ID FRIH_BOVIN Reviewed; 181 AA. AC O46414; Q56JZ8; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 151. 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 Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Spleen; RX PubMed=9467878; DOI=10.1016/s0305-0491(97)00277-0; RA Orino K., Eguchi K., Nakayama T., Yamamoto S., Watanabe K.; RT "Sequencing of cDNA clones that encode bovine ferritin H and L chains."; RL Comp. Biochem. Physiol. 118B:667-673(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymphoid epithelium; RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.; RT "Analysis of sequences obtained from constructed full-length bovine cDNA RT libraries."; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 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; AB003093; BAA24818.1; -; mRNA. DR EMBL; AY911329; AAW82097.1; -; mRNA. DR EMBL; BC105376; AAI05377.1; -; mRNA. DR RefSeq; NP_776487.1; NM_174062.3. DR PDB; 7U5L; EM; 2.67 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=1-181. DR PDBsum; 7U5L; -. DR AlphaFoldDB; O46414; -. DR EMDB; EMD-26354; -. DR SMR; O46414; -. DR STRING; 9913.ENSBTAP00000071152; -. DR PaxDb; 9913-ENSBTAP00000014853; -. DR PeptideAtlas; O46414; -. DR Ensembl; ENSBTAT00000014853.5; ENSBTAP00000014853.5; ENSBTAG00000011184.5. DR GeneID; 281173; -. DR KEGG; bta:281173; -. DR CTD; 2495; -. DR VEuPathDB; HostDB:ENSBTAG00000011184; -. DR VGNC; VGNC:56265; FTH1. DR eggNOG; KOG2332; Eukaryota. DR GeneTree; ENSGT00950000182841; -. DR HOGENOM; CLU_065681_4_0_1; -. DR InParanoid; O46414; -. DR OMA; QKYSDEC; -. DR OrthoDB; 4611704at2759; -. DR Reactome; R-BTA-6798695; Neutrophil degranulation. DR Reactome; R-BTA-917937; Iron uptake and transport. DR Proteomes; UP000009136; Chromosome 29. DR Bgee; ENSBTAG00000011184; Expressed in monocyte and 103 other cell types or tissues. DR ExpressionAtlas; O46414; baseline and differential. 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; IBA:GO_Central. DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC. 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; IBA:GO_Central. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS: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 3D-structure; Acetylation; Cytoplasm; Iron; Iron storage; Metal-binding; KW Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1..181 FT /note="Ferritin heavy chain" FT /id="PRO_0000424468" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000250|UniProtKB:P02794" FT CHAIN 2..181 FT /note="Ferritin heavy chain, N-terminally processed" FT /id="PRO_0000201045" 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 MOD_RES 179 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02794" FT HELIX 15..41 FT /evidence="ECO:0007829|PDB:7U5L" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:7U5L" FT HELIX 50..76 FT /evidence="ECO:0007829|PDB:7U5L" FT HELIX 97..124 FT /evidence="ECO:0007829|PDB:7U5L" FT HELIX 128..137 FT /evidence="ECO:0007829|PDB:7U5L" FT HELIX 139..159 FT /evidence="ECO:0007829|PDB:7U5L" FT TURN 160..163 FT /evidence="ECO:0007829|PDB:7U5L" FT HELIX 165..174 FT /evidence="ECO:0007829|PDB:7U5L" SQ SEQUENCE 181 AA; 21052 MW; 0B46AEC6381CCAE4 CRC64; MTTASPSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS HEEREHAERL MKLQNQRGGR IFLQDIKKPD RDDWENGLTA MECALCLERS VNQSLLELHK LATEKNDPHL CDFIETHYLN EQVEAIKELG DHITNLRKMG APGSGMAEYL FDKHTLGHSE S //