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Ferritin light chain (Ferritin L subunit)

 FRIL_HUMAN              Reviewed;         175 AA.
P02792; B2R4B9; Q6IBT7; Q7Z2W1; Q86WI9; Q8WU07; Q96AU9; Q96CU0;
Q9BTZ8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 193.
RecName: Full=Ferritin light chain;
Short=Ferritin L subunit;
Name=FTL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3840162;
Boyd D., Vecoli C., Belcher D.M., Jain S.K., Drysdale J.W.;
"Structural and functional relationships of human ferritin H and L
chains deduced from cDNA clones.";
J. Biol. Chem. 260:11755-11761(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3858810; DOI=10.1073/pnas.82.10.3139;
Dorner M.H., Salfeld J., Will H., Leibold E.A., Vass J.K., Munro H.N.;
"Structure of human ferritin light subunit messenger RNA: comparison
with heavy subunit message and functional implications.";
Proc. Natl. Acad. Sci. U.S.A. 82:3139-3143(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3754330; DOI=10.1093/nar/14.7.2863;
Santoro C., Marone M., Ferrone M., Costanzo F., Colombo M.,
Minganti C., Cortese R., Silengo L.;
"Cloning of the gene coding for human L apoferritin.";
Nucleic Acids Res. 14:2863-2876(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Jordan T.P., Li X.G., Bhatti A.F., Obunike J.C., Tilson M.D.;
"Expression of a ferritin-like mRNA by abdominal aortic aneurysm (AAA)
adventitial fibroblasts.";
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon endothelium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
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., 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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Skin, Testis, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 33-175.
PubMed=3023856; DOI=10.1128/MCB.6.2.566;
Chou C.-C., Gatti R.A., Fuller M.L., Concannon P., Wong A., Chada S.,
Davis R.C., Salser W.A.;
"Structure and expression of ferritin genes in a human promyelocytic
cell line that differentiates in vitro.";
Mol. Cell. Biol. 6:566-573(1986).
[11]
PROTEIN SEQUENCE OF 2-36 AND 41-175, CLEAVAGE OF INITIATOR METHIONINE,
AND ACETYLATION AT SER-2.
TISSUE=Liver;
PubMed=6653779; DOI=10.1016/0014-5793(83)80037-4;
Addison J.M., Fitton J.E., Lewis W.G., May K., Harrison P.M.;
"The amino acid sequence of human liver apoferritin.";
FEBS Lett. 164:139-144(1983).
[12]
PROTEIN SEQUENCE OF 84-90 AND 145-155.
TISSUE=Placenta;
PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
"Characterization of the human small-ribosomal-subunit proteins by N-
terminal and internal sequencing, and mass spectrometry.";
Eur. J. Biochem. 239:144-149(1996).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
INVOLVEMENT IN LFTD.
PubMed=23940258; DOI=10.1084/jem.20130315;
Cozzi A., Santambrogio P., Privitera D., Broccoli V., Rotundo L.I.,
Garavaglia B., Benz R., Altamura S., Goede J.S., Muckenthaler M.U.,
Levi S.;
"Human L-ferritin deficiency is characterized by idiopathic
generalized seizures and atypical restless leg syndrome.";
J. Exp. Med. 210:1779-1791(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-174, AND SUBUNIT.
PubMed=16790936; DOI=10.1107/S0907444906018294;
Wang Z., Li C., Ellenburg M., Soistman E., Ruble J., Wright B.,
Ho J.X., Carter D.C.;
"Structure of human ferritin L chain.";
Acta Crystallogr. D 62:800-806(2006).
[18]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-191, FUNCTION, SUBUNIT,
AND DOMAIN.
PubMed=19923220; DOI=10.1074/jbc.M109.042986;
Baraibar M.A., Muhoberac B.B., Garringer H.J., Hurley T.D., Vidal R.;
"Unraveling of the E-helices and disruption of 4-fold pores are
associated with iron mishandling in a mutant ferritin causing
neurodegeneration.";
J. Biol. Chem. 285:1950-1956(2010).
[19]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-166, FUNCTION, SUBUNIT,
DOMAIN, FUNCTION AS A FERROXIDASE, IDENTIFICATION BY MASS
SPECTROMETRY, AND ROLE IN DISEASE.
PubMed=20159981; DOI=10.1074/jbc.M109.096404;
Luscieti S., Santambrogio P., Langlois d'Estaintot B., Granier T.,
Cozzi A., Poli M., Gallois B., Finazzi D., Cattaneo A., Levi S.,
Arosio P.;
"Mutant ferritin L-chains that cause neurodegeneration act in a
dominant-negative manner to reduce ferritin iron incorporation.";
J. Biol. Chem. 285:11948-11957(2010).
[20]
VARIANT NBIA3 THR-96.
PubMed=16116125; DOI=10.1212/01.wnl.0000178224.81169.c2;
Maciel P., Cruz V.T., Constante M., Iniesta I., Costa M.C.,
Gallati S., Sousa N., Sequeiros J., Coutinho P., Santos M.M.;
"Neuroferritinopathy: missense mutation in FTL causing early-onset
bilateral pallidal involvement.";
Neurology 65:603-605(2005).
[21]
VARIANT HRFTC ILE-30.
PubMed=19176363; DOI=10.3324/haematol.2008.000125;
Kannengiesser C., Jouanolle A.M., Hetet G., Mosser A., Muzeau F.,
Henry D., Bardou-Jacquet E., Mornet M., Brissot P., Deugnier Y.,
Grandchamp B., Beaumont C.;
"A new missense mutation in the L ferritin coding sequence associated
with elevated levels of glycosylated ferritin in serum and absence of
iron overload.";
Haematologica 94:335-339(2009).
-!- 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).
{ECO:0000250, ECO:0000269|PubMed:19923220,
ECO:0000269|PubMed:20159981}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:16790936, ECO:0000269|PubMed:19923220,
ECO:0000269|PubMed:20159981}.
-!- INTERACTION:
Self; NbExp=12; IntAct=EBI-713279, EBI-713279;
P02794:FTH1; NbExp=14; IntAct=EBI-713279, EBI-713259;
Q6NZ44:FTH1; NbExp=5; IntAct=EBI-713279, EBI-10180219;
P42858:HTT; NbExp=2; IntAct=EBI-713279, EBI-466029;
O00505:KPNA3; NbExp=3; IntAct=EBI-713279, EBI-358297;
P15173:MYOG; NbExp=3; IntAct=EBI-713279, EBI-3906629;
P43490:NAMPT; NbExp=3; IntAct=EBI-713279, EBI-2829310;
Q9NZ42:PSENEN; NbExp=4; IntAct=EBI-713279, EBI-998468;
O00560:SDCBP; NbExp=5; IntAct=EBI-713279, EBI-727004;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-713279, EBI-739895;
-!- DISEASE: Hyperferritinemia with or without cataract (HRFTC)
[MIM:600886]: An autosomal dominant disease characterized by
elevated level of ferritin in serum and tissues, and early-onset
bilateral cataract. Cataracts may be subclinical in some patients.
{ECO:0000269|PubMed:19176363}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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. {ECO:0000269|PubMed:16116125}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: L-ferritin deficiency (LFTD) [MIM:615604]: A 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. {ECO:0000269|PubMed:23940258}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAE11873.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Ferritin entry;
URL="https://en.wikipedia.org/wiki/Ferritin";
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EMBL; M11147; AAA52439.1; -; mRNA.
EMBL; M10119; AAA35831.1; -; mRNA.
EMBL; M12938; AAA52440.1; -; mRNA.
EMBL; AY207005; AAO52739.1; -; mRNA.
EMBL; CR456715; CAG32996.1; -; mRNA.
EMBL; AK311773; BAG34716.1; -; mRNA.
EMBL; BX571748; CAE11873.1; ALT_INIT; mRNA.
EMBL; AC026803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002991; AAH02991.2; -; mRNA.
EMBL; BC004245; AAH04245.1; -; mRNA.
EMBL; BC008439; AAH08439.1; -; mRNA.
EMBL; BC013928; AAH13928.1; -; mRNA.
EMBL; BC016715; AAH16715.1; -; mRNA.
EMBL; BC016346; AAH16346.1; -; mRNA.
EMBL; BC016354; AAH16354.1; -; mRNA.
EMBL; BC018990; AAH18990.1; -; mRNA.
EMBL; BC021670; AAH21670.1; -; mRNA.
EMBL; BC058820; AAH58820.1; -; mRNA.
EMBL; BC062708; AAH62708.1; -; mRNA.
EMBL; X03742; CAA27382.1; -; Genomic_DNA.
EMBL; X03743; CAA27383.1; -; Genomic_DNA.
EMBL; X03743; CAA27384.1; -; Genomic_DNA.
CCDS; CCDS33070.1; -.
PIR; B23920; FRHUL.
RefSeq; NP_000137.2; NM_000146.3.
UniGene; Hs.433670; -.
UniGene; Hs.728304; -.
PDB; 2FFX; X-ray; 1.90 A; J=2-174.
PDB; 2FG4; X-ray; 2.10 A; A=2-175.
PDB; 2FG8; X-ray; 2.50 A; A/B/C/D/E/F/G/H=2-175.
PDB; 3KXU; X-ray; 1.85 A; A=1-166.
PDB; 4V6B; X-ray; 2.85 A; A/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/x=1-166.
PDB; 5LG8; X-ray; 1.98 A; A=1-175.
PDBsum; 2FFX; -.
PDBsum; 2FG4; -.
PDBsum; 2FG8; -.
PDBsum; 3KXU; -.
PDBsum; 4V6B; -.
PDBsum; 5LG8; -.
ProteinModelPortal; P02792; -.
SMR; P02792; -.
BioGrid; 108789; 47.
CORUM; P02792; -.
DIP; DIP-31248N; -.
IntAct; P02792; 29.
MINT; MINT-1187221; -.
STRING; 9606.ENSP00000366525; -.
DrugBank; DB09412; Gallium citrate Ga-67.
DrugBank; DB00893; Iron Dextran.
DrugBank; DB02285; Protoporphyrin Ix.
iPTMnet; P02792; -.
PhosphoSitePlus; P02792; -.
SwissPalm; P02792; -.
BioMuta; FTL; -.
DMDM; 120523; -.
EPD; P02792; -.
MaxQB; P02792; -.
PaxDb; P02792; -.
PeptideAtlas; P02792; -.
PRIDE; P02792; -.
TopDownProteomics; P02792; -.
DNASU; 2512; -.
Ensembl; ENST00000331825; ENSP00000366525; ENSG00000087086.
GeneID; 2512; -.
KEGG; hsa:2512; -.
UCSC; uc002plo.4; human.
CTD; 2512; -.
DisGeNET; 2512; -.
EuPathDB; HostDB:ENSG00000087086.13; -.
GeneCards; FTL; -.
GeneReviews; FTL; -.
HGNC; HGNC:3999; FTL.
HPA; CAB020769; -.
HPA; HPA041602; -.
MalaCards; FTL; -.
MIM; 134790; gene.
MIM; 600886; phenotype.
MIM; 606159; phenotype.
MIM; 615604; phenotype.
neXtProt; NX_P02792; -.
OpenTargets; ENSG00000087086; -.
Orphanet; 254704; Genetic hyperferritinemia without iron overload.
Orphanet; 163; Hereditary hyperferritinemia with congenital cataracts.
Orphanet; 157846; Neuroferritinopathy.
PharmGKB; PA28412; -.
eggNOG; ENOG410KDTV; Eukaryota.
eggNOG; ENOG4111WYH; LUCA.
GeneTree; ENSGT00760000119129; -.
HOVERGEN; HBG000410; -.
InParanoid; P02792; -.
KO; K13625; -.
OMA; VNLYLRA; -.
PhylomeDB; P02792; -.
TreeFam; TF313885; -.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-917937; Iron uptake and transport.
ChiTaRS; FTL; human.
EvolutionaryTrace; P02792; -.
GeneWiki; Ferritin_light_chain; -.
GenomeRNAi; 2512; -.
PRO; PR:P02792; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000087086; -.
CleanEx; HS_FTL; -.
Genevisible; P02792; HS.
GO; GO:0044754; C:autolysosome; IDA:MGI.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0008043; C:intracellular ferritin complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
GO; GO:0055072; P:iron ion homeostasis; TAS:UniProtKB.
GO; GO:0006826; P:iron ion transport; IEA:InterPro.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
Gene3D; 1.20.1260.10; -; 1.
InterPro; IPR001519; Ferritin.
InterPro; IPR012347; Ferritin-like.
InterPro; IPR009040; Ferritin-like_diiron.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR014034; Ferritin_CS.
InterPro; IPR008331; Ferritin_DPS_dom.
PANTHER; PTHR11431; PTHR11431; 1.
Pfam; PF00210; Ferritin; 1.
SUPFAM; SSF47240; SSF47240; 1.
PROSITE; PS00540; FERRITIN_1; 1.
PROSITE; PS00204; FERRITIN_2; 1.
PROSITE; PS50905; FERRITIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cataract; Complete proteome;
Direct protein sequencing; Disease mutation; Iron; Iron storage;
Metal-binding; Neurodegeneration; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6653779}.
CHAIN 2 175 Ferritin light chain.
/FTId=PRO_0000201060.
DOMAIN 7 156 Ferritin-like diiron.
{ECO:0000255|PROSITE-ProRule:PRU00085}.
REGION 54 61 Catalytic site for iron oxidation.
METAL 54 54 Iron.
METAL 57 57 Iron.
METAL 58 58 Iron.
METAL 61 61 Iron.
METAL 64 64 Iron.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:6653779}.
VARIANT 30 30 T -> I (in HRFTC; dbSNP:rs397514540).
{ECO:0000269|PubMed:19176363}.
/FTId=VAR_070948.
VARIANT 96 96 A -> T (in NBIA3; dbSNP:rs104894685).
{ECO:0000269|PubMed:16116125}.
/FTId=VAR_026633.
CONFLICT 54 54 E -> Q (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 87 87 E -> Q (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 89 89 E -> W (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 102 102 A -> T (in Ref. 2; AAA35831).
{ECO:0000305}.
CONFLICT 154 154 R -> A (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 175 175 D -> N (in Ref. 11; AA sequence).
{ECO:0000305}.
TURN 3 5 {ECO:0000244|PDB:2FG4}.
HELIX 11 39 {ECO:0000244|PDB:3KXU}.
TURN 41 43 {ECO:0000244|PDB:3KXU}.
HELIX 46 73 {ECO:0000244|PDB:3KXU}.
HELIX 93 120 {ECO:0000244|PDB:3KXU}.
HELIX 124 133 {ECO:0000244|PDB:3KXU}.
HELIX 135 154 {ECO:0000244|PDB:3KXU}.
HELIX 157 159 {ECO:0000244|PDB:5LG8}.
HELIX 160 170 {ECO:0000244|PDB:2FFX}.
SEQUENCE 175 AA; 20020 MW; 0DB98081FF976BC2 CRC64;
MSSQIRQNYS TDVEAAVNSL VNLYLQASYT YLSLGFYFDR DDVALEGVSH FFRELAEEKR
EGYERLLKMQ NQRGGRALFQ DIKKPAEDEW GKTPDAMKAA MALEKKLNQA LLDLHALGSA
RTDPHLCDFL ETHFLDEEVK LIKKMGDHLT NLHRLGGPEA GLGEYLFERL TLKHD


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