ID FRIH_CANLF Reviewed; 183 AA. AC Q95MP7; Q53VC0; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 133. 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 Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Jeoung D., Jung D., Kim H.; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver, and Spleen; RX PubMed=16040348; DOI=10.1080/10425170400024359; RA Orino K., Miura T., Muto S., Watanabe K.; RT "Sequence analysis of canine and equine ferritin H and L subunit cDNAs."; RL DNA Seq. 16:58-64(2005). 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; AF285177; AAK82992.1; -; mRNA. DR EMBL; AB175610; BAD96175.1; -; mRNA. DR EMBL; AB175611; BAD96176.1; -; mRNA. DR RefSeq; NP_001003080.1; NM_001003080.1. DR RefSeq; NP_001180585.1; NM_001193656.1. DR AlphaFoldDB; Q95MP7; -. DR SMR; Q95MP7; -. DR STRING; 9615.ENSCAFP00000023396; -. DR PaxDb; 9612-ENSCAFP00000023396; -. DR Ensembl; ENSCAFT00030008420.1; ENSCAFP00030007395.1; ENSCAFG00030004568.1. DR Ensembl; ENSCAFT00040038564.1; ENSCAFP00040033637.1; ENSCAFG00040020799.1. DR Ensembl; ENSCAFT00805015422; ENSCAFP00805012074; ENSCAFG00805008422. DR Ensembl; ENSCAFT00805040226; ENSCAFP00805031449; ENSCAFG00805022326. DR GeneID; 100499480; -. DR GeneID; 403631; -. DR KEGG; cfa:403631; -. DR CTD; 2495; -. DR eggNOG; KOG2332; Eukaryota. DR HOGENOM; CLU_065681_4_0_1; -. DR InParanoid; Q95MP7; -. DR OMA; QKYSDEC; -. DR OrthoDB; 4611704at2759; -. DR TreeFam; TF313885; -. DR Reactome; R-CFA-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-CFA-6798695; Neutrophil degranulation. DR Reactome; R-CFA-917937; Iron uptake and transport. DR Proteomes; UP000002254; Unplaced. DR Proteomes; UP000694429; Chromosome 18. DR Proteomes; UP000694542; Chromosome 18. DR Proteomes; UP000805418; Unplaced. DR Bgee; ENSCAFG00000015901; Expressed in granulocyte and 47 other cell types or tissues. 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 2: Evidence at transcript level; KW Acetylation; Cytoplasm; Iron; Iron storage; Metal-binding; Oxidoreductase; KW Phosphoprotein; Reference proteome. FT CHAIN 1..183 FT /note="Ferritin heavy chain" FT /id="PRO_0000424469" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000250|UniProtKB:P02794" FT CHAIN 2..183 FT /note="Ferritin heavy chain, N-terminally processed" FT /id="PRO_0000201046" 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 MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02794" SQ SEQUENCE 183 AA; 21308 MW; 9D22750A1AC4BE72 CRC64; MTTASPSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWENGLNA MECALHLEKS VNQSLLELHK LATDKNDPHL CDFIETHYLN EQVKSIKELG DHVTNLRKMG APESGMAEYL FDKHTLGNSD NES //