNA. Translation: CAA27383.1.
X03743 Genomic DNA. Translation: CAA27384.1.
CCDSiCCDS33070.1.
PIRiB23920. FRHUL.
RefSeqiNP_000137.2. NM_000146.3.
UniGeneiHs.433670.
Hs.728304.

Genome annotation databases

EnsembliENST00000331825; ENSP00000366525; ENSG00000087086.
GeneIDi2512.
KEGGihsa:2512.
UCSCiuc002plo.4. human.

Cross-referencesi

Web resourcesi

Wikipedia

Ferritin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11147 mRNA. Translation: AAA52439.1.
M10119 mRNA. Translation: AAA35831.1.
M12938 mRNA. Translation: AAA52440.1.
AY207005 mRNA. Translation: AAO52739.1.
CR456715 mRNA. Translation: CAG32996.1.
AK311773 mRNA. Translation: BAG34716.1.
BX571748 mRNA. Translation: CAE11873.1. Different initiation.
AC026803 Genomic DNA. No translation available.
BC002991 mRNA. Translation: AAH02991.2.
BC004245 mRNA. Translation: AAH04245.1.
BC008439 mRNA. Translation: AAH08439.1.
BC013928 mRNA. Translation: AAH13928.1.
BC016715 mRNA. Translation: AAH16715.1.
BC016346 mRNA. Translation: AAH16346.1.
BC016354 mRNA. Translation: AAH16354.1.
BC018990 mRNA. Translation: AAH18990.1.
BC021670 mRNA. Translation: AAH21670.1.
BC058820 mRNA. Translation: AAH58820.1.
BC062708 mRNA. Translation: AAH62708.1.
X03742 Genomic DNA. Translation: CAA27382.1.
X03743 Genomic DNA. Translation: CAA27383.1.
X03743 Genomic DNA. Translation: CAA27384.1.
CCDSiCCDS33070.1.
PIRiB23920. FRHUL.
RefSeqiNP_000137.2. NM_000146.3.
UniGeneiHs.433670.
Hs.728304.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FFXX-ray1.90J2-174[»]
2FG4X-ray2.10A2-175[»]
2FG8X-ray2.50A/B/C/D/E/F/G/H2-175[»]
3KXUX-ray1.85A1-166[»]
4V6BX-ray2.85A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x1-166[»]
ProteinModelPortaliP02792.
SMRiP02792.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108789. 47 interactors.
DIPiDIP-31248N.
IntActiP02792. 29 interactors.
MINTiMINT-1187221.
STRINGi9606.ENSP00000366525.

Chemistry databases

DrugBankiDB00893. Iron Dextran.

PTM databases

iPTMnetiP02792.
PhosphoSitePlusiP02792.
SwissPalmiP02792.

Polymorphism and mutation databases

BioMutaiFTL.
DMDMi120523.

Proteomic databases

EPDiP02792.
MaxQBiP02792.
PaxDbiP02792.
PeptideAtlasiP02792.
PRIDEiP02792.
TopDownProteomicsiP02792.

Protocols and materials databases

DNASUi2512.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331825; ENSP00000366525; ENSG00000087086.
GeneIDi2512.
KEGGihsa:2512.
UCSCiuc002plo.4. human.

Organism-specific databases

CTDi2512.
DisGeNETi2512.
GeneCardsiFTL.
GeneReviewsiFTL.
HGNCiHGNC:3999. FTL.
HPAiCAB020769.
HPA041602.
MalaCardsiFTL.
MIMi134790. gene.
600886. phenotype.
606159. phenotype.
615604. phenotype.
neXtProtiNX_P02792.
OpenTargetsiENSG00000087086.
Orphaneti254704. Genetic hyperferritinemia without iron overload.
163. Hereditary hyperferritinemia with congenital cataracts.
157846. Neuroferritinopathy.
PharmGKBiPA28412.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410KDTV. Eukaryota.
ENOG4111WYH. LUCA.
GeneTreeiENSGT00760000119129.
HOVERGENiHBG000410.
InParanoidiP02792.
KOiK13625.
PhylomeDBiP02792.
TreeFamiTF313885.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000087086-MONOMER.
ReactomeiR-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-432722. Golgi Associated Vesicle Biogenesis.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-917937. Iron uptake and transport.

Miscellaneous databases

ChiTaRSiFTL. human.
EvolutionaryTraceiP02792.
GeneWikiiFerritin_light_chain.
GenomeRNAii2512.
PROiP02792.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000087086.
CleanExiHS_FTL.
GenevisibleiP02792. HS.

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 nameiFRIL_HUMAN
AccessioniPrimary (citable) accession number: P02792
Secondary accession number(s): B2R4B9
, Q6IBT7, Q7Z2W1, Q86WI9, Q8WU07, Q96AU9, Q96CU0, Q9BTZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 184 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.