ID B3RTK1_TRIAD Unreviewed; 172 AA.
AC B3RTK1;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE EC=1.16.3.1 {ECO:0000256|RuleBase:RU361145};
GN ORFNames=TRIADDRAFT_37648 {ECO:0000313|EMBL:EDV26143.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV26143.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV26143.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV26143.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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 EMBL; DS985244; EDV26143.1; -; Genomic_DNA.
DR RefSeq; XP_002112176.1; XM_002112140.1.
DR AlphaFoldDB; B3RTK1; -.
DR STRING; 10228.B3RTK1; -.
DR EnsemblMetazoa; TriadT37648; TriadP37648; TriadG37648.
DR GeneID; 6752893; -.
DR KEGG; tad:TRIADDRAFT_37648; -.
DR CTD; 6752893; -.
DR eggNOG; KOG2332; Eukaryota.
DR HOGENOM; CLU_065681_4_0_1; -.
DR InParanoid; B3RTK1; -.
DR OMA; PEPLPCF; -.
DR OrthoDB; 4611704at2759; -.
DR PhylomeDB; B3RTK1; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
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:UP000009022}.
FT DOMAIN 7..156
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
SQ SEQUENCE 172 AA; 19841 MW; E68BCFACCDF791FB CRC64;
MASNARQNYH EDCEAGVNKQ INLELYASYV YLSMAYYFDR DDVSLPNFHK YFKKASYEER
EHAEKLLELQ NTRGGRIVLQ DIKRPERDEW GSCSDAMSAA LALEKYVNQA LLDLHSVAER
HNDSQLCDFL EGNYLQEQVT AIKEIADYVA QLKRVGQGLG EYQFDRLTLG SQ
//
