FRIL_HUMAN
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 03-AUG-2022, entry version 224.
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";
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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 SMR; P02792; -.
DR BioGRID; 108789; 350.
DR CORUM; P02792; -.
DR DIP; DIP-31248N; -.
DR IntAct; P02792; 55.
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; P02792; -.
DR PeptideAtlas; P02792; -.
DR PRIDE; P02792; -.
DR ProteomicsDB; 51599; -.
DR TopDownProteomics; P02792; -.
DR Antibodypedia; 18468; 1044 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 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; SQDEWGT; -.
DR OrthoDB; 323029at2759; -.
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; 22 hits in 1041 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 92 other tissues.
DR ExpressionAtlas; P02792; baseline and differential.
DR Genevisible; P02792; HS.
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:cellular iron ion homeostasis; TAS:ProtInc.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; TAS:UniProtKB.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
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; PTHR11431; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00540; FERRITIN_1; 1.
DR PROSITE; PS00204; FERRITIN_2; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
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
