FRIL_HORSE
ID FRIL_HORSE Reviewed; 175 AA.
AC P02791; Q53VB4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Ferritin light chain;
DE Short=Ferritin L subunit;
GN Name=FTL;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8357841; DOI=10.1016/0167-4781(93)90121-s;
RA Takeda S., Ohta M., Ebina S., Nagayama K.;
RT "Cloning, expression and characterization of horse L-ferritin in
RT Escherichia coli.";
RL Biochim. Biophys. Acta 1174:218-220(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leukocyte;
RX PubMed=16040348; DOI=10.1080/10425170400024359;
RA Orino K., Miura T., Muto S., Watanabe K.;
RT "Sequence analysis of canine and equine ferritin H and L subunit cDNAs.";
RL DNA Seq. 16:58-64(2005).
RN [3]
RP PROTEIN SEQUENCE OF 2-175, AND ACETYLATION AT SER-2.
RC TISSUE=Spleen;
RX PubMed=7026284; DOI=10.1016/0014-5793(81)80193-7;
RA Heusterspreute M., Crichton R.R.;
RT "Amino acid sequence of horse spleen apoferritin.";
RL FEBS Lett. 129:322-327(1981).
RN [4]
RP PROTEIN SEQUENCE OF 2-175.
RC TISSUE=Liver;
RA Mathijs J.M., Crichton R.R.;
RT "Amino acid sequence of horse liver ferritin.";
RL S. Afr. J. Sci. 80:424-426(1984).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=7432529; DOI=10.1038/288298a0;
RA Clegg G.A., Stansfield R.F.D., Bourne P.E., Harrison P.M.;
RT "Helix packing and subunit conformation in horse spleen apoferritin.";
RL Nature 288:298-300(1980).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=15299370; DOI=10.1107/s0907444994003227;
RA Precigoux G., Yariv J., Gallois B., Dautant A., Courseille C.,
RA D'Estaintot B.L.;
RT "A crystallographic study of haem binding to ferritin.";
RL Acta Crystallogr. D 50:739-743(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=9159481; DOI=10.1006/jmbi.1997.0970;
RA Hempstead P.D., Yewdall S.J., Fernie A.R., Lawson D.M., Artymiuk P.J.,
RA Rice D.W., Ford G.C., Harrison P.M.;
RT "Comparison of the three-dimensional structures of recombinant human H and
RT horse L ferritins at high resolution.";
RL J. Mol. Biol. 268:424-448(1997).
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. Also plays a role
CC in delivery of iron to cells. Mediates iron uptake in capsule cells of
CC the developing kidney (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: L
CC (light) chain and H (heavy) chain. The major chain can be light or
CC heavy, depending on the species and tissue type. The functional
CC molecule forms a roughly spherical shell with a diameter of 12 nm and
CC contains a central cavity into which the insoluble mineral iron core is
CC deposited.
CC -!- MISCELLANEOUS: In horse spleen the light chain is the major chain.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; D14523; BAA03396.1; -; mRNA.
DR EMBL; AB175617; BAD96182.1; -; mRNA.
DR PIR; S36118; FRHOL.
DR RefSeq; NP_001108012.1; NM_001114540.1.
DR PDB; 1AEW; X-ray; 1.95 A; A=2-175.
DR PDB; 1DAT; X-ray; 2.05 A; A=2-175.
DR PDB; 1GWG; X-ray; 2.01 A; A=2-175.
DR PDB; 1HRS; X-ray; 2.60 A; A=2-175.
DR PDB; 1IER; X-ray; 2.26 A; A=2-175.
DR PDB; 1IES; X-ray; 2.60 A; A/B/C/D/E/F=2-175.
DR PDB; 1XZ1; X-ray; 1.75 A; A=2-175.
DR PDB; 1XZ3; X-ray; 1.75 A; A=2-175.
DR PDB; 2G4H; X-ray; 2.00 A; A=2-175.
DR PDB; 2GYD; X-ray; 1.72 A; A=3-172.
DR PDB; 2V2I; X-ray; 2.00 A; A=2-175.
DR PDB; 2V2J; X-ray; 2.22 A; A=2-175.
DR PDB; 2V2L; X-ray; 1.90 A; A=2-175.
DR PDB; 2V2M; X-ray; 1.65 A; A=2-175.
DR PDB; 2V2N; X-ray; 1.55 A; A=2-175.
DR PDB; 2V2O; X-ray; 1.87 A; A=2-175.
DR PDB; 2V2P; X-ray; 1.15 A; A=2-175.
DR PDB; 2V2R; X-ray; 1.90 A; A=2-175.
DR PDB; 2V2S; X-ray; 1.37 A; A=2-175.
DR PDB; 2W0O; X-ray; 1.50 A; A=2-175.
DR PDB; 2Z5P; X-ray; 1.65 A; A=2-175.
DR PDB; 2Z5Q; X-ray; 2.10 A; A=2-175.
DR PDB; 2Z5R; X-ray; 2.50 A; A=2-175.
DR PDB; 2ZA6; X-ray; 1.75 A; A=1-175.
DR PDB; 2ZA7; X-ray; 1.40 A; A=5-175.
DR PDB; 2ZA8; X-ray; 1.40 A; A=9-175.
DR PDB; 2ZG7; X-ray; 1.70 A; X=2-175.
DR PDB; 2ZG8; X-ray; 1.60 A; X=2-175.
DR PDB; 2ZG9; X-ray; 1.75 A; X=2-175.
DR PDB; 2ZUR; X-ray; 1.80 A; X=2-175.
DR PDB; 3AF7; X-ray; 1.58 A; X=2-175.
DR PDB; 3AF8; X-ray; 1.66 A; X=2-175.
DR PDB; 3AF9; X-ray; 1.85 A; X=2-175.
DR PDB; 3F32; X-ray; 1.70 A; A=2-175.
DR PDB; 3F33; X-ray; 1.70 A; A=2-175.
DR PDB; 3F34; X-ray; 1.68 A; A=2-175.
DR PDB; 3F35; X-ray; 1.92 A; A=2-175.
DR PDB; 3F36; X-ray; 1.70 A; A=2-175.
DR PDB; 3F37; X-ray; 1.54 A; A=2-175.
DR PDB; 3F38; X-ray; 1.75 A; A=2-175.
DR PDB; 3F39; X-ray; 1.85 A; A=2-175.
DR PDB; 3FI6; X-ray; 1.80 A; A=2-175.
DR PDB; 3H7G; X-ray; 1.65 A; A=2-175.
DR PDB; 3NOZ; X-ray; 1.52 A; X=2-175.
DR PDB; 3NP0; X-ray; 1.48 A; X=2-175.
DR PDB; 3NP2; X-ray; 1.86 A; X=2-175.
DR PDB; 3O7R; X-ray; 1.90 A; A=2-175.
DR PDB; 3O7S; X-ray; 1.73 A; A=2-175.
DR PDB; 3RAV; X-ray; 1.90 A; A=2-175.
DR PDB; 3RD0; X-ray; 2.00 A; A=2-175.
DR PDB; 3U90; X-ray; 1.90 A; A=2-175.
DR PDB; 3WVU; X-ray; 1.92 A; A=2-175.
DR PDB; 3WVV; X-ray; 1.82 A; A=2-175.
DR PDB; 3WVW; X-ray; 2.00 A; A=2-175.
DR PDB; 4DE6; X-ray; 2.18 A; A=2-175.
DR PDB; 4V1W; EM; 4.70 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=2-175.
DR PDB; 4Z3B; X-ray; 1.42 A; A=2-175.
DR PDB; 5AXS; X-ray; 1.67 A; A=2-175.
DR PDB; 5CZU; X-ray; 1.60 A; A=2-175.
DR PDB; 5E1U; X-ray; 1.56 A; A=2-175.
DR PDB; 5E2D; X-ray; 1.87 A; A=2-175.
DR PDB; 5ERJ; X-ray; 1.45 A; A=2-175.
DR PDB; 5ERK; X-ray; 2.00 A; A=2-175.
DR PDB; 5GU0; X-ray; 1.95 A; X=2-175.
DR PDB; 5GU1; X-ray; 2.05 A; X=2-175.
DR PDB; 5GU2; X-ray; 2.12 A; X=2-175.
DR PDB; 5GU3; X-ray; 2.03 A; X=2-175.
DR PDB; 5HQO; X-ray; 1.81 A; A=2-175.
DR PDB; 5IX6; X-ray; 1.85 A; A=2-175.
DR PDB; 5LG2; X-ray; 2.22 A; A=3-173.
DR PDB; 5MIJ; X-ray; 1.49 A; A=2-175.
DR PDB; 5MIK; X-ray; 1.96 A; A=2-175.
DR PDB; 6ENV; X-ray; 1.82 A; A=2-175.
DR PDB; 6ENW; X-ray; 2.60 A; A=2-175.
DR PDB; 6FX8; X-ray; 1.80 A; A=2-175.
DR PDB; 6FX9; X-ray; 1.50 A; A=2-175.
DR PDB; 6GXJ; X-ray; 1.43 A; A=2-175.
DR PDB; 6HJT; X-ray; 1.33 A; A=2-175.
DR PDB; 6HJU; X-ray; 1.58 A; A=2-175.
DR PDB; 6JEE; X-ray; 1.30 A; A=2-175.
DR PDB; 6JEF; X-ray; 1.58 A; A=2-175.
DR PDB; 6MSX; X-ray; 1.43 A; A=2-175.
DR PDB; 6PXM; EM; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/W/X/Y=1-175.
DR PDB; 6RA8; X-ray; 2.00 A; A=2-174.
DR PDB; 6RJH; EM; 2.00 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=3-173.
DR PDB; 6TRZ; X-ray; 2.02 A; AAA=1-175.
DR PDB; 6TSS; X-ray; 2.18 A; AAA=1-175.
DR PDB; 6TSX; X-ray; 2.02 A; AAA=1-175.
DR PDB; 7BD7; X-ray; 1.50 A; A=2-173.
DR PDB; 7BOM; X-ray; 1.93 A; X=2-175.
DR PDB; 7BON; X-ray; 1.48 A; A=2-175.
DR PDB; 7EML; X-ray; 1.25 A; A=2-175.
DR PDB; 7EMM; X-ray; 1.25 A; A=2-175.
DR PDB; 7W7J; X-ray; 1.50 A; A=2-175.
DR PDBsum; 1AEW; -.
DR PDBsum; 1DAT; -.
DR PDBsum; 1GWG; -.
DR PDBsum; 1HRS; -.
DR PDBsum; 1IER; -.
DR PDBsum; 1IES; -.
DR PDBsum; 1XZ1; -.
DR PDBsum; 1XZ3; -.
DR PDBsum; 2G4H; -.
DR PDBsum; 2GYD; -.
DR PDBsum; 2V2I; -.
DR PDBsum; 2V2J; -.
DR PDBsum; 2V2L; -.
DR PDBsum; 2V2M; -.
DR PDBsum; 2V2N; -.
DR PDBsum; 2V2O; -.
DR PDBsum; 2V2P; -.
DR PDBsum; 2V2R; -.
DR PDBsum; 2V2S; -.
DR PDBsum; 2W0O; -.
DR PDBsum; 2Z5P; -.
DR PDBsum; 2Z5Q; -.
DR PDBsum; 2Z5R; -.
DR PDBsum; 2ZA6; -.
DR PDBsum; 2ZA7; -.
DR PDBsum; 2ZA8; -.
DR PDBsum; 2ZG7; -.
DR PDBsum; 2ZG8; -.
DR PDBsum; 2ZG9; -.
DR PDBsum; 2ZUR; -.
DR PDBsum; 3AF7; -.
DR PDBsum; 3AF8; -.
DR PDBsum; 3AF9; -.
DR PDBsum; 3F32; -.
DR PDBsum; 3F33; -.
DR PDBsum; 3F34; -.
DR PDBsum; 3F35; -.
DR PDBsum; 3F36; -.
DR PDBsum; 3F37; -.
DR PDBsum; 3F38; -.
DR PDBsum; 3F39; -.
DR PDBsum; 3FI6; -.
DR PDBsum; 3H7G; -.
DR PDBsum; 3NOZ; -.
DR PDBsum; 3NP0; -.
DR PDBsum; 3NP2; -.
DR PDBsum; 3O7R; -.
DR PDBsum; 3O7S; -.
DR PDBsum; 3RAV; -.
DR PDBsum; 3RD0; -.
DR PDBsum; 3U90; -.
DR PDBsum; 3WVU; -.
DR PDBsum; 3WVV; -.
DR PDBsum; 3WVW; -.
DR PDBsum; 4DE6; -.
DR PDBsum; 4V1W; -.
DR PDBsum; 4Z3B; -.
DR PDBsum; 5AXS; -.
DR PDBsum; 5CZU; -.
DR PDBsum; 5E1U; -.
DR PDBsum; 5E2D; -.
DR PDBsum; 5ERJ; -.
DR PDBsum; 5ERK; -.
DR PDBsum; 5GU0; -.
DR PDBsum; 5GU1; -.
DR PDBsum; 5GU2; -.
DR PDBsum; 5GU3; -.
DR PDBsum; 5HQO; -.
DR PDBsum; 5IX6; -.
DR PDBsum; 5LG2; -.
DR PDBsum; 5MIJ; -.
DR PDBsum; 5MIK; -.
DR PDBsum; 6ENV; -.
DR PDBsum; 6ENW; -.
DR PDBsum; 6FX8; -.
DR PDBsum; 6FX9; -.
DR PDBsum; 6GXJ; -.
DR PDBsum; 6HJT; -.
DR PDBsum; 6HJU; -.
DR PDBsum; 6JEE; -.
DR PDBsum; 6JEF; -.
DR PDBsum; 6MSX; -.
DR PDBsum; 6PXM; -.
DR PDBsum; 6RA8; -.
DR PDBsum; 6RJH; -.
DR PDBsum; 6TRZ; -.
DR PDBsum; 6TSS; -.
DR PDBsum; 6TSX; -.
DR PDBsum; 7BD7; -.
DR PDBsum; 7BOM; -.
DR PDBsum; 7BON; -.
DR PDBsum; 7EML; -.
DR PDBsum; 7EMM; -.
DR PDBsum; 7W7J; -.
DR AlphaFoldDB; P02791; -.
DR PCDDB; P02791; -.
DR SASBDB; P02791; -.
DR SMR; P02791; -.
DR STRING; 9796.ENSECAP00000045456; -.
DR ChEMBL; CHEMBL1293254; -.
DR iPTMnet; P02791; -.
DR PeptideAtlas; P02791; -.
DR PRIDE; P02791; -.
DR Ensembl; ENSECAT00000052660; ENSECAP00000045456; ENSECAG00000029371.
DR GeneID; 100051593; -.
DR KEGG; ecb:100051593; -.
DR CTD; 2512; -.
DR GeneTree; ENSGT00940000153096; -.
DR InParanoid; P02791; -.
DR OrthoDB; 1249457at2759; -.
DR EvolutionaryTrace; P02791; -.
DR Proteomes; UP000002281; Chromosome 10.
DR Bgee; ENSECAG00000029371; Expressed in blood and 23 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008043; C:intracellular ferritin complex; ISS:UniProtKB.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
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; Acetylation; Direct protein sequencing; Iron; Iron storage;
KW Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7026284, ECO:0000269|Ref.4"
FT CHAIN 2..175
FT /note="Ferritin light chain"
FT /id="PRO_0000201059"
FT DOMAIN 7..156
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT REGION 54..61
FT /note="Catalytic site for iron oxidation"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
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 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:7026284"
FT CONFLICT 94
FT /note="L -> P (in Ref. 2; BAA03396)"
FT /evidence="ECO:0000305"
FT CONFLICT 136..138
FT /note="DEE -> NEQ (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:4Z3B"
FT HELIX 11..38
FT /evidence="ECO:0007829|PDB:2V2P"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:2V2P"
FT HELIX 46..73
FT /evidence="ECO:0007829|PDB:2V2P"
FT HELIX 93..120
FT /evidence="ECO:0007829|PDB:2V2P"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:2V2P"
FT HELIX 135..158
FT /evidence="ECO:0007829|PDB:2V2P"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:2V2P"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:1DAT"
SQ SEQUENCE 175 AA; 19978 MW; 2CA54242A04CB93F CRC64;
MSSQIRQNYS TEVEAAVNRL VNLYLRASYT YLSLGFYFDR DDVALEGVCH FFRELAEEKR
EGAERLLKMQ NQRGGRALFQ DLQKPSQDEW GTTLDAMKAA IVLEKSLNQA LLDLHALGSA
QADPHLCDFL ESHFLDEEVK LIKKMGDHLT NIQRLVGSQA GLGEYLFERL TLKHD
