ID   IREB2_XENLA             Reviewed;         955 AA.
AC   Q6NTP2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Iron-responsive element-binding protein 2;
DE            Short=IRE-BP 2;
GN   Name=ireb2;
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 [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-binding protein that binds to iron-responsive elements
CC       (IRES), which are stem-loop structures found in the 5'-UTR of ferritin,
CC       and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of
CC       transferrin receptor mRNA. Binding to the IRE element in ferritin
CC       results in the repression of its mRNA translation. Binding of the
CC       protein to the transferrin receptor mRNA inhibits the degradation of
CC       this otherwise rapidly degraded mRNA.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. [4Fe-4S]-binding affects
CC       RNA-binding activity, thereby inhibiting activity of the protein.
CC       {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Ubiquitinated and degraded by the proteasome in presence of high
CC       level of iron and oxygen. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; BC068915; AAH68915.1; -; mRNA.
DR   RefSeq; NP_001084628.1; NM_001091159.1.
DR   AlphaFoldDB; Q6NTP2; -.
DR   SMR; Q6NTP2; -.
DR   DNASU; 414584; -.
DR   GeneID; 414584; -.
DR   KEGG; xla:414584; -.
DR   CTD; 414584; -.
DR   Xenbase; XB-GENE-943202; ireb2.L.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 414584; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0030350; F:iron-responsive element binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030371; F:translation repressor activity; IEA:InterPro.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR   GO; GO:0055072; P:iron ion homeostasis; ISS:UniProtKB.
DR   CDD; cd01580; AcnA_IRP_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   Gene3D; 3.30.499.10; -; 3.
DR   InterPro; IPR044137; AcnA_IRP_Swivel.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR006249; Aconitase/IRP2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR029755; IRE-BP2.
DR   PANTHER; PTHR11670; PTHR11670; 1.
DR   PANTHER; PTHR11670:SF31; PTHR11670:SF31; 1.
DR   Pfam; PF00330; Aconitase; 2.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR01341; aconitase_1; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Phosphoprotein;
KW   Reference proteome; RNA-binding; Ubl conjugation.
FT   CHAIN           1..955
FT                   /note="Iron-responsive element-binding protein 2"
FT                   /id="PRO_0000380117"
FT   BINDING         504
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         570
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         573
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   955 AA;  104437 MW;  E7C09DDE005849F7 CRC64;
     MTENPFHYLV ETLSGTSDKT FFNVSKLKAT EYDSLPYCIR VVLEAVVRNC DGVLVKEQDA
     FNILNWKTKC EFKEIPFLPA RVMLQDFTGI PAMVDFAAMR DAISKFGKDP KQVNPACPTD
     LIADHSLQLD FTKCIAAQNV SGLPAVETHR PTTTPGKTPG RKAQCRSQGG CKGACDLGAA
     NGSSREQIEN TPMLCPFHLQ PIAEPETALK SLEIEFNRNK ERLQFFKWCS KAFQNVAVIP
     PETGTVHQVN LEFLSRVVME EKGCIYPDSV LGTDSHTTMV NGLGILGLGV GGIESEAAML
     GVPITLTLPE VVGCELTGTI NPIATSIDVV LSITKHLKQA GVAGTFVEFF GNGVSQLSVA
     DRTTIANMCP EYGATVAFFP VDSVTLQHLK QTGVDLQCVK TFENYLKAVK LLRQENVQQP
     LYSKVLQINL NSIVPYVSGP KRPQDRISVM DMKKDFETCL KEKTGLKGFQ IPEEKQNIMV
     PVTYGNSEYS LSHGCVVIAA VTSCTNNCNP SVMLTAGLLA KKAVEAGLTV KPYIKTSLSP
     GSGTVTYYLS ASGVLPYLSK LGFDIIGYGC ARCVGNTNPL PESIVTAIKE GELVACGVFS
     GNKHFEGNRC SCVCANYLAS PPLVVAYALA GTVNIDLQTE PLGENAQGKK IFLQDIWPSR
     EEVLEVEETL VIPSMFSELK LKIEKQNTRW NLLDAPESTL FPWDLRSTYI RSPPFFHKLE
     KIPPPIQPIE RAYVLLYLGD SVTTDHMSPA GSIPRTSPAA KYLMQKNLVP REFNSYGARR
     GNDAVMTRGT FANMKLFNKL VGKTGPKTIH LPSGQTMDVF DAAELYQRSE IPLIIIAGKK
     YGLGNSRDWA AKGPFLLGVR VVIAESYEKI HKDHLVGMGI APLQFLSGEN AETLGLSGKE
     QYSLSLPVDL TPGHKVEIKT NTGKIFHVIA AFDNEAEVTL YKHGGILSYV ARKYL