FRI3_LITCT
ID FRI3_LITCT Reviewed; 173 AA.
AC P07797;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Ferritin, lower subunit;
DE Short=Ferritin L;
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 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=7760335; DOI=10.1006/jmbi.1995.0274;
RA Trikha J., Theil E.C., Allewell N.M.;
RT "High resolution crystal structures of amphibian red-cell L ferritin:
RT potential roles for structural plasticity and solvation in function.";
RL J. Mol. Biol. 248:949-967(1995).
CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form.
CC Important for iron homeostasis. Iron is taken up in the ferrous form
CC and deposited as ferric hydroxides after oxidation.
CC {ECO:0000269|PubMed:7760335}.
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. {ECO:0000269|PubMed:7760335}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02725; AAA49524.1; -; mRNA.
DR PIR; B27805; B27805.
DR PDB; 1RCC; X-ray; 2.40 A; A=1-173.
DR PDB; 1RCD; X-ray; 2.00 A; A=1-173.
DR PDB; 1RCE; X-ray; 2.40 A; A=1-173.
DR PDB; 1RCG; X-ray; 2.20 A; A=1-173.
DR PDB; 1RCI; X-ray; 2.00 A; A=1-173.
DR PDBsum; 1RCC; -.
DR PDBsum; 1RCD; -.
DR PDBsum; 1RCE; -.
DR PDBsum; 1RCG; -.
DR PDBsum; 1RCI; -.
DR AlphaFoldDB; P07797; -.
DR SMR; P07797; -.
DR SABIO-RK; P07797; -.
DR EvolutionaryTrace; P07797; -.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
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.
FT CHAIN 1..173
FT /note="Ferritin, lower subunit"
FT /id="PRO_0000201074"
FT DOMAIN 7..156
FT /note="Ferritin-like diiron"
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 HELIX 11..38
FT /evidence="ECO:0007829|PDB:1RCD"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1RCD"
FT HELIX 46..73
FT /evidence="ECO:0007829|PDB:1RCD"
FT HELIX 93..120
FT /evidence="ECO:0007829|PDB:1RCD"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:1RCD"
FT HELIX 134..156
FT /evidence="ECO:0007829|PDB:1RCD"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:1RCD"
SQ SEQUENCE 173 AA; 19938 MW; 749CFED038F3215C CRC64;
MESQVRQNFH QDCEAGLNRT VNLKFHSSYV YLSMASYFNR DDVALSNFAK FFRERSEEEK
EHAEKLIEYQ NQRGGRVFLQ SVEKPERDDW ANGLEALQTA LKLQKSVNQA LLDLHAVAAD
KSDPHMTDFL ESPYLSESVE TIKKLGDHIT SLKKLWSSHP GMAEYLFNKH TLG
