ID A0A1I8HJB0_9PLAT Unreviewed; 189 AA.
AC A0A1I8HJB0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE EC=1.16.3.1 {ECO:0000256|RuleBase:RU361145};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0006432-snap-gene-0.5-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0006432-snap-gene-0.5-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025111}.
CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form.
CC Important for iron homeostasis. Iron is taken up in the ferrous form
CC and deposited as ferric hydroxides after oxidation.
CC {ECO:0000256|RuleBase:RU361145}.
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:0000256|ARBA:ARBA00001830,
CC ECO:0000256|RuleBase:RU361145};
CC -!- SIMILARITY: Belongs to the ferritin family.
CC {ECO:0000256|ARBA:ARBA00007513, ECO:0000256|RuleBase:RU361145}.
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DR AlphaFoldDB; A0A1I8HJB0; -.
DR WBParaSite; maker-uti_cns_0006432-snap-gene-0.5-mRNA-1; maker-uti_cns_0006432-snap-gene-0.5-mRNA-1; maker-uti_cns_0006432-snap-gene-0.5.
DR Proteomes; UP000095280; Unplaced.
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:intracellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
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:SF75; FERRITIN; 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 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361145};
KW Iron storage {ECO:0000256|ARBA:ARBA00022434,
KW ECO:0000256|RuleBase:RU361145};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361145};
KW Oxidoreductase {ECO:0000256|RuleBase:RU361145};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..189
FT /note="Ferritin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009320246"
FT DOMAIN 31..176
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
SQ SEQUENCE 189 AA; 21608 MW; E6596C5BC6030286 CRC64;
MARFSLLSAI LLHLVVVSMQ QGDDETLDIR QRFGSSSVSM INDQIQREFN AMYLYESMAS
YFGRPSVGLP GFKKFLKKAA NKERERAHKL IDYLNMRGGH VRLKPITFEW FSAFDAAETA
LGAEKNITQE LYRLRDRADM ESDPHLVDFI ESEFLTEQVT SIRDLRELIA RLNKAGSGLG
ELIVDKELN
//
