ID   FRIH3_XENLA             Reviewed;         177 AA.
AC   Q7SXA6; P83457; P83460; P83462; P83463;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Ferritin heavy chain, oocyte isoform;
DE            EC=1.16.3.1;
DE   AltName: Full=A-ferritin;
DE   AltName: Full=GV-HCH;
DE   AltName: Full=XeAF;
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 {ECO:0000312|EMBL:AAQ10928.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 77-83; 106-116; 144-153
RP   AND 155-177.
RC   TISSUE=Oocyte {ECO:0000269|PubMed:14509834};
RX   PubMed=14509834; DOI=10.1080/1042517031000098810;
RA   Huang W.-H., Guo H.-B., Huang X.-Y., Sun F.-Z.;
RT   "Two types of new ferritin cDNA sequences from Xenopus laevis germinal
RT   vesicle oocytes.";
RL   DNA Seq. 14:211-214(2003).
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; AF538970; AAQ10928.1; -; mRNA.
DR   AlphaFoldDB; Q7SXA6; -.
DR   SMR; Q7SXA6; -.
DR   Proteomes; UP000186698; Genome assembly.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..177
FT                   /note="Ferritin heavy chain, oocyte isoform"
FT                   /id="PRO_0000201079"
FT   DOMAIN          7..156
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT                   ECO:0000305"
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        82
FT                   /note="I -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="I -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149..150
FT                   /note="IT -> LA (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173..174
FT                   /note="GE -> W (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   177 AA;  20918 MW;  EC490899B62B0C7B CRC64;
     MNSQIRQNFH QECEAAINRQ VNMELYASYV YLSMSYYFDR DDVALKNFAK YFLHQSHEER
     EHAEKLMKMQ NQRGGRLFLQ DIKKPERDEW ANGLEALECS LQLEKNVNQS ILELHKLSTD
     HNDPHLCDFL ESHYLDEQVK SMKELGDHIT NLRRMGAPSN GLAEYLFDKH TLGEDHE