ID   FRIH_CRIGR              Reviewed;         186 AA.
AC   P29389;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Ferritin heavy chain;
DE            Short=Ferritin H subunit;
DE            EC=1.16.3.1;
GN   Name=FTH1; Synonyms=FTH;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1380656; DOI=10.1016/0921-8777(92)90069-f;
RA   Zhu W., Keng P., Chou W.G.;
RT   "Differential gene expression in wild-type and X-ray-sensitive mutants of
RT   Chinese hamster ovary cell lines.";
RL   Mutat. Res. 274:237-245(1992).
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; M99692; AAB46388.1; -; mRNA.
DR   PIR; I48109; I48109.
DR   RefSeq; XP_007615470.1; XM_007617280.2.
DR   RefSeq; XP_007651686.1; XM_007653496.2.
DR   AlphaFoldDB; P29389; -.
DR   SMR; P29389; -.
DR   STRING; 10029.XP_007615470.1; -.
DR   Ensembl; ENSCGRT00001025594; ENSCGRP00001021350; ENSCGRG00001020220.
DR   GeneID; 100689102; -.
DR   KEGG; cge:100689102; -.
DR   CTD; 2495; -.
DR   eggNOG; KOG2332; Eukaryota.
DR   GeneTree; ENSGT00950000182841; -.
DR   OMA; YLSMGYF; -.
DR   OrthoDB; 1249457at2759; -.
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:0006955; P:immune response; ISS:UniProtKB.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
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; Phosphoprotein.
FT   CHAIN           1..186
FT                   /note="Ferritin heavy chain"
FT                   /id="PRO_0000201047"
FT   DOMAIN          16..165
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         33
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         68
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         68
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         71
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         113
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         147
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02794"
SQ   SEQUENCE   186 AA;  21486 MW;  80BE8A1662E73FC4 CRC64;
     MTTTALTTAS PSQVRQNYHQ DSEAAINRQI NLELYASYVY LSMSCYFDRD DVALKNFAKY
     FLHQSHEERE HAEKLMKLQN QRGGRIFLQD IKKPDRDDWE SGLNAMECAL HLEKSVNQSL
     LELHKLATDK NDPHLCDFIE THYLNEQVKS IKELGDHVTN LRKMGAPEAG MAEYLFDKHT
     LGHSES