ID I3K4W2_ORENI Unreviewed; 970 AA.
AC I3K4W2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Iron-responsive element-binding protein 2 {ECO:0000256|ARBA:ARBA00015385};
GN Name=IREB2 {ECO:0000313|Ensembl:ENSONIP00000016157.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000016157.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000016157.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003938}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU361275}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR RefSeq; XP_003447608.1; XM_003447560.4.
DR AlphaFoldDB; I3K4W2; -.
DR STRING; 8128.ENSONIP00000016157; -.
DR Ensembl; ENSONIT00000016172.2; ENSONIP00000016157.1; ENSONIG00000012838.2.
DR GeneID; 100699929; -.
DR KEGG; onl:100699929; -.
DR CTD; 3658; -.
DR eggNOG; KOG0452; Eukaryota.
DR GeneTree; ENSGT00940000157796; -.
DR HOGENOM; CLU_013476_2_1_1; -.
DR InParanoid; I3K4W2; -.
DR OMA; VYEPMFD; -.
DR OrthoDB; 176941at2759; -.
DR TreeFam; TF313476; -.
DR Proteomes; UP000005207; Linkage group LG7.
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:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 3.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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 NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF31; IRON-RESPONSIVE ELEMENT-BINDING PROTEIN 2; 1.
DR Pfam; PF00330; Aconitase; 2.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU361275};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU361275};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 71..135
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 195..646
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 775..901
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 140..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 106141 MW; 6C453C935D374949 CRC64;
MAYTSPVKEH PYSHLIDTLK DGQIKFFNPY KLNDPRYDKL PLSIRVLLEA AIRNCDGFYT
KQEDVQNILH WQQEQNKAEV PFSPARVLLQ DFTGIPAMVD LAAMRDAVAK HGVDPSLVNP
KCPTDLIVDH SLQIDYSKCA IQNAPNPGGG EGPSQGPSRS VHSRPPSRGA QCGGQRGSCS
KAACSDPPAS PGGSPASVQQ IENTPLLCPF HLQPVSEVET ALRNQEMELI RNKERLQFFK
WCSKAFKNVN VVPPDVGAVH QLNLEYLSRV VQVSDGFIYP DSVVGTDSHT TMINGLGILG
WGVGGIESEA IMLGQPISLT LPQVVGCKLV GSINPLTTSI DIVLGITKHL RQAGIAGKFV
EFFGPGVSQL SVPDRTTIAN MCPEYNATVS FFPVDQVTLK HFKKTNFTPE KLELLESYMK
AVKLFRSYED PSEDPQYSEV IEFNLSSMVP YVSGPKRPQD RVAVSSMKED FQSCLDEKVG
FKGFHIAKEK QEIRVPFLHG GQEYQLSHGS VVIAAVISCT NNCNPSVMLT AGLLARKAVE
AGLLVKPYIR TSLAPGSGMV THYLNASGVL PYFNKLGFEV IGYGCATCVG NTAPLPEAVV
DAIKQGDLVA CGVLSGNRHF EGRLCDCVRA NYLASPPLVV AYAIAGTVGV DFEKEPLGLT
SDGKEVYLRD IWPSREEVQQ IEEDTVFSSI FKDLRGRMEK GNTFWNNVEC SDSLLFPWDQ
KSTYIRSPSF FSKLSKEVPP PQSIENAHAL LFLGDKVTTD HISPAGSIAR VSAAAKYLMS
KRLTPREFNS YGARRGNDAV MTRGTFASIK LQNRFIGKPG PKTLHIPSGQ TLDVFEAADR
YQRDGIPLII LAGKDYGSGN SRDWVAKGPY LLGVRAVIAE SFEKLHRNQL VGMGIMPLQF
LSGQNADSLE LSGKERFSIT LPESLSPGQE LTIKTSQGKS FSVTALFDTD TDVILFQHGG
LLRYVARTLL
//
