ID   FRIM_SALSA              Reviewed;         176 AA.
AC   P49947;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-NOV-2023, entry version 93.
DE   RecName: Full=Ferritin, middle subunit;
DE            Short=Ferritin M;
DE            EC=1.16.3.1;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7773334;
RA   Andersen O., Dehli A., Standal H., Giskegjerde T.A., Karstensen R.,
RA   Roervik K.A.;
RT   "Two ferritin subunits of Atlantic salmon (Salmo salar): cloning of the
RT   liver cDNAs and antibody preparation.";
RL   Mol. Mar. Biol. Biotechnol. 4:164-170(1995).
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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC         Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC   -!- SUBUNIT: Oligomer of 24 subunits. There are at least two types of
CC       subunits. The functional molecule forms a roughly spherical shell with
CC       a diameter of 12 nm and contains a central cavity into which the
CC       insoluble mineral iron core is deposited.
CC   -!- TISSUE SPECIFICITY: Almost exclusively in the gonads.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   EMBL; S77386; AAB34576.1; -; mRNA.
DR   RefSeq; NP_001117130.1; NM_001123658.1.
DR   AlphaFoldDB; P49947; -.
DR   SMR; P49947; -.
DR   STRING; 8030.ENSSSAP00000009545; -.
DR   PaxDb; 8030-ENSSSAP00000009545; -.
DR   GeneID; 100136565; -.
DR   KEGG; sasa:100136565; -.
DR   OrthoDB; 4046447at2759; -.
DR   Proteomes; UP000087266; Unplaced.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
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; IPR014034; Ferritin_CS.
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; PS00204; FERRITIN_2; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Iron; Iron storage; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..176
FT                   /note="Ferritin, middle subunit"
FT                   /id="PRO_0000201076"
FT   DOMAIN          7..156
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         24
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         59
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         59
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         62
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         104
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         138
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   176 AA;  20528 MW;  27E8CDC3808F28DE CRC64;
     MESQIRQNYH HDCERAINRM INMEMFASYT YTSMAFYFSR DDVALPGFAH FFKENSEEER
     EHADKLLSFQ NKRGGRILLQ DIKKPERDEW GNGLEAMQCA LQLEKNVNQA LLDLHKIASD
     KVDPHLCDFL ETHYLNEQVE AIKKLGDHIT NLTKMDAVKN KMAEYLFDKH TLGGQS
//