ID   FRIY_LYMST              Reviewed;         239 AA.
AC   P42578;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=Yolk ferritin;
DE            EC=1.16.3.1;
DE   Flags: Precursor;
OS   Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-38.
RC   TISSUE=Midgut;
RX   PubMed=7517354; DOI=10.1111/j.1432-1033.1994.tb18874.x;
RA   von Darl M., Harrison M., Bottke W.;
RT   "cDNA cloning and deduced amino acid sequence of two ferritins: soma
RT   ferritin and yolk ferritin, from the snail Lymnaea stagnalis L.";
RL   Eur. J. Biochem. 222:353-366(1994).
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 ferric iron core is deposited (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Midgut gland and bloodstream.
CC   -!- DEVELOPMENTAL STAGE: First detected during pregastrulation stage,
CC       levels increase up to the hatching stage, and is still present at the
CC       late veliger stage.
CC   -!- DOMAIN: Contains an 'insertion' sequence of 42 residues which is not
CC       present in other ferritins.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   EMBL; X56779; CAA40097.1; -; mRNA.
DR   PIR; S45604; S45604.
DR   AlphaFoldDB; P42578; -.
DR   SMR; P42578; -.
DR   GO; GO:0005576; C:extracellular region; 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: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; 2.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00204; FERRITIN_2; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:7517354"
FT   CHAIN           19..239
FT                   /note="Yolk ferritin"
FT                   /id="PRO_0000008852"
FT   DOMAIN          27..217
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   REGION          105..146
FT                   /note="Insertion; not present in other ferritins"
FT   BINDING         44
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         79
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         79
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         165
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         199
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   239 AA;  27338 MW;  E1C5873012DEEFFC CRC64;
     MNSVLFLTLA VCSSLAYGKE FVATVRQNYK ENINQLLEQQ IQKELAASYI YQAYASYFQR
     ADVSLPGIKK FFSDASSEER DDAQSLIDYI NQRGGHVQYD KIDLKDACET VMKFVTSDTS
     GLEEFRDRRM CICGFVATKT INDNCGERSD WKEGLIAFED TLAIERYVNA QLLDIHKKAD
     DEKDAHLTHI LEHEFLEEQV SSINKIAHAI TRLRSFEQGS GNNYKLGRVY LRPTPQISH
//