IF6_RAT
ID IF6_RAT Reviewed; 245 AA.
AC Q3KRD8;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Eukaryotic translation initiation factor 6 {ECO:0000255|HAMAP-Rule:MF_03132};
DE Short=eIF-6 {ECO:0000255|HAMAP-Rule:MF_03132};
GN Name=Eif6; Synonyms=Itgb4bp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Binds to the 60S ribosomal subunit and prevents its
CC association with the 40S ribosomal subunit to form the 80S initiation
CC complex in the cytoplasm. Behaves as a stimulatory translation
CC initiation factor downstream insulin/growth factors. Is also involved
CC in ribosome biogenesis. Associates with pre-60S subunits in the nucleus
CC and is involved in its nuclear export. Cytoplasmic release of TIF6 from
CC 60S subunits and nuclear relocalization is promoted by a RACK1 (RACK1)-
CC dependent protein kinase C activity. In tissues responsive to insulin,
CC controls fatty acid synthesis and glycolysis by exerting translational
CC control of adipogenic transcription factors such as CEBPB, CEBPD and
CC ATF4 that have G/C rich or uORF in their 5'UTR. Required for ROS-
CC dependent megakaryocyte maturation and platelets formation, controls
CC the expression of mitochondrial respiratory chain genes involved in
CC reactive oxygen species (ROS) synthesis. Involved in miRNA-mediated
CC gene silencing by the RNA-induced silencing complex (RISC). Required
CC for both miRNA-mediated translational repression and miRNA-mediated
CC cleavage of complementary mRNAs by RISC. Modulates cell cycle
CC progression and global translation of pre-B cells, its activation seems
CC to be rate-limiting in tumorigenesis and tumor growth.
CC {ECO:0000255|HAMAP-Rule:MF_03132}.
CC -!- SUBUNIT: Monomer. Associates with the 60S ribosomal subunit. Interacts
CC with RACK1. Interacts with DICER1, AGO2, TARBP2, MOV10 and RPL7A; they
CC form a large RNA-induced silencing complex (RISC). {ECO:0000255|HAMAP-
CC Rule:MF_03132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03132}.
CC Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03132}. Note=Shuttles
CC between cytoplasm and nucleus/nucleolus. {ECO:0000255|HAMAP-
CC Rule:MF_03132}.
CC -!- PTM: Phosphorylation at Ser-174 and Ser-175 by CSNK1D/CK1 promotes
CC nuclear export. {ECO:0000250|UniProtKB:P56537}.
CC -!- PTM: Ufmylated by UFL1. {ECO:0000250|UniProtKB:O55135}.
CC -!- SIMILARITY: Belongs to the eIF-6 family. {ECO:0000255|HAMAP-
CC Rule:MF_03132}.
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DR EMBL; CH474050; EDL85894.1; -; Genomic_DNA.
DR EMBL; BC105764; AAI05765.1; -; mRNA.
DR RefSeq; NP_001032429.1; NM_001037352.1.
DR RefSeq; XP_006235378.1; XM_006235316.3.
DR RefSeq; XP_017447156.1; XM_017591667.1.
DR AlphaFoldDB; Q3KRD8; -.
DR SMR; Q3KRD8; -.
DR BioGRID; 258203; 1.
DR IntAct; Q3KRD8; 1.
DR STRING; 10116.ENSRNOP00000066257; -.
DR iPTMnet; Q3KRD8; -.
DR PhosphoSitePlus; Q3KRD8; -.
DR jPOST; Q3KRD8; -.
DR PaxDb; Q3KRD8; -.
DR PRIDE; Q3KRD8; -.
DR Ensembl; ENSRNOT00000073492; ENSRNOP00000066257; ENSRNOG00000049497.
DR GeneID; 305506; -.
DR KEGG; rno:305506; -.
DR CTD; 3692; -.
DR RGD; 1305373; Eif6.
DR eggNOG; KOG3185; Eukaryota.
DR GeneTree; ENSGT00390000015972; -.
DR HOGENOM; CLU_071894_0_0_1; -.
DR InParanoid; Q3KRD8; -.
DR OMA; GEDTTGP; -.
DR OrthoDB; 1157302at2759; -.
DR PhylomeDB; Q3KRD8; -.
DR PRO; PR:Q3KRD8; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000049497; Expressed in jejunum and 20 other tissues.
DR ExpressionAtlas; Q3KRD8; baseline and differential.
DR Genevisible; Q3KRD8; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; ISO:RGD.
DR GO; GO:0005638; C:lamin filament; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; ISO:RGD.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IBA:GO_Central.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0042256; P:mature ribosome assembly; ISO:RGD.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0032868; P:response to insulin; ISS:UniProtKB.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR CDD; cd00527; IF6; 1.
DR HAMAP; MF_00032; eIF_6; 1.
DR InterPro; IPR002769; eIF6.
DR PANTHER; PTHR10784; PTHR10784; 1.
DR Pfam; PF01912; eIF-6; 1.
DR PIRSF; PIRSF006413; IF-6; 1.
DR SMART; SM00654; eIF6; 1.
DR TIGRFAMs; TIGR00323; eIF-6; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Ribosome biogenesis;
KW Ubl conjugation.
FT CHAIN 1..245
FT /note="Eukaryotic translation initiation factor 6"
FT /id="PRO_0000402095"
FT MOD_RES 113
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P56537"
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O55135, ECO:0000255|HAMAP-
FT Rule:MF_03132"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55135, ECO:0000255|HAMAP-
FT Rule:MF_03132"
FT MOD_RES 174
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P56537, ECO:0000255|HAMAP-
FT Rule:MF_03132"
FT MOD_RES 175
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P56537, ECO:0000255|HAMAP-
FT Rule:MF_03132"
FT MOD_RES 235
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P56537, ECO:0000255|HAMAP-
FT Rule:MF_03132"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56537, ECO:0000255|HAMAP-
FT Rule:MF_03132"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 245 AA; 26571 MW; 046FA8F06709F69A CRC64;
MAVRASFENN CEVGCFAKLT NTYCLVAIGG SENFYSVFEG ELSDTIPVVH ASIAGCRIIG
RMCVGNRHGL LVPNNTTDQE LQHIRNSLPD SVQIRRVEER LSALGNVTTC NDYVALVHPD
LDRETEEILA DVLKVEVFRQ TVADQVLVGS YCVFSNQGGL VHPKTSIEDQ DELSSLLQVP
LVAGTVNRGS EVIAAGMVVN DWCAFCGLDT TSTELSVVES VFKLNEAKPS TIATSMRDSL
IDSLT
