ID A0A094N628_ANTCR Unreviewed; 854 AA.
AC A0A094N628;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Iron-responsive element-binding protein 2 {ECO:0000256|ARBA:ARBA00015385};
DE Flags: Fragment;
GN ORFNames=N321_09334 {ECO:0000313|EMBL:KFZ62096.1};
OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC Caprimulgidae; Antrostomus.
OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ62096.1, ECO:0000313|Proteomes:UP000053620};
RN [1] {ECO:0000313|EMBL:KFZ62096.1, ECO:0000313|Proteomes:UP000053620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ62096.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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: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 EMBL; KL355875; KFZ62096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094N628; -.
DR Proteomes; UP000053620; Unassembled WGS sequence.
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; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
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; 1.
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:UP000053620};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 34..529
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 658..784
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFZ62096.1"
FT NON_TER 854
FT /evidence="ECO:0000313|EMBL:KFZ62096.1"
SQ SEQUENCE 854 AA; 93637 MW; 281D7F414BAE567E CRC64;
LPYSIRVLFE SSIRNCDGFL VKETDAMNIL DWKTKQNNVE VPFCPARVVL QDFTGIPAMV
DFAAMREAVR NAGGDPVKVN PACPTDLTVD HSLQIDFSKW PETVLKNQEM EYGRNRERLQ
FFKWSSKVFK NISIIPPETG MAHQVNLEYL SRVVFEVKDF LYPDSVVGTD SHTTMVNGLG
ILGWGVGGIE TEAVMLGMPV TLTLPEVVGC ELTGTASPLA TSIDIVLSIT KHLRQADVAG
KFVEFFGSGV SQLSVADRTT IANMCPEYGA ILSFFPVDNV TLKHLKHTGF DKAKLEVMEA
YLKAVKLFRN DESSSREPEY SQVVQISLSS IIPYVSGPKR SQDRVAVNNM KSDFQACLNE
KSGVKGFQIA VEKQNDIVPV QYEGNEYKLS HGCIVIAAVI SCTNNCNPSV MLAAGLLAKK
AVEAGLVVKP YIRTSLSPGS GMVTHYLSSS GVLPYLSKLG FEVVGYGCST CVGNTAPLPE
AIRNAIKQGD IIACGVLSGT KNFEGRLCDC VRANYLASPP LVVAYAIAGT VRIDFETEPL
GTDFNGKSIY LRDIWPTRRE LHTVEEECVI SSMFKELKEK MEKGNKRWNL LEAPESTLFP
WDLKSTYIRC PSFFDKLAKE PVSPQPIENA HVLLYLGDSV TTDHISPAGS IARSSAAAKY
LTNKGLTPRE FNSYGARRGN DAVMTRGTFA NIKLLNKFIG KPAPKTIHFP SGQTLDVFEA
AELYQKEGIP VIILAGKKYG LGSSRDWAAK GPFLLGVKAV LAESYEKVHK SQLIGIGIAP
LQFLPGENPS TLGLTGREQF SILFPPELSP GMTLDIKVSL HTGKVFSVIA LFENDMEITL
YKYGGSLNFV ARRF
//
