ID FRIH_MOUSE Reviewed; 182 AA. AC P09528; Q3UI44; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 207. DE RecName: Full=Ferritin heavy chain; DE Short=Ferritin H subunit; DE EC=1.16.3.1 {ECO:0000250|UniProtKB:P02794}; DE Contains: DE RecName: Full=Ferritin heavy chain, N-terminally processed; GN Name=Fth1; Synonyms=Fth; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BALB/cJ; RX PubMed=2798146; DOI=10.1093/nar/17.19.8005; RA Yachaou A., Renaudie F., Grandchamp B., Beaumont C.; RT "Nucleotide sequence of the mouse ferritin H chain gene."; RL Nucleic Acids Res. 17:8005-8005(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ICR; TISSUE=Macrophage; RX PubMed=3194211; DOI=10.1093/nar/16.21.10373; RA Miyazaki Y., Setoguchi M., Higuchi Y., Yoshida S., Akizuki S., Yamamoto S.; RT "Nucleotide sequence of cDNA encoding the heavy subunit of mouse macrophage RT ferritin."; RL Nucleic Acids Res. 16:10373-10373(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3410854; DOI=10.1016/s0021-9258(18)37801-3; RA Torti S.V., Kwak E.L., Miller S.C., Miller L.L., Ringold G.M., Myambo K.B., RA Young A.P., Torti F.M.; RT "The molecular cloning and characterization of murine ferritin heavy chain, RT a tumor necrosis factor-inducible gene."; RL J. Biol. Chem. 263:12638-12644(1988). RN [4] RP NUCLEOTIDE SEQUENCE. RX PubMed=2258056; DOI=10.1016/0378-1119(90)90396-9; RA Kwak E.L., Torti S.V., Torti F.M.; RT "Murine ferritin heavy chain: isolation and characterization of a RT functional gene."; RL Gene 94:255-261(1990). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2708374; DOI=10.1016/s0021-9258(18)83262-8; RA Beaumont C., Dugast I., Renaudie F., Souroujon M., Grandchamp B.; RT "Transcriptional regulation of ferritin H and L subunits in adult erythroid RT and liver cells from the mouse. Unambiguous identification of mouse RT ferritin subunits and in vitro formation of the ferritin shells."; RL J. Biol. Chem. 264:7498-7504(1989). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Amnion, Heart, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary tumor; 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 [8] RP PROTEIN SEQUENCE OF 11-23 AND 55-64, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. RN [9] RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE. RX PubMed=10652280; DOI=10.1074/jbc.275.5.3021; RA Ferreira C., Bucchini D., Martin M.E., Levi S., Arosio P., Grandchamp B., RA Beaumont C.; RT "Early embryonic lethality of H ferritin gene deletion in mice."; RL J. Biol. Chem. 275:3021-3024(2000). RN [10] RP DISRUPTION PHENOTYPE. RX PubMed=11468145; DOI=10.1182/blood.v98.3.525; RA Ferreira C., Santambrogio P., Martin M.E., Andrieu V., Feldmann G., RA Henin D., Beaumont C.; RT "H ferritin knockout mice: a model of hyperferritinemia in the absence of RT iron overload."; RL Blood 98:525-532(2001). RN [11] RP FUNCTION. RX PubMed=19154717; DOI=10.1016/j.devcel.2008.12.002; RA Li J.Y., Paragas N., Ned R.M., Qiu A., Viltard M., Leete T., Drexler I.R., RA Chen X., Sanna-Cherchi S., Mohammed F., Williams D., Lin C.S., RA Schmidt-Ott K.M., Andrews N.C., Barasch J.; RT "Scara5 is a ferritin receptor mediating non-transferrin iron delivery."; RL Dev. Cell 16:35-46(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form CC (By similarity). Important for iron homeostasis (By similarity). Has CC ferroxidase activity (By similarity). Iron is taken up in the ferrous CC form and deposited as ferric hydroxides after oxidation (By CC similarity). Also plays a role in delivery of iron to cells CC (PubMed:19154717). Mediates iron uptake in capsule cells of the CC developing kidney (PubMed:19154717). {ECO:0000250|UniProtKB:P02794, CC ECO:0000269|PubMed:19154717}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; CC Evidence={ECO:0000250|UniProtKB:P02794}; 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. {ECO:0000250|UniProtKB:P02794}. CC -!- INTERACTION: CC P09528; P09528: Fth1; NbExp=3; IntAct=EBI-308950, EBI-308950; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19130}. CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc, detected at low levels in the CC developing heart and central nervous system. At later stages of CC development, widely expressed, predominantly in the heart and brown fat CC tissue. {ECO:0000269|PubMed:10652280}. CC -!- DISRUPTION PHENOTYPE: Homozygous mutant embryos die in utero between CC 3.5 and 9.5 dpc (PubMed:10652280). Heterozygous animals are healthy and CC fertile and do not present any apparent abnormalities. They show CC slightly elevated tissue light chain ferritin content and 7- to 10-fold CC more light chain ferritin in the serum than normal mice, but their CC serum iron remains unchanged. {ECO:0000269|PubMed:10652280, CC ECO:0000269|PubMed:11468145}. CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}. 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; X52561; CAA36795.1; -; Genomic_DNA. DR EMBL; X12812; CAA31300.1; -; mRNA. DR EMBL; J03941; AAA37611.1; -; mRNA. DR EMBL; M60170; AAA37613.1; -; Genomic_DNA. DR EMBL; M24509; AAA37612.1; -; mRNA. DR EMBL; AK027998; BAC25694.1; -; mRNA. DR EMBL; AK139622; BAE24084.1; -; mRNA. DR EMBL; AK147082; BAE27662.1; -; mRNA. DR EMBL; AK150262; BAE29419.1; -; mRNA. DR EMBL; AK150508; BAE29621.1; -; mRNA. DR EMBL; AK150628; BAE29718.1; -; mRNA. DR EMBL; AK150679; BAE29759.1; -; mRNA. DR EMBL; AK150693; BAE29772.1; -; mRNA. DR EMBL; AK151192; BAE30189.1; -; mRNA. DR EMBL; AK151241; BAE30233.1; -; mRNA. DR EMBL; AK151399; BAE30367.1; -; mRNA. DR EMBL; AK151609; BAE30548.1; -; mRNA. DR EMBL; AK151675; BAE30600.1; -; mRNA. DR EMBL; AK152071; BAE30924.1; -; mRNA. DR EMBL; AK152542; BAE31297.1; -; mRNA. DR EMBL; AK152702; BAE31431.1; -; mRNA. DR EMBL; AK153017; BAE31651.1; -; mRNA. DR EMBL; AK153195; BAE31795.1; -; mRNA. DR EMBL; AK153199; BAE31799.1; -; mRNA. DR EMBL; AK159243; BAE34925.1; -; mRNA. DR EMBL; AK168601; BAE40468.1; -; mRNA. DR EMBL; AK169004; BAE40803.1; -; mRNA. DR EMBL; BC012314; AAH12314.1; -; mRNA. DR CCDS; CCDS29567.1; -. DR PIR; S06070; S06070. DR RefSeq; NP_034369.1; NM_010239.2. DR PDB; 3WNW; X-ray; 2.24 A; A/B/C/D/E/F/G/H/I/J/K/L=1-182. DR PDB; 5OBA; 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=1-177. DR PDB; 5OBB; X-ray; 2.65 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=1-177. DR PDB; 6S61; EM; 1.84 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=1-182. DR PDB; 6SHT; EM; 2.73 A; A=1-182. DR PDB; 6V21; EM; 1.75 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=5-178. DR PDB; 7A4M; EM; 1.22 A; A=6-177. DR PDB; 7KOD; EM; 1.66 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=1-182. DR PDB; 7TB3; EM; 2.57 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=7-182. DR PDB; 7TBH; EM; 2.30 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=7-182. DR PDB; 8BK9; EM; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/W/X/Y=1-182. DR PDB; 8BKA; EM; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/W/X/Y=1-182. DR PDB; 8BKB; EM; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/W/X/Y=1-182. DR PDB; 8EMQ; EM; 1.66 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=6-177. DR PDB; 8EN7; EM; 1.68 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=6-177. DR PDB; 8J5A; EM; 1.19 A; A=6-177. DR PDB; 8PVC; EM; 2.60 A; A=1-182. DR PDBsum; 3WNW; -. DR PDBsum; 5OBA; -. DR PDBsum; 5OBB; -. DR PDBsum; 6S61; -. DR PDBsum; 6SHT; -. DR PDBsum; 6V21; -. DR PDBsum; 7A4M; -. DR PDBsum; 7KOD; -. DR PDBsum; 7TB3; -. DR PDBsum; 7TBH; -. DR PDBsum; 8BK9; -. DR PDBsum; 8BKA; -. DR PDBsum; 8BKB; -. DR PDBsum; 8EMQ; -. DR PDBsum; 8EN7; -. DR PDBsum; 8J5A; -. DR PDBsum; 8PVC; -. DR AlphaFoldDB; P09528; -. DR EMDB; EMD-10101; -. DR EMDB; EMD-10205; -. DR EMDB; EMD-10675; -. DR EMDB; EMD-11638; -. DR EMDB; EMD-12358; -. DR EMDB; EMD-16093; -. DR EMDB; EMD-16094; -. DR EMDB; EMD-16095; -. DR EMDB; EMD-17961; -. DR EMDB; EMD-17995; -. DR EMDB; EMD-21024; -. DR EMDB; EMD-22972; -. DR EMDB; EMD-24795; -. DR EMDB; EMD-24796; -. DR EMDB; EMD-24797; -. DR EMDB; EMD-28259; -. DR EMDB; EMD-28269; -. DR EMDB; EMD-31314; -. DR EMDB; EMD-33707; -. DR EMDB; EMD-35981; -. DR EMDB; EMD-35984; -. DR EMDB; EMD-9914; -. DR SMR; P09528; -. DR BioGRID; 199755; 13. DR IntAct; P09528; 5. DR MINT; P09528; -. DR STRING; 10090.ENSMUSP00000158539; -. DR GlyGen; P09528; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P09528; -. DR MetOSite; P09528; -. DR PhosphoSitePlus; P09528; -. DR SwissPalm; P09528; -. DR REPRODUCTION-2DPAGE; P09528; -. DR CPTAC; non-CPTAC-3809; -. DR EPD; P09528; -. DR jPOST; P09528; -. DR MaxQB; P09528; -. DR PaxDb; 10090-ENSMUSP00000025563; -. DR PeptideAtlas; P09528; -. DR ProteomicsDB; 271802; -. DR Pumba; P09528; -. DR Antibodypedia; 28385; 983 antibodies from 41 providers. DR DNASU; 14319; -. DR Ensembl; ENSMUST00000025563.8; ENSMUSP00000025563.7; ENSMUSG00000024661.8. DR Ensembl; ENSMUST00000235196.2; ENSMUSP00000158539.2; ENSMUSG00000024661.8. DR GeneID; 14319; -. DR KEGG; mmu:14319; -. DR UCSC; uc008got.2; mouse. DR AGR; MGI:95588; -. DR CTD; 2495; -. DR MGI; MGI:95588; Fth1. DR VEuPathDB; HostDB:ENSMUSG00000024661; -. DR eggNOG; KOG2332; Eukaryota. DR GeneTree; ENSGT00950000182841; -. DR HOGENOM; CLU_065681_4_0_1; -. DR InParanoid; P09528; -. DR OMA; GLNTMEC; -. DR OrthoDB; 4611704at2759; -. DR PhylomeDB; P09528; -. DR TreeFam; TF313885; -. DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR Reactome; R-MMU-917937; Iron uptake and transport. DR BioGRID-ORCS; 14319; 3 hits in 75 CRISPR screens. DR ChiTaRS; Fth1; mouse. DR PRO; PR:P09528; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; P09528; Protein. DR Bgee; ENSMUSG00000024661; Expressed in globus pallidus and 278 other cell types or tissues. DR ExpressionAtlas; P09528; baseline and differential. DR GO; GO:0044754; C:autolysosome; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; ISO:MGI. DR GO; GO:0004322; F:ferroxidase activity; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005506; F:iron ion binding; IDA:MGI. DR GO; GO:0140315; F:iron ion sequestering activity; ISO:MGI. DR GO; GO:0006955; P:immune response; ISS:UniProtKB. DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central. DR GO; GO:0006826; P:iron ion transport; IDA:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI. DR CDD; cd01056; Euk_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:SF37; FERRITIN HEAVY 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; P09528; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Iron; KW Iron storage; Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1..182 FT /note="Ferritin heavy chain" FT /id="PRO_0000424473" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000250|UniProtKB:P02794" FT CHAIN 2..182 FT /note="Ferritin heavy chain, N-terminally processed" FT /id="PRO_0000201049" FT DOMAIN 11..160 FT /note="Ferritin-like diiron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 28 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 63 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 63 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 66 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 108 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 142 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P02794" FT MOD_RES 2 FT /note="N-acetylthreonine; in Ferritin heavy chain, N- FT terminally processed" FT /evidence="ECO:0000250|UniProtKB:P02794" FT CONFLICT 17 FT /note="A -> S (in Ref. 5; AAA37612)" FT /evidence="ECO:0000305" FT CONFLICT 137 FT /note="Y -> H (in Ref. 5; AAA37612)" FT /evidence="ECO:0000305" FT CONFLICT 140 FT /note="S -> N (in Ref. 5; AAA37612)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="A -> S (in Ref. 5; AAA37612)" FT /evidence="ECO:0000305" FT HELIX 15..42 FT /evidence="ECO:0007829|PDB:7A4M" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:7A4M" FT HELIX 50..76 FT /evidence="ECO:0007829|PDB:7A4M" FT HELIX 97..124 FT /evidence="ECO:0007829|PDB:7A4M" FT HELIX 128..137 FT /evidence="ECO:0007829|PDB:7A4M" FT HELIX 139..159 FT /evidence="ECO:0007829|PDB:7A4M" FT TURN 160..163 FT /evidence="ECO:0007829|PDB:7A4M" FT HELIX 166..174 FT /evidence="ECO:0007829|PDB:7A4M" SQ SEQUENCE 182 AA; 21067 MW; 129A8887A2BC650B CRC64; MTTASPSQVR QNYHQDAEAA INRQINLELY ASYVYLSMSC YFDRDDVALK NFAKYFLHQS HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWESGLNA MECALHLEKS VNQSLLELHK LATDKNDPHL CDFIETYYLS EQVKSIKELG DHVTNLRKMG APEAGMAEYL FDKHTLGHGD ES //