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Ferritin heavy chain (Ferritin H subunit) (EC 1.16.3.1) [Cleaved into: Ferritin heavy chain, N-terminally processed]

 FRIH_RAT                Reviewed;         182 AA.
P19132;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 136.
RecName: Full=Ferritin heavy chain;
Short=Ferritin H subunit;
EC=1.16.3.1;
Contains:
RecName: Full=Ferritin heavy chain, N-terminally processed;
Name=Fth1; Synonyms=Fth;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3478702; DOI=10.1073/pnas.84.21.7438;
Murray M.T., White K., Munro H.N.;
"Conservation of ferritin heavy subunit gene structure: implications
for the regulation of ferritin gene expression.";
Proc. Natl. Acad. Sci. U.S.A. 84:7438-7442(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Liver;
Wu C.G., Groenink M., Bosma A., Reitsma P.H., van Deventer J.H.,
Chamuleau R.A.F.M.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 81-87, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 137-182.
PubMed=2827671; DOI=10.1016/0006-291X(88)90518-9;
Ursini M.V., de Franciscis V.;
"TSH regulation of ferritin H chain messenger RNA levels in the rat
thyroids.";
Biochem. Biophys. Res. Commun. 150:287-295(1988).
[5]
PROTEIN SEQUENCE OF 159-182.
TISSUE=Liver;
PubMed=6546756;
Leibold E.A., Aziz N., Brown A.J.P., Munro H.N.;
"Conservation in rat liver of light and heavy subunit sequences of
mammalian ferritin. Presence of unique octopeptide in the light
subunit.";
J. Biol. Chem. 259:4327-4334(1984).
-!- FUNCTION: Stores iron in a soluble, non-toxic, readily available
form. Important for iron homeostasis. Has ferroxidase activity.
Iron is taken up in the ferrous form and deposited as ferric
hydroxides after oxidation. Also plays a role in delivery of iron
to cells. Mediates iron uptake in capsule cells of the developing
kidney (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
-!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits:
L (light) chain and H (heavy) chain. The major chain can be light
or heavy, depending on the species and tissue type. The functional
molecule forms a roughly spherical shell with a diameter of 12 nm
and contains a central cavity into which the insoluble mineral
iron core is deposited.
-!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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EMBL; M18053; AAA41153.1; -; Genomic_DNA.
EMBL; M18051; AAA41153.1; JOINED; Genomic_DNA.
EMBL; M18052; AAA41153.1; JOINED; Genomic_DNA.
EMBL; U58829; AAB39890.1; -; mRNA.
EMBL; M29330; AAA42300.1; -; mRNA.
PIR; A39884; A39884.
RefSeq; NP_036980.1; NM_012848.2.
UniGene; Rn.109383; -.
UniGene; Rn.54447; -.
ProteinModelPortal; P19132; -.
SMR; P19132; -.
BioGrid; 247358; 1.
IntAct; P19132; 1.
MINT; MINT-4567905; -.
STRING; 10116.ENSRNOP00000037803; -.
iPTMnet; P19132; -.
PhosphoSitePlus; P19132; -.
PaxDb; P19132; -.
PRIDE; P19132; -.
GeneID; 25319; -.
KEGG; rno:25319; -.
UCSC; RGD:2635; rat.
CTD; 2495; -.
RGD; 2635; Fth1.
eggNOG; KOG2332; Eukaryota.
eggNOG; COG1528; LUCA.
HOVERGEN; HBG000410; -.
InParanoid; P19132; -.
KO; K00522; -.
PRO; PR:P19132; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0044754; C:autolysosome; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005739; C:mitochondrion; ISO:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
GO; GO:0005506; F:iron ion binding; ISO:RGD.
GO; GO:0006955; P:immune response; ISS:UniProtKB.
GO; GO:0006880; P:intracellular sequestering of iron ion; ISO:RGD.
GO; GO:0097286; P:iron ion import; ISO:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
GO; GO:0060547; P:negative regulation of necrotic cell death; IMP:RGD.
Gene3D; 1.20.1260.10; -; 1.
InterPro; IPR001519; Ferritin.
InterPro; IPR012347; Ferritin-like.
InterPro; IPR009040; Ferritin-like_diiron.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR014034; Ferritin_CS.
InterPro; IPR008331; Ferritin_DPS_dom.
PANTHER; PTHR11431; PTHR11431; 1.
Pfam; PF00210; Ferritin; 1.
SUPFAM; SSF47240; SSF47240; 1.
PROSITE; PS00540; FERRITIN_1; 1.
PROSITE; PS00204; FERRITIN_2; 1.
PROSITE; PS50905; FERRITIN_LIKE; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing; Iron;
Iron storage; Metal-binding; Oxidoreductase; Reference proteome.
CHAIN 1 182 Ferritin heavy chain.
/FTId=PRO_0000424476.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:P02794}.
CHAIN 2 182 Ferritin heavy chain, N-terminally
processed.
/FTId=PRO_0000201053.
DOMAIN 11 160 Ferritin-like diiron.
{ECO:0000255|PROSITE-ProRule:PRU00085}.
METAL 28 28 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
METAL 63 63 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
METAL 63 63 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
METAL 66 66 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
METAL 108 108 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
METAL 142 142 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P02794}.
MOD_RES 2 2 N-acetylthreonine; in Ferritin heavy
chain, N-terminally processed.
{ECO:0000250|UniProtKB:P02794}.
CONFLICT 102 102 R -> E (in Ref. 2; AAB39890).
{ECO:0000305}.
CONFLICT 182 182 S -> E (in Ref. 5; AA sequence).
{ECO:0000305}.
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


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