ID A0A1J0I2W0_CALSV Unreviewed; 170 AA. AC A0A1J0I2W0; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 14-DEC-2022, entry version 11. DE RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145}; DE EC=1.16.3.1 {ECO:0000256|RuleBase:RU361145}; OS Calanus sinicus (Copepod). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Hexanauplia; Copepoda; Calanoida; Calanidae; Calanus. OX NCBI_TaxID=114070 {ECO:0000313|EMBL:APC62655.1}; RN [1] {ECO:0000313|EMBL:APC62655.1} RP NUCLEOTIDE SEQUENCE. RA Zhou K., Sun S., Wang M., Wang S., Li C.; RT "Differences in the physiological processes of Calanus sinicus inside and RT outside the Yellow Sea Cold Water Mass."; RL J. Plankton Res. 38:551-563(2016). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KT947476; APC62655.1; -; mRNA. DR AlphaFoldDB; A0A1J0I2W0; -. 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:cellular iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. 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 Pfam; PF00210; Ferritin; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00204; FERRITIN_2; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 2: Evidence at transcript level; KW Iron {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 7..156 FT /note="Ferritin-like diiron" FT /evidence="ECO:0000259|PROSITE:PS50905" SQ SEQUENCE 170 AA; 19175 MW; 76A1794941F33706 CRC64; MTSQIRQNYH EDCEALINKQ INMEFYASYV YLSMSSFFNR DDQALHGFAA FFQKSSNEER EHGMKLMEYQ TKRGGKVVFQ DIAKPSSTEW GTPLQAMEAA LELEKTVNQS LLDLHKASDG KGDAHLCDYL EAEFLGEQVE GIKEIGDMLT KIKRAGDGLG LHIVDKEIGS //