ID   A0A0N5A1Y8_PARTI        Unreviewed;       321 AA.
AC   A0A0N5A1Y8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   03-MAY-2023, entry version 21.
DE   RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE            EC=1.16.3.1 {ECO:0000256|RuleBase:RU361145};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001563400.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001563400.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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|RuleBase:RU361145};
CC   -!- SIMILARITY: Belongs to the ferritin family.
CC       {ECO:0000256|ARBA:ARBA00007513, ECO:0000256|RuleBase:RU361145}.
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DR   AlphaFoldDB; A0A0N5A1Y8; -.
DR   STRING; 131310.A0A0N5A1Y8; -.
DR   WBParaSite; PTRK_0001563400.1; PTRK_0001563400.1; PTRK_0001563400.
DR   Proteomes; UP000038045; 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; IPR008331; Ferritin_DPS_dom.
DR   InterPro; IPR010558; Ly-6-related.
DR   PANTHER; PTHR11431; FERRITIN; 1.
DR   PANTHER; PTHR11431:SF75; FERRITIN; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   Pfam; PF06579; Ly-6_related; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 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..321
FT                   /note="Ferritin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005892529"
FT   DOMAIN          154..302
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000259|PROSITE:PS50905"
SQ   SEQUENCE   321 AA;  36857 MW;  758163228BB01783 CRC64;
     MLLIFILLHT LTFLKEPILA IQCFSCASEE YEALYKKGAF NFNYKPQDFF QPRFDYACDN
     SYETTNFVPV KDCPTNCVVV LEKQFFGGIL NENRPYLYIR GCSSEVFQAG DIHSPEVQFL
     QKSKICLPLM VSQIWPHVES NEYITNKTIA SGRQFFETEV ENALNVQINN ELIASYHYLA
     LANVFAKDTV ALPGAAKFFF KQSEEETGHG RKLMDYVNKR GGTVKLLPIK PLQQNITSLS
     DALLFAQNLE KSNNSSIIEL HKIASTNNDS DLTNFLEEFY LREQIEEINM FTILYNRLQR
     FGSGVGEYFI DKELKELAEK N
//