ID W5KN38_ASTMX Unreviewed; 971 AA.
AC W5KN38;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Iron-responsive element-binding protein 2 {ECO:0000256|ARBA:ARBA00015385};
GN Name=IREB2 {ECO:0000313|Ensembl:ENSAMXP00000009000.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000009000.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000009000.2}
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 AlphaFoldDB; W5KN38; -.
DR STRING; 7994.ENSAMXP00000009000; -.
DR Ensembl; ENSAMXT00000009000.2; ENSAMXP00000009000.2; ENSAMXG00000008756.2.
DR eggNOG; KOG0452; Eukaryota.
DR GeneTree; ENSGT00940000157796; -.
DR HOGENOM; CLU_013476_2_1_1; -.
DR InParanoid; W5KN38; -.
DR OrthoDB; 176941at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000008756; Expressed in liver and 14 other cell types or 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: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:UP000018467};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 75..136
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 213..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 146..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 971 AA; 106326 MW; 913A31CFE3D292FB CRC64;
MALTSSQQEH PFAHLIDTLQ TEKNEAQKYF NPQKLGDPKY ERLPLSIRVL LESAIRKCDG
FYVKQEDVDN ILNWEERQNE AEIPFFPARV LLQDFTGIPA MVDLAAMRDA VAKNGIDPNL
INPKCPTDLI VDHSLQIDFS KCAIQNAPNP GGGDGQGTGP RLGPARSSPR NSQCGGQRGS
CSKGSCSDAP SSASRAPSVQ IENTPLLCPF HLQPVSEQDT AVRNQEMELI RNKERLQFFK
WCSKAFKNVT VVPPDIGSVH QVNLEYLSQV VQEIGGFVYP DTVVGTDSHT TMINGLGILG
WGVGGIESEA VMLGQPVSLT LPHVVGCRLV GSISTLATSI DIVLGITKHL RQASVGGKFV
EFFGPGVSQL SAADRTTIAN MCPEYNATVS FFPVDDTTLK HFKQTNFTEE KLEVMERYLK
AVKLFRSSDD QTEDPQYSEV IEINLASIVP CVSGPKRPQD RVPVPCMKED FLNCLNEKVG
FKGFHIPKEK QCITVPFLHE GTEYFLSHGS VVIAAVISCT NNCNPSVMLT AGLLAKKAVE
AGLTVKPYIR TSLAPGSGMV THYLNASGVL PYLSQLGFEV IGYGCATCVG NTAPLPESVV
DAIKQGDLVA CGVLSGNRHF EGRLCDCVRA NYLASPPLVV AYAITGTVGI DFEKEPIGFN
PEGKEVYLKD VWPSKEEVQD VEEHTVVASV FRELRSRMQK GSTYWSNLDA PDALLFPWDP
KSTYIRCPPF FSKLSKEMPT PVSIDNAHAL LFLGDKVTTD HISPAGSIAR VSAAARYLQS
KRLTPREFNS YGARRGNDAV MTRGTFASIK LQNRFIGKTG PKTLHIPSGQ TLDVFEAAER
YQRDGVPLII LAGKEYGSGN SRDWAAKGPY LLGVRAVIAE SFEKMHKNHL VGMGIAPLQF
LPGQNADSLE LCGKERFSIS IPEEFTPQQE LTVMTSTGKC FRVVALFENE MDVAFYRHGG
ILKYVARGML Q
//
