FRIH_CANLF
ID FRIH_CANLF Reviewed; 183 AA.
AC Q95MP7; Q53VC0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jeoung D., Jung D., Kim H.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver, and Spleen;
RX PubMed=16040348; DOI=10.1080/10425170400024359;
RA Orino K., Miura T., Muto S., Watanabe K.;
RT "Sequence analysis of canine and equine ferritin H and L subunit cDNAs.";
RL DNA Seq. 16:58-64(2005).
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; AF285177; AAK82992.1; -; mRNA.
DR EMBL; AB175610; BAD96175.1; -; mRNA.
DR EMBL; AB175611; BAD96176.1; -; mRNA.
DR RefSeq; NP_001003080.1; NM_001003080.1.
DR RefSeq; NP_001180585.1; NM_001193656.1.
DR AlphaFoldDB; Q95MP7; -.
DR SMR; Q95MP7; -.
DR STRING; 9615.ENSCAFP00000023396; -.
DR PaxDb; Q95MP7; -.
DR PRIDE; Q95MP7; -.
DR Ensembl; ENSCAFT00030008420; ENSCAFP00030007395; ENSCAFG00030004568.
DR Ensembl; ENSCAFT00040038564; ENSCAFP00040033637; ENSCAFG00040020799.
DR GeneID; 100499480; -.
DR GeneID; 403631; -.
DR KEGG; cfa:403631; -.
DR CTD; 2495; -.
DR eggNOG; KOG2332; Eukaryota.
DR HOGENOM; CLU_065681_4_0_1; -.
DR InParanoid; Q95MP7; -.
DR OMA; YLSMGYF; -.
DR OrthoDB; 1249457at2759; -.
DR TreeFam; TF313885; -.
DR Reactome; R-CFA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-CFA-6798695; Neutrophil degranulation.
DR Reactome; R-CFA-917937; Iron uptake and transport.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000015901; Expressed in granulocyte and 47 other tissues.
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: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; IBA:GO_Central.
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 Acetylation; Iron; Iron storage; Metal-binding; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..183
FT /note="Ferritin heavy chain"
FT /id="PRO_0000424469"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02794"
FT CHAIN 2..183
FT /note="Ferritin heavy chain, N-terminally processed"
FT /id="PRO_0000201046"
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 MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02794"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02794"
SQ SEQUENCE 183 AA; 21308 MW; 9D22750A1AC4BE72 CRC64;
MTTASPSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS
HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWENGLNA MECALHLEKS VNQSLLELHK
LATDKNDPHL CDFIETHYLN EQVKSIKELG DHVTNLRKMG APESGMAEYL FDKHTLGNSD
NES
