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IF6_BOVIN
ID   IF6_BOVIN               Reviewed;         245 AA.
AC   Q9TU47; Q2TBM1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Eukaryotic translation initiation factor 6 {ECO:0000255|HAMAP-Rule:MF_03132};
DE            Short=eIF-6 {ECO:0000255|HAMAP-Rule:MF_03132};
DE   AltName: Full=Imc-415 homolog;
GN   Name=EIF6 {ECO:0000255|HAMAP-Rule:MF_03132};
GN   Synonyms=ITGB4BP {ECO:0000255|HAMAP-Rule:MF_03132};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Holstein; TISSUE=Mammary gland;
RX   PubMed=10879479; DOI=10.1271/bbb.64.1052;
RA   Ha S., Baik M., Choi Y.;
RT   "Cloning and expression of bovine imc-415 cDNA from mammary gland.";
RL   Biosci. Biotechnol. Biochem. 64:1052-1054(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). In tissues
CC       responsive to insulin, controls fatty acid synthesis and glycolysis by
CC       exerting translational control of adipogenic transcription factors such
CC       as CEBPB, CEBPD and ATF4 that have G/C rich or uORF in their 5'UTR.
CC       Required for ROS-dependent megakaryocyte maturation and platelets
CC       formation, controls the expression of mitochondrial respiratory chain
CC       genes involved in reactive oxygen species (ROS) synthesis (By
CC       similarity). Involved in miRNA-mediated gene silencing by the RNA-
CC       induced silencing complex (RISC). Required for both miRNA-mediated
CC       translational repression and miRNA-mediated cleavage of complementary
CC       mRNAs by RISC (By similarity). Modulates cell cycle progression and
CC       global translation of pre-B cells, its activation seems to be rate-
CC       limiting in tumorigenesis and tumor growth (By similarity).
CC       {ECO:0000250|UniProtKB:O55135, ECO:0000250|UniProtKB:P56537,
CC       ECO:0000255|HAMAP-Rule:MF_03132}.
CC   -!- SUBUNIT: Monomer. Associates with the 60S ribosomal subunit. Interacts
CC       with RACK1 (By similarity). Interacts with DICER1, AGO2, TARBP2, MOV10
CC       and RPL7A; they form a large RNA-induced silencing complex (RISC) (By
CC       similarity). {ECO:0000250|UniProtKB:P56537, 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; AF141872; AAF00595.1; -; mRNA.
DR   EMBL; BC109922; AAI09923.1; -; mRNA.
DR   PIR; JC7273; JC7273.
DR   RefSeq; NP_777255.1; NM_174830.1.
DR   RefSeq; XP_005214560.1; XM_005214503.3.
DR   AlphaFoldDB; Q9TU47; -.
DR   SMR; Q9TU47; -.
DR   IntAct; Q9TU47; 2.
DR   STRING; 9913.ENSBTAP00000014966; -.
DR   PaxDb; Q9TU47; -.
DR   PRIDE; Q9TU47; -.
DR   Ensembl; ENSBTAT00000076570; ENSBTAP00000062338; ENSBTAG00000011263.
DR   GeneID; 286811; -.
DR   KEGG; bta:286811; -.
DR   CTD; 3692; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011263; -.
DR   VGNC; VGNC:57006; EIF6.
DR   eggNOG; KOG3185; Eukaryota.
DR   GeneTree; ENSGT00390000015972; -.
DR   HOGENOM; CLU_071894_0_0_1; -.
DR   InParanoid; Q9TU47; -.
DR   OMA; GEDTTGP; -.
DR   OrthoDB; 1157302at2759; -.
DR   TreeFam; TF105396; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000011263; Expressed in esophagus and 107 other tissues.
DR   ExpressionAtlas; Q9TU47; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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; IEA:InterPro.
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; IEA:UniProtKB-UniRule.
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   2: Evidence at transcript level;
KW   Cytoplasm; Initiation factor; Nucleus; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome; Ubl conjugation.
FT   CHAIN           1..245
FT                   /note="Eukaryotic translation initiation factor 6"
FT                   /id="PRO_0000259426"
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:0000250|UniProtKB:P56537, ECO:0000255|HAMAP-
FT                   Rule:MF_03132"
FT   CONFLICT        141
FT                   /note="T -> K (in Ref. 1; AAF00595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198
FT                   /note="V -> A (in Ref. 1; AAF00595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        210
FT                   /note="T -> A (in Ref. 1; AAF00595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222..224
FT                   /note="FKL -> SKP (in Ref. 1; AAF00595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="I -> T (in Ref. 1; AAF00595)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   245 AA;  26513 MW;  C62D76AD25402243 CRC64;
     MAVRASFENN CEIGCFAKLT NSYCLVAIGG SENFYSVFEG ELAGTIPVVH ASIAGCRIIG
     RMCVGNRHGL LVPNNTTDQE LQHIRNCLPD SVQIRRVEER LSALGNVTTC NDYVALVHPD
     LDRETEEILA DVLKVEVFRQ TVADQVLVGS YCVFSNQGGL VHPKTSIEDQ DELSSLLQVP
     LVAGTVNRGS EVIAAGMVVN DWCAFCGLDT TSTELSVVES VFKLNEAQPS TIATSMRDSL
     IDSLT
 
 
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