ID   FRIL_FELCA              Reviewed;         175 AA.
AC   Q2MHN1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Ferritin light chain;
DE            Short=Ferritin L subunit;
GN   Name=FTL;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leukocyte;
RA   Orino K., Hirata A., Watanabe K.;
RT   "Sequence analysis of feline ferritin H and L subunit cDNAs.";
RL   Jui Seikagaku 42:7-11(2005).
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   EMBL; AB193258; BAE78406.1; -; mRNA.
DR   RefSeq; NP_001041615.1; NM_001048150.1.
DR   AlphaFoldDB; Q2MHN1; -.
DR   SMR; Q2MHN1; -.
DR   STRING; 9685.ENSFCAP00000003087; -.
DR   Ensembl; ENSFCAT00000003348; ENSFCAP00000003087; ENSFCAG00000003348.
DR   GeneID; 654515; -.
DR   KEGG; fca:654515; -.
DR   CTD; 2512; -.
DR   eggNOG; KOG2332; Eukaryota.
DR   GeneTree; ENSGT00940000153096; -.
DR   HOGENOM; CLU_065681_4_0_1; -.
DR   InParanoid; Q2MHN1; -.
DR   OMA; SQDEWGT; -.
DR   OrthoDB; 1249457at2759; -.
DR   Proteomes; UP000011712; Chromosome E2.
DR   Bgee; ENSFCAG00000003348; Expressed in adult mammalian kidney and 10 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   2: Evidence at transcript level;
KW   Acetylation; Iron; Iron storage; Metal-binding; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02791"
FT   CHAIN           2..175
FT                   /note="Ferritin light chain"
FT                   /id="PRO_0000226722"
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   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02791"
SQ   SEQUENCE   175 AA;  20103 MW;  A7FE5B7AB90EC122 CRC64;
     MSSQIRQNYS TEVEAAVNRL VNMHLRASYT YLSLGFYFDR DDVALEGVGH FFRELAEEKR
     EGAERLLKMQ NQRGGRALFL DVQKPSQDEW GKTLDAMEAA LLLEKNLNQG LLDLHALGSA
     RADPHLCDFL ENHFLDEEVK LIKKMGDHLT NLRRLSGPQA ELGEYLFERL TLKHD