FRIHB_XENLA
ID FRIHB_XENLA Reviewed; 176 AA.
AC P17663; B7ZS33; Q66LL5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ferritin heavy chain B;
DE Short=Ferritin H subunit B;
DE AltName: Full=Ferritin heavy chain 1;
DE EC=1.16.3.1;
GN Name=fth1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2336402; DOI=10.1093/nar/18.8.2184;
RA Moskaitis J.E., Pastori R.L., Schoenberg D.;
RT "Sequence of Xenopus laevis ferritin mRNA.";
RL Nucleic Acids Res. 18:2184-2184(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1993207; DOI=10.1021/bi00221a033;
RA Holland L.J., Wall A.A., Bhattacharya A.;
RT "Xenopus liver ferritin H subunit: cDNA sequence and mRNA production in the
RT liver following estrogen treatment.";
RL Biochemistry 30:1965-1972(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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 24 subunits. The functional molecule is roughly
CC spherical and contains a central cavity into which the polymeric
CC mineral iron core is deposited (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: There are three types of ferritin subunits in amphibia:
CC L, M and H chains. M and H chains are fast mineralizing; the L chain is
CC very slow mineralizing (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; X51395; CAA35760.1; -; mRNA.
DR EMBL; M55010; AAA49708.1; -; mRNA.
DR EMBL; BC044961; AAH44961.1; -; mRNA.
DR EMBL; BC170380; AAI70380.1; -; mRNA.
DR EMBL; BC170382; AAI70382.1; -; mRNA.
DR PIR; A37959; FRXL.
DR RefSeq; NP_001079580.1; NM_001086111.1.
DR AlphaFoldDB; P17663; -.
DR SMR; P17663; -.
DR DNASU; 379267; -.
DR GeneID; 379267; -.
DR KEGG; xla:379267; -.
DR CTD; 379267; -.
DR Xenbase; XB-GENE-6256345; fth1.1.S.
DR OrthoDB; 1249457at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 379267; Expressed in intestine and 19 other tissues.
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; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00540; FERRITIN_1; 1.
DR PROSITE; PS00204; FERRITIN_2; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 2: Evidence at transcript level;
KW Iron; Iron storage; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..176
FT /note="Ferritin heavy chain B"
FT /id="PRO_0000201077"
FT DOMAIN 7..156
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 24
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 104
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 138
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT CONFLICT 6
FT /note="R -> L (in Ref. 1; CAA35760)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="A -> I (in Ref. 1; CAA35760)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..158
FT /note="VP -> A (in Ref. 1; CAA35760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 20563 MW; C325E410FB3EC648 CRC64;
MQSQVRQNFN SDCEAAINRM VNLEMYASYV YLSMSYYFDR DDVALHHVAK FFKEQSHEER
EHAEKFLKYQ NKRGGRVVLQ DIKKPERDEW SNTLEAMQAA LQLEKTVNQA LLDLHKLASD
KVDPQLCDFL ESEYLEEQVK AMKELGDYIT NLKRLGVPQN GMGEYLFDKH TLGESS
