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Database: UniProt
Entry: A0A1I7W9I9_HETBA
LinkDB: A0A1I7W9I9_HETBA
Original site: A0A1I7W9I9_HETBA 
ID   A0A1I7W9I9_HETBA        Unreviewed;       236 AA.
AC   A0A1I7W9I9;
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   Heterorhabditis bacteriophora (Entomopathogenic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Heterorhabditidae;
OC   Heterorhabditis.
OX   NCBI_TaxID=37862 {ECO:0000313|Proteomes:UP000095283, ECO:0000313|WBParaSite:Hba_01320};
RN   [1] {ECO:0000313|WBParaSite:Hba_01320}
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. 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; A0A1I7W9I9; -.
DR   WBParaSite; Hba_01320; Hba_01320; Hba_01320.
DR   Proteomes; UP000095283; 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   PANTHER; PTHR11431; FERRITIN; 1.
DR   PANTHER; PTHR11431:SF75; FERRITIN; 1.
DR   Pfam; PF00210; Ferritin; 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}.
FT   DOMAIN          76..232
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000259|PROSITE:PS50905"
SQ   SEQUENCE   236 AA;  27595 MW;  28DDF0BD6DB9FCB2 CRC64;
     MLLAPNFKFI PYFSGTTQIN NIHHVLTILT PESECFHPPL ARNVIPVCFC FADFVYSRST
     IENLFYILSM FAAYFSQNVR LSENRRITVV NIELYASYVY LSMSFYFDRD DVALPNISKF
     SISNSRWFRK QSDEEREHAI HLMKFQNTRG GRVMLQAVNK PEKDEWGTAL DAFKAALALE
     KFNNQSLLEL HSLASTNNDA HMSDFLEEKY LNEQKLHTLL HVYTIIRINQ IIEYQL
//
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