FRIL_RABIT
ID FRIL_RABIT Reviewed; 175 AA.
AC P09451;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ferritin light chain;
DE Short=Ferritin L subunit;
GN Name=FTL;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=3412911; DOI=10.1093/nar/16.15.7741;
RA Daniels-Mcqueen S., Ray A., Walden W.E., Ray B.K., Brown P.H., Thach R.E.;
RT "Nucleotide sequence of cDNA encoding rabbit ferritin L chain.";
RL Nucleic Acids Res. 16:7741-7741(1988).
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; X07830; CAA30682.1; -; mRNA.
DR PIR; S01239; S01239.
DR RefSeq; NP_001095158.1; NM_001101688.1.
DR AlphaFoldDB; P09451; -.
DR SMR; P09451; -.
DR STRING; 9986.ENSOCUP00000016423; -.
DR GeneID; 100009254; -.
DR KEGG; ocu:100009254; -.
DR CTD; 2512; -.
DR eggNOG; KOG2332; Eukaryota.
DR InParanoid; P09451; -.
DR OrthoDB; 1249457at2759; -.
DR Proteomes; UP000001811; Unplaced.
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 Iron; Iron storage; Metal-binding; Reference proteome.
FT CHAIN 1..175
FT /note="Ferritin light chain"
FT /id="PRO_0000201065"
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 175 AA; 20075 MW; 3B02FBF2FB6E2EB6 CRC64;
MTSQIRQNYS PEVEAAVNHL VNLHLRASYT YLSLGFYFDR DDVALEGVSH FFRELAEEKR
EAAERLLKMQ NQRGGRALFQ DVQKPSQDEW GKTLNAMEAA LALEKNLNQA LLDLHALGSA
HTDPHLCDFL ENHFLDEEVK LLKKMGDHLT NIRRLSGPQA SLGEYLFERL TLKHD