ID   FRIH_ANAPL              Reviewed;          32 AA.
AC   P80145;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Ferritin heavy chain;
DE            Short=Ferritin H subunit;
DE            EC=1.16.3.1;
DE   AltName: Full=Prosome-like particle;
DE            Short=PLP;
DE   AltName: Full=RNP particle;
DE   Flags: Fragments;
GN   Name=FTH;
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]
RP   PROTEIN SEQUENCE, AND FUNCTION.
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 (By similarity).
CC       {ECO:0000250}.
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+) + 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   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   PIR; S24135; S24135.
DR   AlphaFoldDB; P80145; -.
DR   SMR; P80145; -.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase; RNA-binding.
FT   CHAIN           <1..32
FT                   /note="Ferritin heavy chain"
FT                   /id="PRO_0000201056"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   32 AA;  3592 MW;  D7274FD4CB175252 CRC64;
     NVNQSLLELH GAPKYGMAEY LFDKHTLGES DN