ID   A0A2U9CPE9_SCOMX        Unreviewed;       142 AA.
AC   A0A2U9CPE9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
GN   ORFNames=SMAX5B_006249 {ECO:0000313|EMBL:AWP18417.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP18417.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP18417.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form.
CC       Important for iron homeostasis. Has ferroxidase activity. Iron is taken
CC       up in the ferrous form and deposited as ferric hydroxides after
CC       oxidation. {ECO:0000256|ARBA:ARBA00025111}.
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.
CC       {ECO:0000256|RuleBase:RU361145}.
CC   -!- SIMILARITY: Belongs to the ferritin family.
CC       {ECO:0000256|ARBA:ARBA00007513, ECO:0000256|RuleBase:RU361145}.
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DR   EMBL; CP026261; AWP18417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9CPE9; -.
DR   STRING; 52904.ENSSMAP00000029398; -.
DR   Proteomes; UP000246464; Chromosome 19.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   CDD; cd01056; Euk_Ferritin; 1.
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; IPR008331; Ferritin_DPS_dom.
DR   PANTHER; PTHR11431; FERRITIN; 1.
DR   PANTHER; PTHR11431:SF54; FERRITIN; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361145};
KW   Iron storage {ECO:0000256|ARBA:ARBA00022434,
KW   ECO:0000256|RuleBase:RU361145};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361145};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT   DOMAIN          19..142
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000259|PROSITE:PS50905"
SQ   SEQUENCE   142 AA;  16783 MW;  1B87E884F5D929A0 CRC64;
     MTVRNEHGFY KNWTKLLITV DRQKLQLFSN YYHVQENFPH GFSFSHAFYF SRDDVALPGF
     SHFFKENSEE EREHADKLLS FQNNRGGRIF LQDVKKPERD EWGSGLEAMQ CALQLEKNVN
     QALLDLHKLA SEDVDPHTRH EL
//