FRI1_LITCT
ID FRI1_LITCT Reviewed; 176 AA.
AC P07229;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ferritin, higher subunit;
DE Short=Ferritin H;
DE EC=1.16.3.1;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
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: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 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
