ID FRIH_PIG Reviewed; 181 AA. AC P19130; P19131; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 135. DE RecName: Full=Ferritin heavy chain; DE Short=Ferritin H subunit; DE EC=1.16.3.1 {ECO:0000250|UniProtKB:P02794}; DE Contains: DE RecName: Full=Ferritin heavy chain, N-terminally processed; GN Name=FTH1; Synonyms=FTH; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Hamasima N., Suzuki H., Fujii H., Ito T., Murakami Y., Yamada R., RA Yazawa T., Yasue H.; RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 102-181. RC TISSUE=Spleen; RX PubMed=3688879; DOI=10.1016/0003-9861(87)90475-9; RA Collawn J.F. Jr., Gowan L.K., Crow H., Schwabe C., Fish W.W.; RT "Isolation and partial amino acid sequence of three subunit species of RT porcine spleen ferritin: evidence of multiple H subunits."; RL Arch. Biochem. Biophys. 259:105-113(1987). RN [3] RP INTERACTION WITH CLASSICAL SWINE FEVER VIRUS PROTEIN NS4B (MICROBIAL RP INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=29844394; DOI=10.1038/s41598-018-26777-8; RA Qian G., Lv H., Lin J., Li X., Lv Q., Wang T., Zhang J., Dong W., Guo K., RA Zhang Y.; RT "FHC, an NS4B-interacting Protein, Enhances Classical Swine Fever Virus RT Propagation and Acts Positively in Viral Anti-apoptosis."; RL Sci. Rep. 8:8318-8318(2018). RN [4] RP INTERACTION WITH PCV2 ORF4 (MICROBIAL INFECTION). RX PubMed=26333394; DOI=10.1007/s12038-015-9551-3; RA Lv Q., Guo K., Wang T., Zhang C., Zhang Y.; RT "Porcine circovirus type 2 ORF4 protein binds heavy chain ferritin."; RL J. Biosci. 40:477-485(2015). RN [5] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION PCV2 ORF4 (MICROBIAL RP INFECTION). RX PubMed=27030984; DOI=10.1099/jgv.0.000472; RA Lv Q., Guo K., Zhang G., Zhang Y.; RT "The ORF4 protein of porcine circovirus type 2 antagonizes apoptosis by RT stabilizing the concentration of ferritin heavy chain through physical RT interaction."; RL J. Gen. Virol. 97:1636-1646(2016). CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form CC (By similarity). Important for iron homeostasis (By similarity). Has CC ferroxidase activity (By similarity). Iron is taken up in the ferrous CC form and deposited as ferric hydroxides after oxidation (By CC similarity). Also plays a role in delivery of iron to cells (By CC similarity). Mediates iron uptake in capsule cells of the developing CC kidney (By similarity). {ECO:0000250|UniProtKB:P02794, CC ECO:0000250|UniProtKB:P09528}. CC -!- FUNCTION: (Microbial infection) Is unable to assume its function upon CC interaction with viral proteins, thereby increasing Fe concentration in CC the cytoplasm. This would inhibit the accumulation of reactive oxygen CC in host cells, leading to reduced apoptosis and increasing the survival CC of virus infected cell. {ECO:0000269|PubMed:27030984}. 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 Evidence={ECO:0000250|UniProtKB:P02794}; 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. {ECO:0000250|UniProtKB:P09528}. CC -!- SUBUNIT: (Microbial infection) Interacts with classical swine fever CC virus protein NS4B. {ECO:0000269|PubMed:29844394}. CC -!- SUBUNIT: (Microbial infection) Interacts with Porcine circovirus 2 ORF4 CC protein. {ECO:0000269|PubMed:26333394, ECO:0000269|PubMed:27030984}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29844394}. CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D15071; BAA03666.1; -; mRNA. DR PIR; S06279; S06279. DR RefSeq; NP_999140.1; NM_213975.1. DR AlphaFoldDB; P19130; -. DR SMR; P19130; -. DR IntAct; P19130; 1. DR STRING; 9823.ENSSSCP00000044712; -. DR PaxDb; 9823-ENSSSCP00000026601; -. DR PeptideAtlas; P19130; -. DR GeneID; 397030; -. DR KEGG; ssc:397030; -. DR CTD; 2495; -. DR eggNOG; KOG2332; Eukaryota. DR InParanoid; P19130; -. DR OrthoDB; 4611704at2759; -. DR ChiTaRS; FTH1; pig. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. 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:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central. DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central. DR CDD; cd01056; Euk_Ferritin; 1. 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; FERRITIN; 1. DR PANTHER; PTHR11431:SF37; FERRITIN HEAVY CHAIN; 1. DR Pfam; PF00210; Ferritin; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00204; FERRITIN_2; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Host-virus interaction; KW Iron; Iron storage; Metal-binding; Oxidoreductase; Phosphoprotein; KW Reference proteome. FT CHAIN 1..181 FT /note="Ferritin heavy chain" FT /id="PRO_0000424475" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000250|UniProtKB:P02794" FT CHAIN 2..181 FT /note="Ferritin heavy chain, N-terminally processed" FT /id="PRO_0000201051" FT DOMAIN 11..160 FT /note="Ferritin-like diiron" 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 VARIANT 111 FT /note="V -> M" FT VARIANT 116 FT /note="L -> H" FT CONFLICT 103 FT /note="F -> C (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 107..108 FT /note="VV -> LE (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 112 FT /note="Y -> N (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 140 FT /note="H -> D (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 181 AA; 21045 MW; 8E6D9710CC57F757 CRC64; MTTSCSSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS HGGRGHAEKL MKLQTQRGAR IFLQDIMKPE RDDWENGLTA MEFALHVVKN VYQSLLELHK LATDKNDPHL CDFIETHYLH EQVKAIKELG DHITNLHRMG APEYGMAEYL FDKHTLGSSE S //