FRIMS_TREBE
ID FRIMS_TREBE Reviewed; 176 AA.
AC P85839;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Ferritin, spleen middle subunit {ECO:0000303|PubMed:11895429, ECO:0000303|PubMed:18625196};
DE Short=Ferritin M {ECO:0000303|PubMed:11895429, 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, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Spleen {ECO:0000269|PubMed:11895429};
RX PubMed=11895429; DOI=10.1046/j.1432-1327.2002.02762.x;
RA Mignogna G., Chiaraluce R., Consalvi V., Cavallo S., Stefanini S.,
RA Chiancone E.;
RT "Ferritin from the spleen of the Antarctic teleost Trematomus bernacchii is
RT an M-type homopolymer.";
RL Eur. J. Biochem. 269:1600-1606(2002).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Spleen {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:11895429, ECO:0000269|PubMed:18625196};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Stable at acidic pHs. {ECO:0000269|PubMed:11895429};
CC Temperature dependence:
CC Thermostable. {ECO:0000269|PubMed:11895429};
CC -!- SUBUNIT: 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:11895429, ECO:0000269|PubMed:18625196,
CC ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Spleen (at protein level).
CC {ECO:0000269|PubMed:11895429, ECO:0000269|PubMed:18625196}.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000255}.
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DR AlphaFoldDB; P85839; -.
DR SMR; P85839; -.
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, spleen middle subunit"
FT /id="PRO_0000343460"
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; 20426 MW; 014A34B79B94411C CRC64;
MDSQVRQNYH RDCEAAVNRM INMELFASYS YTSMAFYFSR DDVALPGFAH FFKENSDEER
EHADKLLTFQ NSRGGRIFLQ DIKKPERDEW GNGVDVMQCA LQLEKNVNQA LLDLHKIASG
KVDPHMCDFL ETHYLNEQVE SIKKLGDFIT NLSRMDAVKN KMAEYLFDKH TMGGKN