FRIH_RAT
ID FRIH_RAT Reviewed; 182 AA.
AC P19132;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ferritin heavy chain;
DE Short=Ferritin H subunit;
DE EC=1.16.3.1;
DE Contains:
DE RecName: Full=Ferritin heavy chain, N-terminally processed;
GN Name=Fth1; Synonyms=Fth;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3478702; DOI=10.1073/pnas.84.21.7438;
RA Murray M.T., White K., Munro H.N.;
RT "Conservation of ferritin heavy subunit gene structure: implications for
RT the regulation of ferritin gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7438-7442(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RA Wu C.G., Groenink M., Bosma A., Reitsma P.H., van Deventer J.H.,
RA Chamuleau R.A.F.M.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 81-87, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 137-182.
RX PubMed=2827671; DOI=10.1016/0006-291x(88)90518-9;
RA Ursini M.V., de Franciscis V.;
RT "TSH regulation of ferritin H chain messenger RNA levels in the rat
RT thyroids.";
RL Biochem. Biophys. Res. Commun. 150:287-295(1988).
RN [5]
RP PROTEIN SEQUENCE OF 159-182.
RC TISSUE=Liver;
RX PubMed=6546756; DOI=10.1016/s0021-9258(17)43049-3;
RA Leibold E.A., Aziz N., Brown A.J.P., Munro H.N.;
RT "Conservation in rat liver of light and heavy subunit sequences of
RT mammalian ferritin. Presence of unique octopeptide in the light subunit.";
RL J. Biol. Chem. 259:4327-4334(1984).
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. Also plays a role in delivery of iron to cells. Mediates
CC iron uptake in capsule cells of the developing kidney (By similarity).
CC {ECO:0000250}.
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 two types of subunits: L
CC (light) chain and H (heavy) chain. The major chain can be light or
CC heavy, depending on the species and tissue type. The functional
CC molecule forms a roughly spherical shell with a diameter of 12 nm and
CC contains a central cavity into which the insoluble mineral iron core is
CC deposited.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; M18053; AAA41153.1; -; Genomic_DNA.
DR EMBL; M18051; AAA41153.1; JOINED; Genomic_DNA.
DR EMBL; M18052; AAA41153.1; JOINED; Genomic_DNA.
DR EMBL; U58829; AAB39890.1; -; mRNA.
DR EMBL; M29330; AAA42300.1; -; mRNA.
DR PIR; A39884; A39884.
DR RefSeq; NP_036980.1; NM_012848.2.
DR AlphaFoldDB; P19132; -.
DR SMR; P19132; -.
DR BioGRID; 247358; 1.
DR IntAct; P19132; 1.
DR STRING; 10116.ENSRNOP00000037803; -.
DR iPTMnet; P19132; -.
DR PhosphoSitePlus; P19132; -.
DR SwissPalm; P19132; -.
DR jPOST; P19132; -.
DR PaxDb; P19132; -.
DR PRIDE; P19132; -.
DR DNASU; 25319; -.
DR GeneID; 25319; -.
DR KEGG; rno:25319; -.
DR UCSC; RGD:2635; rat.
DR CTD; 2495; -.
DR RGD; 2635; Fth1.
DR eggNOG; KOG2332; Eukaryota.
DR InParanoid; P19132; -.
DR OrthoDB; 1249457at2759; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-917937; Iron uptake and transport.
DR PRO; PR:P19132; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0044754; C:autolysosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005506; F:iron ion binding; ISO:RGD.
DR GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; ISO:RGD.
DR GO; GO:0006826; P:iron ion transport; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0060547; P:negative regulation of necrotic cell death; IMP:RGD.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..182
FT /note="Ferritin heavy chain"
FT /id="PRO_0000424476"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02794"
FT CHAIN 2..182
FT /note="Ferritin heavy chain, N-terminally processed"
FT /id="PRO_0000201053"
FT DOMAIN 11..160
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 28
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 66
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 108
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02794"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Ferritin heavy chain, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P02794"
FT CONFLICT 102
FT /note="R -> E (in Ref. 2; AAB39890)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 21127 MW; F27E105373235B43 CRC64;
MTTASPSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSC YFDRDDVALK NFAKYFLHQS
HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWESGLNA MRCALHLEKS VNQSLLELHK
LATDKNDPHL CDFIETHYLN EQVKSIKELG DHVTNLRKMG APESGMAEYL FDKHTLGHGD
ES
