IREB2_CHICK
ID IREB2_CHICK Reviewed; 965 AA.
AC Q5ZLQ4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Iron-responsive element-binding protein 2;
DE Short=IRE-BP 2;
GN Name=IREB2; ORFNames=RCJMB04_5d21;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719680; CAG31339.1; -; mRNA.
DR RefSeq; NP_001026625.1; NM_001031454.1.
DR AlphaFoldDB; Q5ZLQ4; -.
DR SMR; Q5ZLQ4; -.
DR STRING; 9031.ENSGALP00000038943; -.
DR PaxDb; Q5ZLQ4; -.
DR GeneID; 427490; -.
DR KEGG; gga:427490; -.
DR CTD; 3658; -.
DR VEuPathDB; HostDB:geneid_427490; -.
DR eggNOG; KOG0452; Eukaryota.
DR InParanoid; Q5ZLQ4; -.
DR OrthoDB; 190960at2759; -.
DR PhylomeDB; Q5ZLQ4; -.
DR PRO; PR:Q5ZLQ4; -.
DR Proteomes; UP000000539; 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.
DR PROSITE; PS01244; ACONITASE_2; 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..965
FT /note="Iron-responsive element-binding protein 2"
FT /id="PRO_0000380116"
FT REGION 142..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 580
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 583
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 965 AA; 105362 MW; B8860E6552906AC8 CRC64;
MDALRPGSPY QPIIEELRNY PQKRFYNVSK LGGTKYDVLP YSIRVLFESS IRNCDGFLVK
ETDAMNILDW KTKQNDVEVP FCPARVVLQD FTGIPAMVDF AAMREAVRNA GGDPVKVNPA
CPTDLTVDHS LQIDFSKCAI QNAPNPGGGE AQKPTAKLSP LKGQPRKLPC RGQSSCKGPC
SAGELSRASG QFSAQIENTP ILCPFHLQPV PEPETVLKNQ EMEFGRNRER LQFFKWSSKV
FKNTSIIPPE TGMAHQVNLE YLSRVVFDVE DFLYPDSVVG TDSHTTMVNG LGILGWGVGG
IETEAVMLGM PVTLTLPEVV GCELTGTASP LATSIDIVLG ITKHLRQAEV AGKFVEFFGS
GVSQLSVADR TTIANMCPEY GAILSFFPVD NVTLKHLRHT GFDEAKLEVM EAYLKAVKLF
RNGESSSREP EYSQVVQISL SSIIPHVSGP KRSQDRVAVN NMKSDFQTCL NEKAGVKGFQ
IAAEKQNDVV PVQYEGNQYE LSHGCVVIAA VISCTNNCNP SVMLAAGLLA KKAVEAGLEV
KPYIRTSLSP GSGMVTHYLS SSGVLPYLSK LGFEVVGYGC STCVGNTAPL PEAIRNAIKQ
GDIIACGVLS GTKNFEGRLC DCVRANYLAS PPLVVAYAIA GTVRIDFETE PLGTGFNGRS
IYLRDIWPTR KELHTVEEEC VISSMFKELK EKMEKGNKRW NSLEAPESPL FPWDLKSTYI
RCPSFFDKLA KEPVSLQPIE NAHVLLYLGD SVTTDHISPA GSIARSSAAA KYLTNKGLTP
REFNSYGARR GNDAVMTRGT FANIKLLNKF IGKPAPKTIH FPSGQTLDVF EAAELYQKEG
IPVIILAGKK YGLGSSRDWA AKGPFLLGVK AVLAESYEKV HKSQLIGIGI APLQFLPGEN
PNTLGLTGRE QFSILFPPEL SPKMTLDIKT STGKVFSVFA LFENDVEITL YKNGGSLNFV
ARRFL
