FRIHA_XENLA
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 03-AUG-2022, entry version 98.
DE RecName: Full=Ferritin heavy chain A;
DE Short=Ferritin H subunit A;
DE AltName: Full=Ferritin heavy chain 2;
DE EC=1.16.3.1;
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 (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Oligomer of 24 subunits. The functional molecule is roughly
CC spherical and contains a central cavity into which the polymeric
CC mineral iron core is deposited (By similarity). {ECO:0000250}.
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 CTD; 399281; -.
DR Xenbase; XB-GENE-22064562; fth1.2.L.
DR OMA; EKIMTYM; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 399281; Expressed in neurula embryo and 19 other tissues.
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:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
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; PTHR11431; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; SSF47240; 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 Iron; Iron storage; Metal-binding; Oxidoreductase; 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