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Database: UniProt
Entry: A0A1Y3AMC4_EURMA
LinkDB: A0A1Y3AMC4_EURMA
Original site: A0A1Y3AMC4_EURMA 
ID   A0A1Y3AMC4_EURMA        Unreviewed;       177 AA.
AC   A0A1Y3AMC4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   03-MAY-2023, entry version 14.
DE   RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE            EC=1.16.3.1 {ECO:0000256|RuleBase:RU361145};
GN   ORFNames=BLA29_002580 {ECO:0000313|EMBL:OTF69602.1};
OS   Euroglyphus maynei (Mayne's house dust mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC   Pyroglyphidae; Pyroglyphinae; Euroglyphus.
OX   NCBI_TaxID=6958 {ECO:0000313|EMBL:OTF69602.1, ECO:0000313|Proteomes:UP000194236};
RN   [1] {ECO:0000313|EMBL:OTF69602.1, ECO:0000313|Proteomes:UP000194236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arlian Lab {ECO:0000313|EMBL:OTF69602.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OTF69602.1};
RA   Arlian L.G., Morgan M.S., Rider S.D.;
RT   "Genome Survey of Euroglyphus maynei.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OTF69602.1}.
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DR   EMBL; MUJZ01069608; OTF69602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3AMC4; -.
DR   OrthoDB; 4611704at2759; -.
DR   Proteomes; UP000194236; Unassembled WGS sequence.
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; PS00540; FERRITIN_1; 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   Reference proteome {ECO:0000313|Proteomes:UP000194236}.
FT   DOMAIN          12..161
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000259|PROSITE:PS50905"
SQ   SEQUENCE   177 AA;  20505 MW;  2036BB591BECDC67 CRC64;
     MAESTKVSRV RMNFHKECED GVNKQINLEL YASYIYQQMA FHFNRDDVAL PGFEKFFDES
     SKEEREHAEK FMKLQNQRGG RIVLDDIRKP PQQDWSSGLE AIRAALELEK TVNQALLDLH
     GLAVKHDDAQ FADFIESHYL HEQVEAIKKL ADYVTNLERC GPGLGEYLFD RHTLQSS
//
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