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P02792 (FRIL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferritin light chain

Short name=Ferritin L subunit
Gene names
Name:FTL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15 Ref.16

Subunit structure

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. Ref.14 Ref.15 Ref.16

Involvement in disease

Hereditary hyperferritinemia-cataract syndrome (HHCS) [MIM:600886]: An autosomal dominant disease characterized by elevated level of ferritin in serum and tissues, and early-onset bilateral cataract.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Neurodegeneration with brain iron accumulation 3 (NBIA3) [MIM:606159]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Sequence caution

The sequence CAE11873.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 175174Ferritin light chain
PRO_0000201060

Regions

Domain7 – 156150Ferritin-like diiron
Region54 – 618Catalytic site for iron oxidation

Sites

Metal binding541Iron
Metal binding571Iron
Metal binding581Iron
Metal binding611Iron
Metal binding641Iron

Amino acid modifications

Modified residue21N-acetylserine Ref.11

Natural variations

Natural variant961A → T in NBIA3. Ref.17
VAR_026633

Experimental info

Sequence conflict541E → Q AA sequence Ref.11
Sequence conflict871E → Q AA sequence Ref.11
Sequence conflict891E → W AA sequence Ref.12
Sequence conflict1021A → T in AAA35831. Ref.2
Sequence conflict1541R → A AA sequence Ref.12
Sequence conflict1751D → N AA sequence Ref.11

Secondary structure

.................. 175
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02792 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0DB98081FF976BC2

FASTA17520,020
        10         20         30         40         50         60 
MSSQIRQNYS TDVEAAVNSL VNLYLQASYT YLSLGFYFDR DDVALEGVSH FFRELAEEKR 

        70         80         90        100        110        120 
EGYERLLKMQ NQRGGRALFQ DIKKPAEDEW GKTPDAMKAA MALEKKLNQA LLDLHALGSA 

       130        140        150        160        170 
RTDPHLCDFL ETHFLDEEVK LIKKMGDHLT NLHRLGGPEA GLGEYLFERL TLKHD 

« Hide

References

« Hide 'large scale' references
[1]"Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones."
Boyd D., Vecoli C., Belcher D.M., Jain S.K., Drysdale J.W.
J. Biol. Chem. 260:11755-11761(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications."
Dorner M.H., Salfeld J., Will H., Leibold E.A., Vass J.K., Munro H.N.
Proc. Natl. Acad. Sci. U.S.A. 82:3139-3143(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning of the gene coding for human L apoferritin."
Santoro C., Marone M., Ferrone M., Costanzo F., Colombo M., Minganti C., Cortese R., Silengo L.
Nucleic Acids Res. 14:2863-2876(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Expression of a ferritin-like mRNA by abdominal aortic aneurysm (AAA) adventitial fibroblasts."
Jordan T.P., Li X.G., Bhatti A.F., Obunike J.C., Tilson M.D.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon endothelium.
[8]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: Brain, Skin, Testis and Urinary bladder.
[10]"Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro."
Chou C.-C., Gatti R.A., Fuller M.L., Concannon P., Wong A., Chada S., Davis R.C., Salser W.A.
Mol. Cell. Biol. 6:566-573(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-175.
[11]"The amino acid sequence of human liver apoferritin."
Addison J.M., Fitton J.E., Lewis W.G., May K., Harrison P.M.
FEBS Lett. 164:139-144(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-36 AND 41-175.
Tissue: Liver.
[12]"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 84-90 AND 145-155.
Tissue: Placenta.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Structure of human ferritin L chain."
Wang Z., Li C., Ellenburg M., Soistman E., Ruble J., Wright B., Ho J.X., Carter D.C.
Acta Crystallogr. D 62:800-806(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-174, SUBUNIT.
[15]"Unraveling of the E-helices and disruption of 4-fold pores are associated with iron mishandling in a mutant ferritin causing neurodegeneration."
Baraibar M.A., Muhoberac B.B., Garringer H.J., Hurley T.D., Vidal R.
J. Biol. Chem. 285:1950-1956(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-191, FUNCTION, SUBUNIT, DOMAIN.
[16]"Mutant ferritin L-chains that cause neurodegeneration act in a dominant-negative manner to reduce ferritin iron incorporation."
Luscieti S., Santambrogio P., Langlois d'Estaintot B., Granier T., Cozzi A., Poli M., Gallois B., Finazzi D., Cattaneo A., Levi S., Arosio P.
J. Biol. Chem. 285:11948-11957(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-166, FUNCTION, SUBUNIT, DOMAIN, FUNCTION AS A FERROXIDASE, IDENTIFICATION BY MASS SPECTROMETRY, ROLE IN DISEASE.
[17]"Neuroferritinopathy: missense mutation in FTL causing early-onset bilateral pallidal involvement."
Maciel P., Cruz V.T., Constante M., Iniesta I., Costa M.C., Gallati S., Sousa N., Sequeiros J., Coutinho P., Santos M.M.
Neurology 65:603-605(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NBIA3 THR-96.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRFRHUL. B23920.
RefSeqNP_000137.2. NM_000146.3.
UniGeneHs.433670.
Hs.728304.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FFXX-ray1.90J2-173[»]
2FG4X-ray2.10A2-174[»]
2FG8X-ray2.50A/B/C/D/E/F/G/H2-174[»]
3HX2X-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/x1-175[»]
3HX5X-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/x1-175[»]
3HX7X-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/x1-175[»]
3KXUX-ray1.85A1-166[»]
ProteinModelPortalP02792.
SMRP02792. Positions 2-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108789. 28 interactions.
DIPDIP-31248N.
IntActP02792. 18 interactions.
MINTMINT-1187221.
STRING9606.ENSP00000366525.

Chemistry

DrugBankDB00893. Iron Dextran.

PTM databases

PhosphoSiteP02792.

Polymorphism databases

DMDM120523.

Proteomic databases

PaxDbP02792.
PRIDEP02792.

Protocols and materials databases

DNASU2512.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331825; ENSP00000366525; ENSG00000087086.
GeneID2512.
KEGGhsa:2512.
UCSCuc002plo.3. human.

Organism-specific databases

CTD2512.
GeneCardsGC19P049468.
HGNCHGNC:3999. FTL.
HPACAB020769.
HPA041602.
MIM134790. gene.
600886. phenotype.
606159. phenotype.
neXtProtNX_P02792.
Orphanet254704. Genetic hyperferritinemia without iron overload.
163. Hereditary hyperferritinemia with congenital cataracts.
157846. Neuroferritinopathy.
PharmGKBPA28412.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG321513.
HOVERGENHBG000410.
InParanoidP02792.
KOK13625.
OMAMYLQASY.
OrthoDBEOG7DRJ49.
PhylomeDBP02792.
TreeFamTF313885.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_15518. Transmembrane transport of small molecules.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP02792.
BgeeP02792.
CleanExHS_FTL.
GenevestigatorP02792.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERPTHR11431. PTHR11431. 1 hit.
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFTL. human.
EvolutionaryTraceP02792.
GeneWikiFerritin_light_chain.
GenomeRNAi2512.
NextBio9899.
PROP02792.
SOURCESearch...

Entry information

Entry nameFRIL_HUMAN
AccessionPrimary (citable) accession number: P02792
Secondary accession number(s): B2R4B9 expand/collapse secondary AC list , Q6IBT7, Q7Z2W1, Q86WI9, Q8WU07, Q96AU9, Q96CU0, Q9BTZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM