ID   FRIL_XENLA              Reviewed;         177 AA.
AC   Q7SXA5; P83458; P83459; P83461;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Ferritin light chain, oocyte isoform;
DE   AltName: Full=B-ferritin;
DE   AltName: Full=GV-LCH;
DE   AltName: Full=XeBF;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000312|EMBL:AAQ10929.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 63-70; 108-118 AND
RP   146-155.
RC   TISSUE=Oocyte {ECO:0000269|PubMed:14509834};
RX   PubMed=14509834; DOI=10.1080/1042517031000098810;
RA   Huang W.-H., Guo H.-B., Huang X.-Y., Sun F.-Z.;
RT   "Two types of new ferritin cDNA sequences from Xenopus laevis germinal
RT   vesicle oocytes.";
RL   DNA Seq. 14:211-214(2003).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Oligomer of 24 subunits. The functional molecule is roughly
CC       spherical and contains a central cavity into which the polymeric
CC       mineral iron core is deposited (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: There are three types of ferritin subunits in amphibia:
CC       L, M and H chains. M and H chains are fast mineralizing; the L chain is
CC       very slow mineralizing (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   EMBL; AF538971; AAQ10929.1; -; mRNA.
DR   AlphaFoldDB; Q7SXA5; -.
DR   SMR; Q7SXA5; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
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..177
FT                   /note="Ferritin light chain, oocyte isoform"
FT                   /id="PRO_0000201080"
FT   DOMAIN          9..158
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT                   ECO:0000305"
FT   BINDING         26
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P02794,
FT                   ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         64
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P02794,
FT                   ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         106
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P02794,
FT                   ECO:0000255|PROSITE-ProRule:PRU00085"
FT   CONFLICT        109
FT                   /note="I -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   177 AA;  20538 MW;  9D79BE23C3E25989 CRC64;
     MSAQSQIRQN YHEESEAGVN RIANLELQAS YLYLSVGYYF DRDDVALSKF SKFFRELSEK
     KRDHAEDFLK FQNKRGGRVV LQDVKKPDDD EWGNGTKAME VALNLEKSIN QAVLDLHKIA
     TDHTDPHMQD YLEHEFLEEE VKLIKKLGDH LTNLRRVKAA EEGMGEYLFD KLTLGED