ID   FRIL_PONAB              Reviewed;         175 AA.
AC   Q5R538;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Ferritin light chain;
DE            Short=Ferritin L subunit;
GN   Name=FTL;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CR861037; CAH93128.1; -; mRNA.
DR   RefSeq; NP_001126850.1; NM_001133378.1.
DR   AlphaFoldDB; Q5R538; -.
DR   SMR; Q5R538; -.
DR   STRING; 9601.ENSPPYP00000011435; -.
DR   PRIDE; Q5R538; -.
DR   Ensembl; ENSPPYT00000011877; ENSPPYP00000011435; ENSPPYG00000010223.
DR   GeneID; 100173858; -.
DR   KEGG; pon:100173858; -.
DR   CTD; 2512; -.
DR   eggNOG; KOG2332; Eukaryota.
DR   GeneTree; ENSGT00940000153096; -.
DR   InParanoid; Q5R538; -.
DR   OrthoDB; 1249457at2759; -.
DR   Proteomes; UP000001595; Chromosome 19.
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; 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_0000201064"
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:0000250|UniProtKB:P02791"
SQ   SEQUENCE   175 AA;  20019 MW;  B7A89021EE977B04 CRC64;
     MSSQIRQNYS TDVEAAVNSL VNMYLQASYT YLSLGFYFDR DDVALEGVSH FFRELAEEKR
     EGYERLLKMQ NQRGGRALFQ DIKKPAEDEW GKTPDAMKAA MALEKKLNQA LLDLHALGSA
     HTDPHLCDFL ETHFLDEEVK LIKKMGDHLT NLHRLGGPEA GLGEYLFERL TLKHD