FRIL1_MOUSE
ID FRIL1_MOUSE Reviewed; 183 AA.
AC P29391; Q8WUQ8;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ferritin light chain 1;
DE AltName: Full=Ferritin L subunit 1;
GN Name=Ftl1; Synonyms=Ftl, Ftl-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2708374; DOI=10.1016/s0021-9258(18)83262-8;
RA Beaumont C., Dugast I., Renaudie F., Souroujon M., Grandchamp B.;
RT "Transcriptional regulation of ferritin H and L subunits in adult erythroid
RT and liver cells from the mouse. Unambiguous identification of mouse
RT ferritin subunits and in vitro formation of the ferritin shells.";
RL J. Biol. Chem. 264:7498-7504(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=7648356;
RA Renaudie F., Boulanger L., Grandchamp B., Beaumont C.;
RT "Cloning, characterization and expression of mouse ferritin L subunit
RT gene.";
RL C. R. Acad. Sci. III, Sci. Vie 318:431-437(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 106-121 AND 155-177, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP FUNCTION.
RX PubMed=19154717; DOI=10.1016/j.devcel.2008.12.002;
RA Li J.Y., Paragas N., Ned R.M., Qiu A., Viltard M., Leete T., Drexler I.R.,
RA Chen X., Sanna-Cherchi S., Mohammed F., Williams D., Lin C.S.,
RA Schmidt-Ott K.M., Andrews N.C., Barasch J.;
RT "Scara5 is a ferritin receptor mediating non-transferrin iron delivery.";
RL Dev. Cell 16:35-46(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000269|PubMed:19154717}.
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 -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; J04716; AAA37614.1; -; mRNA.
DR EMBL; L39879; AAA62259.1; -; Genomic_DNA.
DR EMBL; BC019840; AAH19840.1; -; mRNA.
DR CCDS; CCDS39952.1; -.
DR PIR; B33355; B33355.
DR PDB; 1H96; X-ray; 1.60 A; A=2-183.
DR PDB; 1LB3; X-ray; 1.21 A; A=2-183.
DR PDB; 6Z3D; X-ray; 1.70 A; A/B/C/D/E/F=1-183.
DR PDB; 6ZH5; EM; 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/Z=1-183.
DR PDB; 6ZLG; EM; 3.00 A; A/B/C/D/E/F/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-183.
DR PDB; 6ZLQ; EM; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/Z=1-183.
DR PDBsum; 1H96; -.
DR PDBsum; 1LB3; -.
DR PDBsum; 6Z3D; -.
DR PDBsum; 6ZH5; -.
DR PDBsum; 6ZLG; -.
DR PDBsum; 6ZLQ; -.
DR AlphaFoldDB; P29391; -.
DR SMR; P29391; -.
DR IntAct; P29391; 5.
DR MINT; P29391; -.
DR STRING; 10090.ENSMUSP00000088372; -.
DR iPTMnet; P29391; -.
DR MetOSite; P29391; -.
DR PhosphoSitePlus; P29391; -.
DR SwissPalm; P29391; -.
DR COMPLUYEAST-2DPAGE; P29391; -.
DR SWISS-2DPAGE; P29391; -.
DR CPTAC; non-CPTAC-3810; -.
DR EPD; P29391; -.
DR jPOST; P29391; -.
DR MaxQB; P29391; -.
DR PaxDb; P29391; -.
DR PeptideAtlas; P29391; -.
DR PRIDE; P29391; -.
DR ProteomicsDB; 267626; -.
DR MGI; MGI:95589; Ftl1.
DR eggNOG; KOG2332; Eukaryota.
DR InParanoid; P29391; -.
DR PhylomeDB; P29391; -.
DR ChiTaRS; Ftl1; mouse.
DR EvolutionaryTrace; P29391; -.
DR PRO; PR:P29391; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P29391; protein.
DR GO; GO:0044754; C:autolysosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0042802; F:identical protein binding; ISO:MGI.
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; Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW Reference proteome.
FT CHAIN 1..183
FT /note="Ferritin light chain 1"
FT /id="PRO_0000201061"
FT DOMAIN 7..156
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
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 CONFLICT 25
FT /note="L -> V (in Ref. 3; AAH19840)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="T -> A (in Ref. 3; AAH19840)"
FT /evidence="ECO:0000305"
FT HELIX 11..38
FT /evidence="ECO:0007829|PDB:1LB3"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1LB3"
FT HELIX 46..73
FT /evidence="ECO:0007829|PDB:1LB3"
FT HELIX 93..120
FT /evidence="ECO:0007829|PDB:1LB3"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:1LB3"
FT HELIX 135..155
FT /evidence="ECO:0007829|PDB:1LB3"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:1LB3"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:6ZH5"
SQ SEQUENCE 183 AA; 20802 MW; F15598CCBAAF4C0B CRC64;
MTSQIRQNYS TEVEAAVNRL VNLHLRASYT YLSLGFFFDR DDVALEGVGH FFRELAEEKR
EGAERLLEFQ NDRGGRALFQ DVQKPSQDEW GKTQEAMEAA LAMEKNLNQA LLDLHALGSA
RTDPHLCDFL ESHYLDKEVK LIKKMGNHLT NLRRVAGPQP AQTGAPQGSL GEYLFERLTL
KHD
