ID   FRIHA_XENLA             Reviewed;         176 AA.
AC   P49948;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Ferritin heavy chain A;
DE            Short=Ferritin H subunit A;
DE            EC=1.16.3.1 {ECO:0000250|UniProtKB:P02794};
DE   AltName: Full=Ferritin heavy chain 2;
DE   AltName: Full=XL2-17;
GN   Name=fth1-a;
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=1718317; DOI=10.1089/dna.1991.10.571;
RA   Muller J.-P., Vedel M., Monnot M.-J., Touzet N., Wegnez M.;
RT   "Molecular cloning and expression of ferritin mRNA in heavy metal-poisoned
RT   Xenopus laevis cells.";
RL   DNA Cell Biol. 10:571-579(1991).
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+) + 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 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}.
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DR   EMBL; S64727; AAB20316.1; -; mRNA.
DR   RefSeq; NP_001084057.1; NM_001090588.2.
DR   AlphaFoldDB; P49948; -.
DR   SMR; P49948; -.
DR   GeneID; 399281; -.
DR   KEGG; xla:399281; -.
DR   AGR; Xenbase:XB-GENE-22064562; -.
DR   CTD; 399281; -.
DR   Xenbase; XB-GENE-22064562; fth1.2.L.
DR   OMA; SKEANSW; -.
DR   OrthoDB; 4611704at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 399281; Expressed in neurula embryo and 19 other cell types or tissues.
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:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
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: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 A"
FT                   /id="PRO_0000201078"
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"
SQ   SEQUENCE   176 AA;  20526 MW;  A3C167469B3F3F74 CRC64;
     MQSQVRQNFH SDCEAAINRM VNMEMYASYV YLSMSYYFDR DDVALHHVAK FFKEQSHEER
     EHAEKFLKYQ NKRGGRVVLQ DIKKPERDEW GNTLEATQAA LQLEKTVNQA LLDLHKLASD
     KVDAHLCDFL ESEYLEEQVK AMKQLGDYIT NLKRLGVPQN GMGEYLFDKH TLGESS
//