ID FRI2_AQUCT Reviewed; 176 AA. AC P07798; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 123. DE RecName: Full=Ferritin, middle subunit; DE Short=Ferritin M; DE EC=1.16.3.1; DE AltName: Full=Ferritin H'; DE AltName: Full=Ferritin X; 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 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=10439069; DOI=10.1007/s007750050310; RA Ha Y., Shi D., Small G.W., Theil E.C., Allewell N.M.; RT "Crystal structure of bullfrog M ferritin at 2.8 A resolution: analysis of RT subunit interactions and the binuclear metal center."; RL J. Biol. Inorg. Chem. 4:243-256(1999). 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. 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}. 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; J02724; AAA49525.1; -; mRNA. DR PIR; C27805; C27805. DR PDB; 1MFR; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176. DR PDB; 3KA3; X-ray; 1.40 A; A=1-176. DR PDB; 3KA4; X-ray; 1.40 A; A=1-176. DR PDB; 3KA6; X-ray; 1.40 A; A=1-176. DR PDB; 3KA8; X-ray; 1.35 A; A=1-176. DR PDB; 3KA9; X-ray; 1.45 A; A=1-176. DR PDB; 3RBC; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176. DR PDB; 3RE7; X-ray; 2.82 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176. DR PDB; 3RGD; X-ray; 2.89 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176. DR PDB; 3SE1; X-ray; 1.65 A; A=1-176. DR PDB; 3SH6; X-ray; 1.40 A; A=1-176. DR PDB; 3SHX; X-ray; 1.35 A; A=1-176. DR PDB; 4DAS; X-ray; 2.56 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176. DR PDB; 4LPJ; X-ray; 1.27 A; A=1-176. DR PDB; 4LPM; X-ray; 1.65 A; A=2-175. DR PDB; 4LPN; X-ray; 1.66 A; A=1-176. DR PDB; 4LQH; X-ray; 1.16 A; A=1-176. DR PDB; 4LQJ; X-ray; 1.20 A; A=1-176. DR PDB; 4LQV; X-ray; 1.54 A; A=1-176. DR PDB; 4LYU; X-ray; 1.75 A; A=1-176. DR PDB; 4LYX; X-ray; 1.23 A; A=1-176. DR PDB; 4MJY; X-ray; 1.40 A; A=1-176. DR PDB; 4MKU; X-ray; 1.30 A; A=1-176. DR PDB; 4ML5; X-ray; 1.22 A; A=1-176. DR PDB; 4MN9; X-ray; 1.15 A; A=1-176. DR PDB; 4MY7; X-ray; 1.48 A; A=1-176. DR PDB; 4P18; X-ray; 1.91 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176. DR PDB; 5J8S; X-ray; 1.50 A; A=1-176. DR PDB; 5J8W; X-ray; 1.11 A; A=1-176. DR PDB; 5J93; X-ray; 1.10 A; A=1-176. DR PDB; 5J9V; X-ray; 1.16 A; A=1-176. DR PDB; 5JAC; X-ray; 1.18 A; A=1-176. DR PDB; 5XHI; X-ray; 1.26 A; A=2-175. DR PDB; 5XHM; X-ray; 1.70 A; A=2-175. DR PDB; 5XHN; X-ray; 1.63 A; A=2-175. DR PDB; 5XHO; X-ray; 1.73 A; A=2-175. DR PDB; 6I36; X-ray; 1.59 A; A=1-176. DR PDB; 6I9P; X-ray; 1.25 A; A=1-176. DR PDB; 6I9T; X-ray; 1.20 A; A=1-176. DR PDB; 6IAF; X-ray; 1.35 A; A=1-176. DR PDB; 6IAJ; X-ray; 1.62 A; A=1-176. DR PDBsum; 1MFR; -. DR PDBsum; 3KA3; -. DR PDBsum; 3KA4; -. DR PDBsum; 3KA6; -. DR PDBsum; 3KA8; -. DR PDBsum; 3KA9; -. DR PDBsum; 3RBC; -. DR PDBsum; 3RE7; -. DR PDBsum; 3RGD; -. DR PDBsum; 3SE1; -. DR PDBsum; 3SH6; -. DR PDBsum; 3SHX; -. DR PDBsum; 4DAS; -. DR PDBsum; 4LPJ; -. DR PDBsum; 4LPM; -. DR PDBsum; 4LPN; -. DR PDBsum; 4LQH; -. DR PDBsum; 4LQJ; -. DR PDBsum; 4LQV; -. DR PDBsum; 4LYU; -. DR PDBsum; 4LYX; -. DR PDBsum; 4MJY; -. DR PDBsum; 4MKU; -. DR PDBsum; 4ML5; -. DR PDBsum; 4MN9; -. DR PDBsum; 4MY7; -. DR PDBsum; 4P18; -. DR PDBsum; 5J8S; -. DR PDBsum; 5J8W; -. DR PDBsum; 5J93; -. DR PDBsum; 5J9V; -. DR PDBsum; 5JAC; -. DR PDBsum; 5XHI; -. DR PDBsum; 5XHM; -. DR PDBsum; 5XHN; -. DR PDBsum; 5XHO; -. DR PDBsum; 6I36; -. DR PDBsum; 6I9P; -. DR PDBsum; 6I9T; -. DR PDBsum; 6IAF; -. DR PDBsum; 6IAJ; -. DR AlphaFoldDB; P07798; -. DR SMR; P07798; -. DR BRENDA; 1.16.3.1; 5278. DR SABIO-RK; P07798; -. DR EvolutionaryTrace; P07798; -. 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; cd00904; 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, middle subunit" FT /id="PRO_0000201073" 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 BINDING 59 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT BINDING 59 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT BINDING 62 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT BINDING 104 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT BINDING 138 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT BINDING 141 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT HELIX 11..38 FT /evidence="ECO:0007829|PDB:5J93" FT TURN 41..43 FT /evidence="ECO:0007829|PDB:5J93" FT HELIX 46..73 FT /evidence="ECO:0007829|PDB:5J93" FT HELIX 93..120 FT /evidence="ECO:0007829|PDB:5J93" FT HELIX 124..133 FT /evidence="ECO:0007829|PDB:5J93" FT HELIX 135..154 FT /evidence="ECO:0007829|PDB:5J93" FT TURN 155..159 FT /evidence="ECO:0007829|PDB:5J93" FT HELIX 161..170 FT /evidence="ECO:0007829|PDB:5J93" SQ SEQUENCE 176 AA; 20592 MW; A9F0F5BEB8584D46 CRC64; MVSQVRQNYH SDCEAAVNRM LNLELYASYT YSSMYAFFDR DDVALHNVAE FFKEHSHEER EHAEKFMKYQ NKRGGRVVLQ DIKKPERDEW GNTLEAMQAA LQLEKTVNQA LLDLHKLATD KVDPHLCDFL ESEYLEEQVK DIKRIGDFIT NLKRLGLPEN GMGEYLFDKH SVKESS //