FRIL2_MOUSE
ID FRIL2_MOUSE Reviewed; 183 AA.
AC P49945;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ferritin light chain 2;
DE AltName: Full=Ferritin L subunit 2;
DE AltName: Full=Ferritin subunit LG;
GN Name=Ftl2; Synonyms=Ftl-2;
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 [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Bone marrow;
RX PubMed=1543909; DOI=10.1007/bf00302872;
RA Renaudie F., Yachou A.K., Grandchamp B., Jones R., Beaumont C.;
RT "A second ferritin L subunit is encoded by an intronless gene in the
RT mouse.";
RL Mamm. Genome 2:143-149(1992).
RN [2]
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).
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; M73706; AAB00809.1; -; Genomic_DNA.
DR AlphaFoldDB; P49945; -.
DR SMR; P49945; -.
DR SwissPalm; P49945; -.
DR jPOST; P49945; -.
DR MaxQB; P49945; -.
DR PeptideAtlas; P49945; -.
DR PRIDE; P49945; -.
DR ProteomicsDB; 267501; -.
DR MGI; MGI:95590; Ftl2.
DR InParanoid; P49945; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR PRO; PR:P49945; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P49945; protein.
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 3: Inferred from homology;
KW Iron; Iron storage; Metal-binding; Reference proteome.
FT CHAIN 1..183
FT /note="Ferritin light chain 2"
FT /id="PRO_0000201062"
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"
SQ SEQUENCE 183 AA; 20843 MW; D4A0A4789A0AC451 CRC64;
MTSQIRQNYS TEVEAAVNRL VNLHLRASYT YLSLGFFFDR DDVALEGVGH FFRELAEEKR
EGAERLLKLQ NERGGRALFQ DVQKPSQDEW GKTLEAIQAA LRLEKNLNQA LLDLHALGSA
RTDPHLCDFL ESHFLDKEVK LIKKMGNHLT NLRRVAGPQP VQTGVAQASL GEYLFERLTL
KHD
