FRIH_PIG
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 25-MAY-2022, entry version 128.
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 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 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 -!- 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 -!- 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 (By similarity). {ECO:0000250}.
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}.
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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.ENSSSCP00000026601; -.
DR PeptideAtlas; P19130; -.
DR PRIDE; P19130; -.
DR GeneID; 397030; -.
DR KEGG; ssc:397030; -.
DR CTD; 2495; -.
DR eggNOG; KOG2332; Eukaryota.
DR InParanoid; P19130; -.
DR OrthoDB; 1249457at2759; -.
DR ChiTaRS; FTH1; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 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; 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
