ID FRIH_SHEEP Reviewed; 171 AA. AC P18685; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 08-NOV-2023, entry version 123. 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 Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=8915895; RX DOI=10.1002/(sici)1097-4547(19961015)46:2<187::aid-jnr6>3.0.co;2-d; RA Sanyal B., Polak P.E., Szuchet S.; RT "Differential expression of the heavy-chain ferritin gene in non-adhered RT and adhered oligodendrocytes."; RL J. Neurosci. Res. 46:187-197(1996). RN [2] RP PROTEIN SEQUENCE OF 72-102. RX PubMed=2472118; DOI=10.1016/0003-9861(89)90198-7; RA McKenzie R.A., Yablonski M.J., Gillespie G.Y., Theil E.C.; RT "Crosslinks between intramolecular pairs of ferritin subunits: effects on RT both H and L subunits and on immunoreactivity of sheep spleen ferritin."; RL Arch. Biochem. Biophys. 272:88-96(1989). 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; U54800; AAB19186.1; -; mRNA. DR AlphaFoldDB; P18685; -. DR SMR; P18685; -. DR STRING; 9940.ENSOARP00000018968; -. DR PaxDb; 9940-ENSOARP00000018968; -. DR eggNOG; KOG2332; Eukaryota. DR Proteomes; UP000002356; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006955; P:immune response; ISS:UniProtKB. DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. 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; 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..171 FT /note="Ferritin heavy chain" FT /id="PRO_0000424477" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000250|UniProtKB:P02794" FT CHAIN 2..171 FT /note="Ferritin heavy chain, N-terminally processed" FT /id="PRO_0000201054" 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 79 FT /note="A -> G (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 171 AA; 20063 MW; 4BA0A64EF1356379 CRC64; MTTASPSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS HEEREHAERL MKLQNQRGAR IFLQDIKKPD RDDWENGLNA MECALCLERS VNQSLLELHK LATEKNDPHL CDFIETHYLN EQVEAIKELG DHITNLRKMG ALWIGHGRVP L //