ID   FRIM_TRENE              Reviewed;         176 AA.
AC   P85835;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-MAY-2023, entry version 39.
DE   RecName: Full=Ferritin, middle subunit {ECO:0000303|PubMed:18625196};
DE            Short=Ferritin M {ECO:0000303|PubMed:18625196};
DE            EC=1.16.3.1;
OS   Trematomus newnesi (Dusky notothen).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Trematomus.
OX   NCBI_TaxID=35730;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver {ECO:0000269|PubMed:18625196}, and Spleen
RC   {ECO:0000269|PubMed:18625196};
RX   PubMed=18625196; DOI=10.1016/j.abb.2008.06.022;
RA   Giorgi A., Mignogna G., Bellapadrona G., Gattoni M., Chiaraluce R.,
RA   Consalvi V., Chiancone E., Stefanini S.;
RT   "The unusual co-assembly of H- and M-chains in the ferritin molecule from
RT   the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi.";
RL   Arch. Biochem. Biophys. 478:69-74(2008).
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 (By similarity). {ECO:0000250|UniProtKB:P07798}.
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         Evidence={ECO:0000269|PubMed:18625196};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable. {ECO:0000269|PubMed:18625196};
CC   -!- SUBUNIT: In liver, forms a heteromer consisting of middle and heavy
CC       subunits. In spleen, forms a homomer. The functional molecule forms a
CC       roughly spherical shell with a diameter of 12 nm and contains a central
CC       cavity into which the insoluble mineral iron core is deposited.
CC       {ECO:0000269|PubMed:18625196, ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Liver and spleen (at protein level).
CC       {ECO:0000269|PubMed:18625196}.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000255}.
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DR   AlphaFoldDB; P85835; -.
DR   SMR; P85835; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..176
FT                   /note="Ferritin, middle subunit"
FT                   /id="PRO_0000352783"
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:0000250|UniProtKB:P07798,
FT                   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:0000250|UniProtKB:P07798,
FT                   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:0000250|UniProtKB:P07798,
FT                   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:0000250|UniProtKB:P07798,
FT                   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:0000250|UniProtKB:P07798,
FT                   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:0000250|UniProtKB:P07798,
FT                   ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   176 AA;  20450 MW;  161929EF2565AC4B CRC64;
     MDSQVRQNYH RDCEAAVNRM INMELFASYS YTSMAFYFSR DDVALPGFAH FFKENSEEER
     EHADKLLTFQ NSRGGRIFLQ DIKKPERDEW GSGLDALQSS LQLEKNVNQA LLDLHKIASD
     HTDPHMCDFL ETHYLNEQVE SIKKLGDFIT NLSRMDAVKN KMAEYLFDKH TMGGKN
//