FRIY_LYMST
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 03-AUG-2022, entry version 96.
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: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; PTHR11431; 2.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; SSF47240; 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