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IREB2_XENTR
ID   IREB2_XENTR             Reviewed;         957 AA.
AC   A0JMA0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Iron-responsive element-binding protein 2;
DE            Short=IRE-BP 2;
GN   Name=ireb2;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Skeletal muscle;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2006) 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; BC125797; AAI25798.1; -; mRNA.
DR   RefSeq; NP_001072764.1; NM_001079296.1.
DR   AlphaFoldDB; A0JMA0; -.
DR   SMR; A0JMA0; -.
DR   DNASU; 780221; -.
DR   GeneID; 780221; -.
DR   KEGG; xtr:780221; -.
DR   CTD; 3658; -.
DR   Xenbase; XB-GENE-943197; ireb2.
DR   InParanoid; A0JMA0; -.
DR   OrthoDB; 190960at2759; -.
DR   Reactome; R-XTR-917937; Iron uptake and transport.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0003994; F:aconitate hydratase activity; IBA:GO_Central.
DR   GO; GO:0030350; F:iron-responsive element binding; IBA:GO_Central.
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:0006101; P:citrate metabolic process; IBA:GO_Central.
DR   GO; GO:0055072; P:iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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..957
FT                   /note="Iron-responsive element-binding protein 2"
FT                   /id="PRO_0000380118"
FT   BINDING         506
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         572
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         575
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   957 AA;  104874 MW;  1A0B63C0285384CA CRC64;
     MTENPFHYLV EPLSGTSDKT FFNVSKLKAT EYDSLPYCIR VVLEAVVRNC DGVLVKEQDA
     FNILNWKATC EFKEIPFLPA RVMLQDFTGI PAMVDFAAMR DAISKFGRDP KQVNPACPTD
     LIADHSLQLD FTKCIVAQNV SSVPTVETHK PTTKQSPGKT LGRKAQCRSQ SGCKGACELG
     AAHGSSREQI ENTPMLCPFH LQPIAEPEAA LKSLEIEFNR NKERLQFFKW CTKAFHNVAV
     IPPETGTVHQ VNLEFLSRVV MEEKGFIYPD SVLGTDSHTT MVNGLGILGL GVGGIESEAA
     MLGVPITLTL PEVIGCELTG AINPLATSID VVLSITKHLK QAGVAGTFVE FFGNGVSQLS
     VADRTTIANM CPEYGATVAF FPVDSVTLRH LKQTGVDVQS VSTFETYLQA VKLLRQENVQ
     QPEYSKVLQI NLNSIVPYVS GPKRPQDRIS VMDMKKDFEA CLNEKTGLKG FQIPEKKQSI
     MVPVTYENSE YSLSHGCVVI AAVTSCTNNC NPSVMLTAGL LAKKAVEAGL TVKPYIKTSL
     SPGSGTVTYY LSASGVLPYL SKLGFDIIGY GCARCVGNTN PLPESIVTAI KEGELVACGV
     FSGNKHFEGN RCSCVCANYL ASPPLVVAYA LAGTVNIDLQ TEALGENAQG EKIFLRDIWP
     SREEVLEVEE TMVIPSMFSE LKLKIEKQNT RWNLLDAPES TLFPWDLRST FIRSPPFFHK
     LEKIPPPIQP IEKAHVLLYL GDSVTTDHMS PAGSIPRTSP AAKYLIQKNL IPREFNSYGA
     RRGNDAVMTR GTFANMKLFN KLVGKTGPKT FHLPSGQIMD VFDAAELYQK AEIPLIIIAG
     KKYGLGNSRD WAAKGPFLLG VRVVIAESYE KIHKDHLVGM GIAPLQFLSG ENAETLGLSA
     KEQYSFSLPV DLTPRHKIEV KTNTGKTFHV IAAFDNEAEV TFYKHGGILS YVARKYL
 
 
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