ID   FRIH1_SCHMA             Reviewed;         173 AA.
AC   P25319;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Ferritin-1 heavy chain;
DE            EC=1.16.3.1;
GN   Name=SCM-1;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1741011; DOI=10.1016/0166-6851(92)90221-5;
RA   Dietzel J., Hirzmann J., Preis D., Symmons P., Kunz W.;
RT   "Ferritins of Schistosoma mansoni: sequence comparison and expression in
RT   female and male worms.";
RL   Mol. Biochem. Parasitol. 50:245-254(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 (By similarity). {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. The functional molecule forms a
CC       roughly spherical shell with a diameter of 12 nm and contains a central
CC       cavity into which the insoluble mineral iron core is deposited (By
CC       similarity). {ECO:0000250}.
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; M64538; AAA29880.1; -; mRNA.
DR   PIR; B45628; B45628.
DR   RefSeq; XP_018645099.1; XM_018791779.1.
DR   AlphaFoldDB; P25319; -.
DR   SMR; P25319; -.
DR   STRING; 6183.Smp_087760.1; -.
DR   EnsemblMetazoa; Smp_087760.1; Smp_087760.1; Smp_087760.
DR   GeneID; 8355419; -.
DR   KEGG; smm:Smp_087760; -.
DR   WBParaSite; Smp_087760.1; Smp_087760.1; Smp_087760.
DR   CTD; 8355419; -.
DR   eggNOG; KOG2332; Eukaryota.
DR   HOGENOM; CLU_065681_4_0_1; -.
DR   OMA; EKIMTYM; -.
DR   OrthoDB; 1249457at2759; -.
DR   PhylomeDB; P25319; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   ExpressionAtlas; P25319; baseline and differential.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Iron; Iron storage; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..173
FT                   /note="Ferritin-1 heavy chain"
FT                   /id="PRO_0000201082"
FT   DOMAIN          6..155
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         23
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         58
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         58
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         61
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         103
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         137
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   173 AA;  20173 MW;  BDE8C72CCF5B91D0 CRC64;
     MSLCRQNYHE ECEAGVNKQI NMELYASYVY MTMAFHFNRD DVALNGFYKF FLNESEEERQ
     HAIKLMTYQN MRGGRIVLQD ISAPPQLSWN SGLHAMQDAL DLEKKVNQSL MELVAVGERH
     RDTHFCDFIN NEYLEIQVQS MKKLSDYITN LIRVGNGLGE YTFDKETLHG ESQ