ID   FRIH_ANAPL              Reviewed;         181 AA.
AC   P80145; L7XWS8;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2023, sequence version 2.
DT   02-SEP-2026, entry version 90.
DE   RecName: Full=Ferritin heavy chain {ECO:0000303|PubMed:24981929};
DE            Short=Ferritin H subunit;
DE            EC=1.16.3.1 {ECO:0000250|UniProtKB:P02794};
DE   AltName: Full=Prosome-like particle {ECO:0000303|PubMed:1499559};
DE            Short=PLP {ECO:0000303|PubMed:1499559};
DE   AltName: Full=RNP particle {ECO:0000303|PubMed:1499559};
GN   Name=FTH1 {ECO:0000303|PubMed:24981929};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839;
RN   [1] {ECO:0000312|EMBL:AGD91914.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=24981929; DOI=10.1007/s11033-014-3503-0;
RA   Xu Q., Chen Y., Zhang Y., Tong Y.Y., Huang Z.Y., Zhao W.M., Duan X.J.,
RA   Li X., Chang G.B., Chen G.H.;
RT   "Molecular cloning and expression analysis of ferritin, heavy polypeptide 1
RT   gene from duck (Anas platyrhynchos).";
RL   Mol. Biol. Rep. 41:6233-6240(2014).
RN   [2]
RP   PROTEIN SEQUENCE OF 109-118 AND 159-181, AND TISSUE SPECIFICITY.
RC   TISSUE=Erythroblast;
RX   PubMed=1499559; DOI=10.1111/j.1432-1033.1992.tb17113.x;
RA   Coux O., Camoin L., Nothwang H.-G., Bey F., Silva-Pereira I., Keith G.,
RA   Strosberg A.-D., Scherrer K.;
RT   "The protein of M(r) 21,000 constituting the prosome-like particle of duck
RT   erythroblasts is homologous to apoferritin.";
RL   Eur. J. Biochem. 207:823-832(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. Delivery to
CC       lysosomes is mediated by the cargo receptor NCOA4 for autophagic
CC       degradation and release of iron (By similarity).
CC       {ECO:0000250|UniProtKB:P02794}.
CC   -!- FUNCTION: Inhibits translation of various mRNA species in vitro.
CC       Associates with a 35S prosome-like particle that contains non-
CC       translated mRNAs in a complex with proteins. May be involved in pre-
CC       translational regulation of some mRNA. {ECO:0000269|PubMed:1499559}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(2+) + O2 + 4 H(+) = 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:P02794}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19130}.
CC       Lysosome {ECO:0000250|UniProtKB:P02794}. Cytoplasmic vesicle,
CC       autophagosome {ECO:0000250|UniProtKB:P02794}.
CC   -!- TISSUE SPECIFICITY: Expressed in erythroblasts (at protein level)
CC       (PubMed:1499559). Expressed in heart, liver, spleen, lung, kidney,
CC       large intestine, small intestine, muscle, glandular stomach, ovary and
CC       oviduct (PubMed:24981929). {ECO:0000269|PubMed:1499559,
CC       ECO:0000269|PubMed:24981929}.
CC   -!- INDUCTION: By duck hepatitis virus type I (DHV-1) (PubMed:24981929). By
CC       polyinosinic:polycytidylic acid (poly I:C) which mimicks viral double-
CC       stranded RNA (PubMed:1499559). {ECO:0000269|PubMed:1499559,
CC       ECO:0000269|PubMed:24981929}.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   EMBL; KC117386; AGD91914.1; -; mRNA.
DR   PIR; S24135; S24135.
DR   RefSeq; NP_001297306.1; NM_001310377.1.
DR   AlphaFoldDB; P80145; -.
DR   SMR; P80145; -.
DR   Ensembl; ENSAPLT00020007285; ENSAPLP00020006780; ENSAPLG00020004941.
DR   GeneID; 101798267; -.
DR   KEGG; apla:101798267; -.
DR   CTD; 2495; -.
DR   OrthoDB; 186462at2759; -.
DR   GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:TreeGrafter.
DR   GO; GO:0004322; F:ferroxidase activity; ISS:UniProtKB.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:InterPro.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   GO; GO:0110076; P:negative regulation of ferroptosis; ISS:UniProtKB.
DR   CDD; cd01056; Euk_Ferritin; 1.
DR   FunFam; 1.20.1260.10:FF:000024; Ferritin heavy chain; 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.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Iron;
KW   Iron storage; Lysosome; Metal-binding; Oxidoreductase; RNA-binding.
FT   CHAIN           1..181
FT                   /note="Ferritin heavy chain"
FT                   /id="PRO_0000201056"
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"
FT   CONFLICT        180..181
FT                   /note="ES -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   181 AA;  21232 MW;  FB0CC1420D209BA0 CRC64;
     MATPLSQVRQ NYHQDCEAAV NRQINLELYA SYVYLSMSYY FDRDDVALKN FAKYFLHQSH
     EEREHAEKLM KLQNQRGGRI FLQDIKKPDR DDWENGLTAM ECALHLEKNV NQSLLELHKL
     ATEKNDPHLC DFIETHYLDE QVKAIKELGD HVTNLRKMGA PKYGMAEYLF DKHTLGHSDE
     S
//