FRIML_TREBE
ID FRIML_TREBE Reviewed; 176 AA.
AC P85836;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Ferritin, liver middle subunit {ECO:0000303|PubMed:18625196};
DE Short=Ferritin M {ECO:0000303|PubMed:18625196};
DE EC=1.16.3.1;
OS Trematomus bernacchii (Emerald rockcod) (Pseudotrematomus bernacchii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Trematomus.
OX NCBI_TaxID=40690;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Liver {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 -!- SUBUNIT: In liver, forms a heteromer consisting of middle and heavy
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. {ECO:0000269|PubMed:18625196,
CC ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Liver (at protein level).
CC {ECO:0000269|PubMed:18625196}.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P85836; -.
DR SMR; P85836; -.
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: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 Oxidoreductase.
FT CHAIN 1..176
FT /note="Ferritin, liver middle subunit"
FT /id="PRO_0000352782"
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; 20436 MW; A61829EF2564AC4B CRC64;
MDSQVRQNYH RDCEAAVNRM INMELFASYS YTSMAFYFSR DDVALPGFAH FFKENSDEER
EHADKLLTFQ NSRGGRIFLQ DIKKPERDEW GSGLDALQSS LQLEKNVNQA LLDLHKIASD
HTDPHMCDFL ETHYLNEQVE SIKKLGDFIT NLSRMDAVKN KMAEYLFDKH TMGGKN