ID FRIH_RAT Reviewed; 182 AA. AC P19132; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 164. 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 Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3478702; DOI=10.1073/pnas.84.21.7438; RA Murray M.T., White K., Munro H.N.; RT "Conservation of ferritin heavy subunit gene structure: implications for RT the regulation of ferritin gene expression."; RL Proc. Natl. Acad. Sci. U.S.A. 84:7438-7442(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Liver; RA Wu C.G., Groenink M., Bosma A., Reitsma P.H., van Deventer J.H., RA Chamuleau R.A.F.M.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 81-87, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (JUL-2007) to UniProtKB. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 137-182. RX PubMed=2827671; DOI=10.1016/0006-291x(88)90518-9; RA Ursini M.V., de Franciscis V.; RT "TSH regulation of ferritin H chain messenger RNA levels in the rat RT thyroids."; RL Biochem. Biophys. Res. Commun. 150:287-295(1988). RN [5] RP PROTEIN SEQUENCE OF 159-182. RC TISSUE=Liver; RX PubMed=6546756; DOI=10.1016/s0021-9258(17)43049-3; RA Leibold E.A., Aziz N., Brown A.J.P., Munro H.N.; RT "Conservation in rat liver of light and heavy subunit sequences of RT mammalian ferritin. Presence of unique octopeptide in the light subunit."; RL J. Biol. Chem. 259:4327-4334(1984). 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 (By CC similarity). Mediates iron uptake in capsule cells of the developing CC kidney (By similarity). {ECO:0000250|UniProtKB:P02794, CC ECO:0000250|UniProtKB:P09528}. 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:P09528}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19130}. 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; M18053; AAA41153.1; -; Genomic_DNA. DR EMBL; M18051; AAA41153.1; JOINED; Genomic_DNA. DR EMBL; M18052; AAA41153.1; JOINED; Genomic_DNA. DR EMBL; U58829; AAB39890.1; -; mRNA. DR EMBL; M29330; AAA42300.1; -; mRNA. DR PIR; A39884; A39884. DR RefSeq; NP_036980.1; NM_012848.2. DR AlphaFoldDB; P19132; -. DR SMR; P19132; -. DR BioGRID; 247358; 1. DR IntAct; P19132; 1. DR STRING; 10116.ENSRNOP00000037803; -. DR iPTMnet; P19132; -. DR PhosphoSitePlus; P19132; -. DR SwissPalm; P19132; -. DR jPOST; P19132; -. DR PaxDb; 10116-ENSRNOP00000037803; -. DR DNASU; 25319; -. DR GeneID; 25319; -. DR KEGG; rno:25319; -. DR UCSC; RGD:2635; rat. DR AGR; RGD:2635; -. DR CTD; 2495; -. DR RGD; 2635; Fth1. DR eggNOG; KOG2332; Eukaryota. DR InParanoid; P19132; -. DR OrthoDB; 4611704at2759; -. DR Reactome; R-RNO-6798695; Neutrophil degranulation. DR Reactome; R-RNO-917937; Iron uptake and transport. DR PRO; PR:P19132; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0044754; C:autolysosome; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; ISO:RGD. DR GO; GO:0004322; F:ferroxidase activity; ISO:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0005506; F:iron ion binding; ISO:RGD. DR GO; GO:0140315; F:iron ion sequestering activity; ISO:RGD. 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; ISO:RGD. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB. 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. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Iron; Iron storage; KW Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1..182 FT /note="Ferritin heavy chain" FT /id="PRO_0000424476" 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_0000201053" 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 102 FT /note="R -> E (in Ref. 2; AAB39890)" FT /evidence="ECO:0000305" FT CONFLICT 182 FT /note="S -> E (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 182 AA; 21127 MW; F27E105373235B43 CRC64; MTTASPSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSC YFDRDDVALK NFAKYFLHQS HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWESGLNA MRCALHLEKS VNQSLLELHK LATDKNDPHL CDFIETHYLN EQVKSIKELG DHVTNLRKMG APESGMAEYL FDKHTLGHGD ES //