ID   FRI_PACLE               Reviewed;         181 AA.
AC   Q26061;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Ferritin;
DE            EC=1.16.3.1;
OS   Pacifastacus leniusculus (Signal crayfish).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Astacoidea; Astacidae; Pacifastacus.
OX   NCBI_TaxID=6720;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 76-88.
RC   TISSUE=Hepatopancreas;
RX   PubMed=8612615; DOI=10.1111/j.1432-1033.1996.00450.x;
RA   Huang T.-S., Law J.H., Soederhaell K.;
RT   "Purification and cDNA cloning of ferritin from the hepatopancreas of the
RT   freshwater crayfish Pacifastacus leniusculus.";
RL   Eur. J. Biochem. 236:450-456(1996).
CC   -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form.
CC       Important for iron homeostasis. Has ferroxidase activity. Iron is taken
CC       up in the ferrous form and deposited as ferric hydroxides after
CC       oxidation (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Oligomer of 12 or 24 subunits. The functional molecule is
CC       roughly spherical and contains a central cavity into which the
CC       polymeric mineral iron core is deposited (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: There are 2 types of crayfish ferritin subunit: a 19 kDa
CC       chain and a 20 kDa chain.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   EMBL; X90566; CAA62186.1; -; mRNA.
DR   PIR; S62651; S62651.
DR   AlphaFoldDB; Q26061; -.
DR   SMR; Q26061; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR008331; Ferritin_DPS_dom.
DR   PANTHER; PTHR11431; PTHR11431; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..181
FT                   /note="Ferritin"
FT                   /id="PRO_0000201071"
FT   DOMAIN          6..155
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         23
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         58
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         58
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         61
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         103
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         137
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   181 AA;  20671 MW;  C7318FC910178C55 CRC64;
     MASQIRHNYH EDCEPINKQI NLEFYASYVY MSMGHYFDRD DISLPGASKF FKDSSDEERE
     HGQKLMKYQN KRGARIVLQA IAAPSLQEWG NLHDALQAAL DLENEVNQSL LDLDATASKI
     NDPHLTNMLE GEFLEEQVES IEKIGNLITR LKRAGTSGLG EFLFDKELKQ RFLPSLTSHP
     N