FRI2_LITCT
ID FRI2_LITCT Reviewed; 176 AA.
AC P07798;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 118.
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 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 (2.8 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: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, 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
