ID FRIHB_XENLA Reviewed; 176 AA. AC P17663; B7ZS33; Q66LL5; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 2. DT 04-NOV-2026, entry version 124. DE RecName: Full=Ferritin heavy chain B; DE Short=Ferritin H subunit B; DE EC=1.16.3.1 {ECO:0000250|UniProtKB:P02794}; DE AltName: Full=Ferritin heavy chain 1; GN Name=fth1-b; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2336402; DOI=10.1093/nar/18.8.2184; RA Moskaitis J.E., Pastori R.L., Schoenberg D.; RT "Sequence of Xenopus laevis ferritin mRNA."; RL Nucleic Acids Res. 18:2184-2184(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=1993207; DOI=10.1021/bi00221a033; RA Holland L.J., Wall A.A., Bhattacharya A.; RT "Xenopus liver ferritin H subunit: cDNA sequence and mRNA production in the RT liver following estrogen treatment."; RL Biochemistry 30:1965-1972(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo, and Tail bud; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form. CC Important for iron homeostasis. Has ferroxidase activity. Iron is taken CC up in the ferrous form and deposited as ferric hydroxides after CC oxidation. {ECO:0000250|UniProtKB:P02794}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(2+) + O2 + 4 H(+) = 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 functional molecule is roughly CC spherical and contains a central cavity into which the insoluble CC mineral iron core is deposited. {ECO:0000250|UniProtKB:P02794}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19130}. CC -!- MISCELLANEOUS: There are three types of ferritin subunits in amphibia: CC L, M and H chains. M and H chains are fast mineralizing; the L chain is CC very slow mineralizing (By similarity). {ECO:0000250}. 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; X51395; CAA35760.1; -; mRNA. DR EMBL; M55010; AAA49708.1; -; mRNA. DR EMBL; BC044961; AAH44961.1; -; mRNA. DR EMBL; BC170380; AAI70380.1; -; mRNA. DR EMBL; BC170382; AAI70382.1; -; mRNA. DR PIR; A37959; FRXL. DR AlphaFoldDB; P17663; -. DR SMR; P17663; -. DR DNASU; 379267; -. DR GeneID; 379267; -. DR KEGG; xla:379267; -. DR AGR; Xenbase:XB-GENE-6256345; -. DR CTD; 379267; -. DR Xenbase; XB-GENE-6256345; fth1.S. DR OMA; AANHDDA; -. DR OrthoDB; 186462at2759; -. DR Proteomes; UP000186698; Chromosome 7S. DR Bgee; 379267; Expressed in intestine and 19 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:InterPro. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR GO; GO:0110076; P:negative regulation of ferroptosis; ISS:UniProtKB. DR CDD; cd01056; Euk_Ferritin; 1. DR FunFam; 1.20.1260.10:FF:000002; Ferritin, mitochondrial; 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:SF54; FERRITIN; 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 Cytoplasm; Iron; Iron storage; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1..176 FT /note="Ferritin heavy chain B" FT /id="PRO_0000201077" FT DOMAIN 7..156 FT /note="Ferritin-like diiron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 24 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 59 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 59 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 62 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 104 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 138 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT CONFLICT 6 FT /note="R -> L (in Ref. 1; CAA35760)" FT /evidence="ECO:0000305" FT CONFLICT 15 FT /note="A -> I (in Ref. 1; CAA35760)" FT /evidence="ECO:0000305" FT CONFLICT 157..158 FT /note="VP -> A (in Ref. 1; CAA35760)" FT /evidence="ECO:0000305" SQ SEQUENCE 176 AA; 20563 MW; C325E410FB3EC648 CRC64; MQSQVRQNFN SDCEAAINRM VNLEMYASYV YLSMSYYFDR DDVALHHVAK FFKEQSHEER EHAEKFLKYQ NKRGGRVVLQ DIKKPERDEW SNTLEAMQAA LQLEKTVNQA LLDLHKLASD KVDPQLCDFL ESEYLEEQVK AMKELGDYIT NLKRLGVPQN GMGEYLFDKH TLGESS //