ID FRIL_HUMAN Reviewed; 175 AA. AC P02792; B2R4B9; Q6IBT7; Q7Z2W1; Q86WI9; Q8WU07; Q96AU9; Q96CU0; Q9BTZ8; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 233. DE RecName: Full=Ferritin light chain; DE Short=Ferritin L subunit; GN Name=FTL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3840162; DOI=10.1016/s0021-9258(17)39094-4; RA Boyd D., Vecoli C., Belcher D.M., Jain S.K., Drysdale J.W.; RT "Structural and functional relationships of human ferritin H and L chains RT deduced from cDNA clones."; RL J. Biol. Chem. 260:11755-11761(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3858810; DOI=10.1073/pnas.82.10.3139; RA Dorner M.H., Salfeld J., Will H., Leibold E.A., Vass J.K., Munro H.N.; RT "Structure of human ferritin light subunit messenger RNA: comparison with RT heavy subunit message and functional implications."; RL Proc. Natl. Acad. Sci. U.S.A. 82:3139-3143(1985). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3754330; DOI=10.1093/nar/14.7.2863; RA Santoro C., Marone M., Ferrone M., Costanzo F., Colombo M., Minganti C., RA Cortese R., Silengo L.; RT "Cloning of the gene coding for human L apoferritin."; RL Nucleic Acids Res. 14:2863-2876(1986). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Jordan T.P., Li X.G., Bhatti A.F., Obunike J.C., Tilson M.D.; RT "Expression of a ferritin-like mRNA by abdominal aortic aneurysm (AAA) RT adventitial fibroblasts."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon endothelium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Skin, Testis, and Urinary bladder; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-175. RX PubMed=3023856; DOI=10.1128/mcb.6.2.566-573.1986; RA Chou C.-C., Gatti R.A., Fuller M.L., Concannon P., Wong A., Chada S., RA Davis R.C., Salser W.A.; RT "Structure and expression of ferritin genes in a human promyelocytic cell RT line that differentiates in vitro."; RL Mol. Cell. Biol. 6:566-573(1986). RN [11] RP PROTEIN SEQUENCE OF 2-36 AND 41-175, CLEAVAGE OF INITIATOR METHIONINE, AND RP ACETYLATION AT SER-2. RC TISSUE=Liver; RX PubMed=6653779; DOI=10.1016/0014-5793(83)80037-4; RA Addison J.M., Fitton J.E., Lewis W.G., May K., Harrison P.M.; RT "The amino acid sequence of human liver apoferritin."; RL FEBS Lett. 164:139-144(1983). RN [12] RP PROTEIN SEQUENCE OF 84-90 AND 145-155. RC TISSUE=Placenta; RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x; RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., RA Thiede B., Wittmann-Liebold B., Otto A.; RT "Characterization of the human small-ribosomal-subunit proteins by N- RT terminal and internal sequencing, and mass spectrometry."; RL Eur. J. Biochem. 239:144-149(1996). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP INVOLVEMENT IN LFTD. RX PubMed=23940258; DOI=10.1084/jem.20130315; RA Cozzi A., Santambrogio P., Privitera D., Broccoli V., Rotundo L.I., RA Garavaglia B., Benz R., Altamura S., Goede J.S., Muckenthaler M.U., RA Levi S.; RT "Human L-ferritin deficiency is characterized by idiopathic generalized RT seizures and atypical restless leg syndrome."; RL J. Exp. Med. 210:1779-1791(2013). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-174, AND SUBUNIT. RX PubMed=16790936; DOI=10.1107/s0907444906018294; RA Wang Z., Li C., Ellenburg M., Soistman E., Ruble J., Wright B., Ho J.X., RA Carter D.C.; RT "Structure of human ferritin L chain."; RL Acta Crystallogr. D 62:800-806(2006). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-191, FUNCTION, SUBUNIT, AND RP DOMAIN. RX PubMed=19923220; DOI=10.1074/jbc.m109.042986; RA Baraibar M.A., Muhoberac B.B., Garringer H.J., Hurley T.D., Vidal R.; RT "Unraveling of the E-helices and disruption of 4-fold pores are associated RT with iron mishandling in a mutant ferritin causing neurodegeneration."; RL J. Biol. Chem. 285:1950-1956(2010). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-166, FUNCTION, SUBUNIT, DOMAIN, RP FUNCTION AS A FERROXIDASE, IDENTIFICATION BY MASS SPECTROMETRY, AND ROLE IN RP DISEASE. RX PubMed=20159981; DOI=10.1074/jbc.m109.096404; RA Luscieti S., Santambrogio P., Langlois d'Estaintot B., Granier T., RA Cozzi A., Poli M., Gallois B., Finazzi D., Cattaneo A., Levi S., Arosio P.; RT "Mutant ferritin L-chains that cause neurodegeneration act in a dominant- RT negative manner to reduce ferritin iron incorporation."; RL J. Biol. Chem. 285:11948-11957(2010). RN [20] RP VARIANT NBIA3 THR-96. RX PubMed=16116125; DOI=10.1212/01.wnl.0000178224.81169.c2; RA Maciel P., Cruz V.T., Constante M., Iniesta I., Costa M.C., Gallati S., RA Sousa N., Sequeiros J., Coutinho P., Santos M.M.; RT "Neuroferritinopathy: missense mutation in FTL causing early-onset RT bilateral pallidal involvement."; RL Neurology 65:603-605(2005). RN [21] RP VARIANT HRFTC ILE-30. RX PubMed=19176363; DOI=10.3324/haematol.2008.000125; RA Kannengiesser C., Jouanolle A.M., Hetet G., Mosser A., Muzeau F., Henry D., RA Bardou-Jacquet E., Mornet M., Brissot P., Deugnier Y., Grandchamp B., RA Beaumont C.; RT "A new missense mutation in the L ferritin coding sequence associated with RT elevated levels of glycosylated ferritin in serum and absence of iron RT overload."; RL Haematologica 94:335-339(2009). CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form. CC Important for iron homeostasis. Iron is taken up in the ferrous form CC and deposited as ferric hydroxides after oxidation. Also plays a role CC in delivery of iron to cells. Mediates iron uptake in capsule cells of CC the developing kidney (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:19923220, ECO:0000269|PubMed:20159981}. CC -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: L CC (light) chain and H (heavy) chain. The major chain can be light or CC heavy, depending on the species and tissue type. The functional CC molecule forms a roughly spherical shell with a diameter of 12 nm and CC contains a central cavity into which the insoluble mineral iron core is CC deposited. Iron enters the spherical protein shell through pores that CC are formed between subunits. Mutations leading to truncation or the CC addition of extra residues at the C-terminus interfere with normal pore CC formation and with iron accumulation. {ECO:0000269|PubMed:16790936, CC ECO:0000269|PubMed:19923220, ECO:0000269|PubMed:20159981}. CC -!- INTERACTION: CC P02792; P54253: ATXN1; NbExp=6; IntAct=EBI-713279, EBI-930964; CC P02792; P50570-2: DNM2; NbExp=3; IntAct=EBI-713279, EBI-10968534; CC P02792; P02794: FTH1; NbExp=16; IntAct=EBI-713279, EBI-713259; CC P02792; Q6NZ44: FTH1; NbExp=5; IntAct=EBI-713279, EBI-10180219; CC P02792; P02792: FTL; NbExp=14; IntAct=EBI-713279, EBI-713279; CC P02792; P42858: HTT; NbExp=20; IntAct=EBI-713279, EBI-466029; CC P02792; O00505: KPNA3; NbExp=3; IntAct=EBI-713279, EBI-358297; CC P02792; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-713279, EBI-16439278; CC P02792; P15173: MYOG; NbExp=4; IntAct=EBI-713279, EBI-3906629; CC P02792; P43490: NAMPT; NbExp=3; IntAct=EBI-713279, EBI-2829310; CC P02792; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-713279, EBI-741158; CC P02792; P49768-2: PSEN1; NbExp=3; IntAct=EBI-713279, EBI-11047108; CC P02792; P49810: PSEN2; NbExp=3; IntAct=EBI-713279, EBI-2010251; CC P02792; Q9NZ42: PSENEN; NbExp=4; IntAct=EBI-713279, EBI-998468; CC P02792; O00560: SDCBP; NbExp=6; IntAct=EBI-713279, EBI-727004; CC P02792; P37840: SNCA; NbExp=3; IntAct=EBI-713279, EBI-985879; CC P02792; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-713279, EBI-739895; CC P02792; O76024: WFS1; NbExp=3; IntAct=EBI-713279, EBI-720609; CC -!- DISEASE: Hyperferritinemia with or without cataract (HRFTC) CC [MIM:600886]: An autosomal dominant disease characterized by elevated CC level of ferritin in serum and tissues, and early-onset bilateral CC cataract. Cataracts may be subclinical in some patients. CC {ECO:0000269|PubMed:19176363}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Neurodegeneration with brain iron accumulation 3 (NBIA3) CC [MIM:606159]: A neurodegenerative disorder associated with iron CC accumulation in the brain, primarily in the basal ganglia. It is CC characterized by a variety of neurological signs including CC parkinsonism, ataxia, corticospinal signs, mild non-progressive CC cognitive deficit and episodic psychosis. It is linked with decreased CC serum ferritin levels. {ECO:0000269|PubMed:16116125}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- DISEASE: L-ferritin deficiency (LFTD) [MIM:615604]: A condition CC characterized by low levels of ferritin in serum and tissues in the CC absence of other hematological symptoms. Seizures and mild CC neuropsychologic impairment may manifest in individuals with complete CC ferritin deficiency. {ECO:0000269|PubMed:23940258}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAE11873.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ferritin entry; CC URL="https://en.wikipedia.org/wiki/Ferritin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M11147; AAA52439.1; -; mRNA. DR EMBL; M10119; AAA35831.1; -; mRNA. DR EMBL; M12938; AAA52440.1; -; mRNA. DR EMBL; AY207005; AAO52739.1; -; mRNA. DR EMBL; CR456715; CAG32996.1; -; mRNA. DR EMBL; AK311773; BAG34716.1; -; mRNA. DR EMBL; BX571748; CAE11873.1; ALT_INIT; mRNA. DR EMBL; AC026803; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002991; AAH02991.2; -; mRNA. DR EMBL; BC004245; AAH04245.1; -; mRNA. DR EMBL; BC008439; AAH08439.1; -; mRNA. DR EMBL; BC013928; AAH13928.1; -; mRNA. DR EMBL; BC016715; AAH16715.1; -; mRNA. DR EMBL; BC016346; AAH16346.1; -; mRNA. DR EMBL; BC016354; AAH16354.1; -; mRNA. DR EMBL; BC018990; AAH18990.1; -; mRNA. DR EMBL; BC021670; AAH21670.1; -; mRNA. DR EMBL; BC058820; AAH58820.1; -; mRNA. DR EMBL; BC062708; AAH62708.1; -; mRNA. DR EMBL; X03742; CAA27382.1; -; Genomic_DNA. DR EMBL; X03743; CAA27383.1; -; Genomic_DNA. DR EMBL; X03743; CAA27384.1; -; Genomic_DNA. DR CCDS; CCDS33070.1; -. DR PIR; B23920; FRHUL. DR RefSeq; NP_000137.2; NM_000146.3. DR PDB; 2FFX; X-ray; 1.90 A; J=2-174. DR PDB; 2FG4; X-ray; 2.10 A; A=2-175. DR PDB; 2FG8; X-ray; 2.50 A; A/B/C/D/E/F/G/H=2-175. DR PDB; 3KXU; X-ray; 1.85 A; A=1-166. DR 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. DR PDB; 5LG8; X-ray; 1.98 A; A=1-175. DR PDB; 6TR9; X-ray; 2.46 A; AAA=1-175. DR PDB; 6TS0; X-ray; 2.20 A; AAA=1-175. DR PDB; 6TS1; X-ray; 2.20 A; AAA=1-175. DR PDB; 6TSA; X-ray; 2.18 A; AAA=1-175. DR PDB; 6TSF; X-ray; 2.09 A; AAA=1-175. DR PDB; 6TSJ; X-ray; 2.30 A; AAA=1-175. DR PDB; 6WX6; EM; 2.00 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=1-175. DR PDBsum; 2FFX; -. DR PDBsum; 2FG4; -. DR PDBsum; 2FG8; -. DR PDBsum; 3KXU; -. DR PDBsum; 4V6B; -. DR PDBsum; 5LG8; -. DR PDBsum; 6TR9; -. DR PDBsum; 6TS0; -. DR PDBsum; 6TS1; -. DR PDBsum; 6TSA; -. DR PDBsum; 6TSF; -. DR PDBsum; 6TSJ; -. DR PDBsum; 6WX6; -. DR AlphaFoldDB; P02792; -. DR EMDB; EMD-21951; -. DR SMR; P02792; -. DR BioGRID; 108789; 355. DR CORUM; P02792; -. DR DIP; DIP-31248N; -. DR IntAct; P02792; 56. DR MINT; P02792; -. DR STRING; 9606.ENSP00000366525; -. DR DrugBank; DB09147; Ferric pyrophosphate. DR DrugBank; DB13995; Ferric pyrophosphate citrate. DR DrugBank; DB06784; Gallium citrate Ga-67. DR DrugBank; DB00893; Iron Dextran. DR DrugBank; DB02285; Protoporphyrin. DR DrugBank; DB09517; Sodium ferric gluconate complex. DR iPTMnet; P02792; -. DR PhosphoSitePlus; P02792; -. DR SwissPalm; P02792; -. DR BioMuta; FTL; -. DR DMDM; 120523; -. DR CPTAC; CPTAC-1407; -. DR CPTAC; CPTAC-1408; -. DR EPD; P02792; -. DR jPOST; P02792; -. DR MassIVE; P02792; -. DR MaxQB; P02792; -. DR PaxDb; 9606-ENSP00000366525; -. DR PeptideAtlas; P02792; -. DR ProteomicsDB; 51599; -. DR Pumba; P02792; -. DR TopDownProteomics; P02792; -. DR Antibodypedia; 18468; 1142 antibodies from 40 providers. DR DNASU; 2512; -. DR Ensembl; ENST00000331825.11; ENSP00000366525.2; ENSG00000087086.15. DR GeneID; 2512; -. DR KEGG; hsa:2512; -. DR MANE-Select; ENST00000331825.11; ENSP00000366525.2; NM_000146.4; NP_000137.2. DR UCSC; uc002plo.4; human. DR AGR; HGNC:3999; -. DR CTD; 2512; -. DR DisGeNET; 2512; -. DR GeneCards; FTL; -. DR GeneReviews; FTL; -. DR HGNC; HGNC:3999; FTL. DR HPA; ENSG00000087086; Tissue enhanced (liver). DR MalaCards; FTL; -. DR MIM; 134790; gene. DR MIM; 600886; phenotype. DR MIM; 606159; phenotype. DR MIM; 615604; phenotype. DR neXtProt; NX_P02792; -. DR OpenTargets; ENSG00000087086; -. DR Orphanet; 254704; Genetic hyperferritinemia without iron overload. DR Orphanet; 163; Hereditary hyperferritinemia-cataract syndrome. DR Orphanet; 440731; L-ferritin deficiency. DR Orphanet; 157846; Neuroferritinopathy. DR PharmGKB; PA28412; -. DR VEuPathDB; HostDB:ENSG00000087086; -. DR eggNOG; KOG2332; Eukaryota. DR GeneTree; ENSGT00940000153096; -. DR HOGENOM; CLU_065681_4_0_1; -. DR InParanoid; P02792; -. DR OMA; CARADPH; -. DR OrthoDB; 4611704at2759; -. DR PhylomeDB; P02792; -. DR TreeFam; TF313885; -. DR PathwayCommons; P02792; -. DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-917937; Iron uptake and transport. DR SignaLink; P02792; -. DR BioGRID-ORCS; 2512; 25 hits in 1123 CRISPR screens. DR ChiTaRS; FTL; human. DR EvolutionaryTrace; P02792; -. DR GeneWiki; Ferritin_light_chain; -. DR GenomeRNAi; 2512; -. DR Pharos; P02792; Tbio. DR PRO; PR:P02792; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P02792; Protein. DR Bgee; ENSG00000087086; Expressed in stromal cell of endometrium and 94 other cell types or tissues. DR ExpressionAtlas; P02792; baseline and differential. DR GO; GO:0044754; C:autolysosome; IDA:MGI. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0008043; C:intracellular ferritin complex; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB. DR GO; GO:0006879; P:intracellular iron ion homeostasis; TAS:ProtInc. DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR CDD; cd00904; Ferritin; 1. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR001519; Ferritin. DR InterPro; IPR012347; Ferritin-like. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR014034; Ferritin_CS. DR InterPro; IPR008331; Ferritin_DPS_dom. DR PANTHER; PTHR11431; FERRITIN; 1. DR PANTHER; PTHR11431:SF47; FERRITIN LIGHT CHAIN; 1. DR Pfam; PF00210; Ferritin; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00540; FERRITIN_1; 1. DR PROSITE; PS00204; FERRITIN_2; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. DR Genevisible; P02792; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cataract; Direct protein sequencing; KW Disease variant; Iron; Iron storage; Metal-binding; Neurodegeneration; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:6653779" FT CHAIN 2..175 FT /note="Ferritin light chain" FT /id="PRO_0000201060" FT DOMAIN 7..156 FT /note="Ferritin-like diiron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT REGION 54..61 FT /note="Catalytic site for iron oxidation" FT BINDING 54 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 57 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 58 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 61 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 64 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:6653779" FT VARIANT 30 FT /note="T -> I (in HRFTC; dbSNP:rs397514540)" FT /evidence="ECO:0000269|PubMed:19176363" FT /id="VAR_070948" FT VARIANT 96 FT /note="A -> T (in NBIA3; dbSNP:rs104894685)" FT /evidence="ECO:0000269|PubMed:16116125" FT /id="VAR_026633" FT CONFLICT 54 FT /note="E -> Q (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 87 FT /note="E -> Q (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 89 FT /note="E -> W (in Ref. 12; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 102 FT /note="A -> T (in Ref. 2; AAA35831)" FT /evidence="ECO:0000305" FT CONFLICT 154 FT /note="R -> A (in Ref. 12; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 175 FT /note="D -> N (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT TURN 3..5 FT /evidence="ECO:0007829|PDB:2FG4" FT HELIX 11..39 FT /evidence="ECO:0007829|PDB:3KXU" FT TURN 41..43 FT /evidence="ECO:0007829|PDB:3KXU" FT HELIX 46..73 FT /evidence="ECO:0007829|PDB:3KXU" FT HELIX 93..120 FT /evidence="ECO:0007829|PDB:3KXU" FT HELIX 124..133 FT /evidence="ECO:0007829|PDB:3KXU" FT HELIX 135..154 FT /evidence="ECO:0007829|PDB:3KXU" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:5LG8" FT HELIX 160..170 FT /evidence="ECO:0007829|PDB:2FFX" SQ 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 //