ID   FRI1_AQUCT              Reviewed;         176 AA.
AC   P07229;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Ferritin, higher subunit;
DE            Short=Ferritin H;
DE            EC=1.16.3.1;
OS   Aquarana catesbeiana (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Aquarana.
OX   NCBI_TaxID=8400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3495534; DOI=10.1016/s0021-9258(18)47653-3;
RA   Dickey L.F., Sreedharan S., Theil E.C., Didsbury J.R., Wang Y.-H.,
RA   Kaufman R.E.;
RT   "Differences in the regulation of messenger RNA for housekeeping and
RT   specialized-cell ferritin. A comparison of three distinct ferritin
RT   complementary DNAs, the corresponding subunits, and identification of the
RT   first processed in amphibia.";
RL   J. Biol. Chem. 262:7901-7907(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Erythrocyte;
RX   PubMed=3484480; DOI=10.1016/s0021-9258(17)36189-6;
RA   Didsbury J.R., Theil E.C., Kaufman R.E., Dickey L.F.;
RT   "Multiple red cell ferritin mRNAs, which code for an abundant protein in
RT   the embryonic cell type, analyzed by cDNA sequence and by primer extension
RT   of the 5'-untranslated regions.";
RL   J. Biol. Chem. 261:949-955(1986).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT GLN-84, FUNCTION, AND
RP   MUTAGENESIS OF LEU-135.
RX   PubMed=9668036; DOI=10.1074/jbc.273.30.18685;
RA   Takagi H., Shi D., Ha Y., Allewell N.M., Theil E.C.;
RT   "Localized unfolding at the junction of three ferritin subunits. A
RT   mechanism for iron release?";
RL   J. Biol. Chem. 273:18685-18688(1998).
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:0000269|PubMed:9668036}.
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.
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.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   EMBL; M15655; AAA49523.1; -; mRNA.
DR   EMBL; M12120; AAA49532.1; -; mRNA.
DR   PIR; A25627; FRFGL.
DR   PIR; A27805; A27805.
DR   PDB; 1BG7; X-ray; 1.85 A; A=1-176.
DR   PDBsum; 1BG7; -.
DR   AlphaFoldDB; P07229; -.
DR   SMR; P07229; -.
DR   SABIO-RK; P07229; -.
DR   EvolutionaryTrace; P07229; -.
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   1: Evidence at protein level;
KW   3D-structure; Iron; Iron storage; Metal-binding; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..176
FT                   /note="Ferritin, higher subunit"
FT                   /id="PRO_0000201072"
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         58
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
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   MUTAGEN         83
FT                   /note="K->Q: Improves crystallization."
FT   MUTAGEN         135
FT                   /note="L->P: Reduces initial rate of ferroxidation and
FT                   accelerates iron release."
FT                   /evidence="ECO:0000269|PubMed:9668036"
FT   CONFLICT        83
FT                   /note="K -> E (in Ref. 2; AAA49532)"
FT                   /evidence="ECO:0000305"
FT   HELIX           11..38
FT                   /evidence="ECO:0007829|PDB:1BG7"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:1BG7"
FT   HELIX           46..73
FT                   /evidence="ECO:0007829|PDB:1BG7"
FT   HELIX           93..113
FT                   /evidence="ECO:0007829|PDB:1BG7"
FT   HELIX           138..154
FT                   /evidence="ECO:0007829|PDB:1BG7"
FT   TURN            155..159
FT                   /evidence="ECO:0007829|PDB:1BG7"
FT   HELIX           161..170
FT                   /evidence="ECO:0007829|PDB:1BG7"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:1BG7"
SQ   SEQUENCE   176 AA;  20533 MW;  81EF7F13362ED5DE CRC64;
     MDSQVRQNFH RDCEAAINRM VNMELYASYT YLSMAFYFDR DDIALHNVAK FFKEQSHEER
     EHAEKLMKDQ NKRGGRIVLQ DVKKPERDEW GNTLEAMQAA LQLEKTVNQA LLDLHKVGSD
     KVDPHLCDFL ETEYLEEQVK SIKQLGDYIT NLKRLGLPQN GMGEYLFDKH TMGESS
//