IREB2_PIG
ID IREB2_PIG Reviewed; 964 AA.
AC B3VKQ2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Iron-responsive element-binding protein 2;
DE Short=IRE-BP 2;
GN Name=IREB2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wu Y.-X., Wang Y.-L., Zhao W.-D., Wang J., Zhang Z.-Q., Zang M., Tai Y.-L.,
RA Wang W.-J., Yang G.-Y.;
RL Submitted (MAY-2008) 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. {ECO:0000250|UniProtKB:P48200}.
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 -!- SUBUNIT: Interacts with RBCK1 only in iron-rich conditions. Interacts
CC (when associated with the 4Fe-4S) with FBXL5 (By similarity). Interacts
CC with CIAO1 and CIAO2A (By similarity). {ECO:0000250|UniProtKB:P48200,
CC ECO:0000250|UniProtKB:Q811J3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Ubiquitinated and degraded by the proteasome in presence of high
CC level of iron and oxygen. Ubiquitinated by a SCF complex containing
CC FBXL5. Upon iron and oxygen depletion FBXL5 is degraded, preventing
CC ubiquitination and allowing its RNA-binding activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; EU755259; ACE78187.1; -; mRNA.
DR AlphaFoldDB; B3VKQ2; -.
DR SMR; B3VKQ2; -.
DR STRING; 9823.ENSSSCP00000001913; -.
DR PaxDb; B3VKQ2; -.
DR PeptideAtlas; B3VKQ2; -.
DR PRIDE; B3VKQ2; -.
DR Ensembl; ENSSSCT00070039612; ENSSSCP00070033178; ENSSSCG00070019970.
DR eggNOG; KOG0452; Eukaryota.
DR HOGENOM; CLU_013476_2_1_1; -.
DR InParanoid; B3VKQ2; -.
DR TreeFam; TF313476; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 7.
DR Genevisible; B3VKQ2; SS.
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; ISS:UniProtKB.
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; Reference proteome;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..964
FT /note="Iron-responsive element-binding protein 2"
FT /id="PRO_0000380115"
FT BINDING 513
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 579
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 582
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 964 AA; 105187 MW; 254C81EA557C3052 CRC64;
MDAPSAGYAF EYLIETLNDS SHKKFFNVPR LGGTKYDVLP YSIRVLLEAA VRNCDGFLMK
KEDVMNILDW KTKQSNVEVP FFPGRVLLQD FTGIPAMVDF AAMREAVKTL GGDPKKVHPA
CPTDLTVDHS LQIDFNKCAI QNAPNPGGGD LQKAGKLSPL RVQPKKLPCR GQTACRGSCD
SGDLGRNSGK FSSQIENTPI LCPFHLQPVP EPETVLKNQE VEFGRNRERL QFFKWSSRVF
KNVAVIPPGT GMAHQVNLEY LSRVVFEEKD LLFPDSVVGT DSHITMVNGL GILGWGVGGI
ETEAVMLGLP VSLTLPEVVG CELTGSSNPF VTSIDVVLGI TKHLRQIGVA GKFVEFFGSG
VSQLSIVDRT TIANMCPEYG AILSFFPVDN VTLKHLEYTG FNKAKLKSME TYLKAVKLFR
NDQDNSGEPE YSQVIQINLN SIVPSVSGPK RPQDRVAVTD MKSDFQACLN EKVGFKGFQI
AAEKQNDTVS IHYEGSEYKL SHGSVVIAAV ISCTNNCNPS VMLAAGLLAK KAVEAGLRVK
PYIRTSLSPG SGMVTHYLSS SGVLPYLSKL GFEIVGYGCS TCVGNTAPLS EAVLNAVKQG
DLVTCGVLSG NKNFEGRLCD CVRANYLASP PLVVAYAIAG TVNIDFRTEP LGTDPTGKNI
YLHDIWPSRE EVHQIEEEHV VLSMFKALKE KIEMGNKRWN SLEAPDSVLF PWDLKSTYIR
CPSFFDKLTK EPVALQPIEN AHVLLYLGDS VTTDHISPAG SIARSSAAAK YLTNRGLTPR
EFNSYGARRG NDAVMTRGTF ANIKLFNKFI GKPAPKTIHF PSGQTLDVFE AAELYQKEGI
PLIILAGKKY GSGNSRDWAA KGPYLLGVKA VLAESYEKIH KDHLIGIGIA PLQFLPGENA
DSLGLSGRET FSLTFPEELS PGVTLNIKTS TGKIFSVIAS FENDVEIILY KHGGLLNFVA
RKFS
