FRIH_SALSA
ID FRIH_SALSA Reviewed; 177 AA.
AC P49946;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ferritin, heavy subunit;
DE Short=Ferritin H;
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: Liver, gonads, head kidney, heart and spleen.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; S77332; AAB34575.1; -; mRNA.
DR RefSeq; NP_001117129.1; NM_001123657.1.
DR AlphaFoldDB; P49946; -.
DR SMR; P49946; -.
DR STRING; 8030.ENSSSAP00000050052; -.
DR PRIDE; P49946; -.
DR GeneID; 100136564; -.
DR KEGG; sasa:100136564; -.
DR OrthoDB; 1249457at2759; -.
DR Proteomes; UP000087266; Chromosome ssa26.
DR Bgee; ENSSSAG00000049977; Expressed in spleen and 16 other tissues.
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; PS00540; FERRITIN_1; 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..177
FT /note="Ferritin, heavy subunit"
FT /id="PRO_0000201075"
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 177 AA; 20730 MW; 09CDBCE719ADA6F4 CRC64;
MTSQVRQNFH QDCEAAINRQ INLELYASYV YLSMAYYFDR DDQALHNFAK FFKNQSHEER
EHAEKLMKVQ NQRGGRIFLQ DVKKPEKDEW GSGVEALESS LQLEKSVNQS LLDLHKVCSE
HNDPHMCDFI ETHYLDEQVK SIKELGDWVT NLRRMGAPQN GMAEYLFDKH TLGKEST