ID   FRIL_PIG                Reviewed;          78 AA.
AC   P19133;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Ferritin light chain;
DE            Short=Ferritin L subunit;
DE   Flags: Fragment;
GN   Name=FTL;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Spleen;
RX   PubMed=3688879; DOI=10.1016/0003-9861(87)90475-9;
RA   Collawn J.F. Jr., Gowan L.K., Crow H., Schwabe C., Fish W.W.;
RT   "Isolation and partial amino acid sequence of three subunit species of
RT   porcine spleen ferritin: evidence of multiple H subunits.";
RL   Arch. Biochem. Biophys. 259:105-113(1987).
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   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   PIR; S06906; S06906.
DR   AlphaFoldDB; P19133; -.
DR   SMR; P19133; -.
DR   STRING; 9823.ENSSSCP00000003417; -.
DR   PaxDb; P19133; -.
DR   PeptideAtlas; P19133; -.
DR   eggNOG; KOG2332; Eukaryota.
DR   HOGENOM; CLU_065681_4_0_1; -.
DR   InParanoid; P19133; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; P19133; SS.
DR   GO; GO:0008043; C:intracellular ferritin complex; ISS:UniProtKB.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
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; PS00204; FERRITIN_2; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW   Reference proteome.
FT   CHAIN           <1..78
FT                   /note="Ferritin light chain"
FT                   /id="PRO_0000201063"
FT   DOMAIN          <1..59
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   NON_TER         1
SQ   SEQUENCE   78 AA;  8784 MW;  3436F3309ADCDC43 CRC64;
     EAALHLEKGL NQALVDLHAL GSARADPHLC DFLENHFLDE EVKLIKKMGD HLTNLRRLSG
     PQAGLGEYLF ERLTLKHD