FRIH_CHICK
ID FRIH_CHICK Reviewed; 180 AA.
AC P08267;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ferritin heavy chain;
DE Short=Ferritin H subunit;
DE EC=1.16.3.1;
GN Name=FTH;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3600643; DOI=10.1128/mcb.7.5.1751-1758.1987;
RA Stevens P.W., Dodgson J.B., Engel J.D.;
RT "Structure and expression of the chicken ferritin H-subunit gene.";
RL Mol. Cell. Biol. 7:1751-1758(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Mikulits W., Linhartova I., Dolznig H., Propst F., Wiche G., Beug H.,
RA Muellner E.W.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
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; M16343; AAA48768.1; -; Genomic_DNA.
DR EMBL; Y14698; CAA75004.1; -; mRNA.
DR PIR; A26886; A26886.
DR RefSeq; NP_990417.1; NM_205086.1.
DR AlphaFoldDB; P08267; -.
DR SMR; P08267; -.
DR STRING; 9031.ENSGALP00000011673; -.
DR PaxDb; P08267; -.
DR Ensembl; ENSGALT00000011687; ENSGALP00000011673; ENSGALG00000007220.
DR GeneID; 395970; -.
DR KEGG; gga:395970; -.
DR CTD; 2495; -.
DR VEuPathDB; HostDB:geneid_395970; -.
DR eggNOG; KOG2332; Eukaryota.
DR GeneTree; ENSGT00950000182841; -.
DR HOGENOM; CLU_065681_4_0_1; -.
DR InParanoid; P08267; -.
DR OMA; YLSMGYF; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; P08267; -.
DR Reactome; R-GGA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR Reactome; R-GGA-917937; Iron uptake and transport.
DR PRO; PR:P08267; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000007220; Expressed in granulocyte and 13 other tissues.
DR GO; GO:0044754; C:autolysosome; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
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 INIT_MET 1
FT /note="Removed"
FT CHAIN 2..180
FT /note="Ferritin heavy chain"
FT /id="PRO_0000201057"
FT DOMAIN 10..159
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 27
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
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 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 65
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 141
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ SEQUENCE 180 AA; 21092 MW; 0A779C213E5EF35E CRC64;
MATPPSQVRQ NYHQDCEAAI NRQINLELYA SYVYLSMSYY FDRDDVALKN FAKYFLHQSH
EEREHAEKLM KLQNQRGGRI FLQDIKKPDR DDWENGLTAM ECALHLEKNV NQSLLELHKL
ATEKNDPHLC DFIETHYLDE QVKAIKQLGD HVTNLRKMGA PKYGMAEYLF DKHTLGESDS
