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EIF3D_PONAB
ID   EIF3D_PONAB             Reviewed;         548 AA.
AC   Q5R925;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit D {ECO:0000255|HAMAP-Rule:MF_03003};
DE            Short=eIF3d {ECO:0000255|HAMAP-Rule:MF_03003};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 7 {ECO:0000255|HAMAP-Rule:MF_03003};
DE   AltName: Full=eIF-3-zeta {ECO:0000255|HAMAP-Rule:MF_03003};
GN   Name=EIF3D {ECO:0000255|HAMAP-Rule:MF_03003};
GN   Synonyms=EIF3S7 {ECO:0000255|HAMAP-Rule:MF_03003};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: mRNA cap-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, a complex required for several
CC       steps in the initiation of protein synthesis of a specialized
CC       repertoire of mRNAs. The eIF-3 complex associates with the 40S ribosome
CC       and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-
CC       tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The
CC       eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning
CC       of the mRNA for AUG recognition. The eIF-3 complex is also required for
CC       disassembly and recycling of post-termination ribosomal complexes and
CC       subsequently prevents premature joining of the 40S and 60S ribosomal
CC       subunits prior to initiation. The eIF-3 complex specifically targets
CC       and initiates translation of a subset of mRNAs involved in cell
CC       proliferation, including cell cycling, differentiation and apoptosis,
CC       and uses different modes of RNA stem-loop binding to exert either
CC       translational activation or repression. In the eIF-3 complex, EIF3D
CC       specifically recognizes and binds the 7-methylguanosine cap of a subset
CC       of mRNAs. {ECO:0000255|HAMAP-Rule:MF_03003}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC       EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC       EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC       is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC       EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC       EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC       EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC       subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC       interacts with RPS6KB1 under conditions of nutrient depletion.
CC       Mitogenic stimulation leads to binding and activation of a complex
CC       composed of MTOR and RPTOR, leading to phosphorylation and release of
CC       RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000255|HAMAP-
CC       Rule:MF_03003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
CC   -!- DOMAIN: The RNA gate region regulates mRNA cap recognition to prevent
CC       promiscuous mRNA-binding before assembly of eif3d into the full
CC       eukaryotic translation initiation factor 3 (eIF-3) complex.
CC       {ECO:0000255|HAMAP-Rule:MF_03003}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit D family. {ECO:0000255|HAMAP-
CC       Rule:MF_03003}.
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DR   EMBL; CR859571; CAH91735.1; -; mRNA.
DR   RefSeq; NP_001126007.1; NM_001132535.1.
DR   AlphaFoldDB; Q5R925; -.
DR   SMR; Q5R925; -.
DR   STRING; 9601.ENSPPYP00000013137; -.
DR   GeneID; 100172951; -.
DR   KEGG; pon:100172951; -.
DR   CTD; 8664; -.
DR   eggNOG; KOG2479; Eukaryota.
DR   InParanoid; Q5R925; -.
DR   OrthoDB; 1030308at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; ISS:UniProtKB.
DR   GO; GO:0098808; F:mRNA cap binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0002191; P:cap-dependent translational initiation; ISS:UniProtKB.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR   HAMAP; MF_03003; eIF3d; 1.
DR   InterPro; IPR007783; eIF3d.
DR   PANTHER; PTHR12399; PTHR12399; 1.
DR   Pfam; PF05091; eIF-3_zeta; 1.
DR   PIRSF; PIRSF016281; EIF-3_zeta; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..548
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D"
FT                   /id="PRO_0000292661"
FT   REGION          285..299
FT                   /note="RNA gate"
FT                   /evidence="ECO:0000250|UniProtKB:K7IM66"
FT   REGION          288..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..548
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         53
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O70194"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15371"
FT   MOD_RES         528
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15371"
FT   MOD_RES         529
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15371"
SQ   SEQUENCE   548 AA;  63957 MW;  42A0448A82FE171A CRC64;
     MAKFMTPVIQ DNPSGWGPCA VPEQFRDMPY QPFSKGDRLG KVADWTGATY QDKRYTNKYS
     SQFGGGSQYA YFHEEDESSF QLVDTARTQK TAYQRNRMRF AQRNLRRDKD RRNMLQFNLQ
     ILPKSAKQKE RERIRLQKKF QKQFGVRQKW DQKSQKPRDS SVEVRSDWEV KEEMDFPQLM
     KMRYLEVSEP QDIECCGALE YYDKAFDRIT TRSEKPLRSI KRIFHTVTTT DDPVIRKLAK
     TQGNVFATDA ILATLMSCTR SVYSWDIVVQ RVGSKLFFDK RDNSDFDLPT VSETANEPPQ
     DEGNSFNSPR NLAMEATYIN HNFSQQCLRM GKERYNFPNP NPFVEDDMDK NEIASVAYRY
     RRWKLGDDID LIVRCEHDGV MTGANGEVSF INIKTLNEWD SRHCNGVDWR QKLDSQRGAV
     IATELKNNSY KLARWTCCAL LAGSEYLKLG YVSRYHVKDS SRHVILGTQQ FKPNEFASQI
     NLSVENAWGI LRCVIDICMK LEEGKYLILK DPNKQVIRVY SLPDGTFSSD EDEEEEEEEE
     EEEEEEET
 
 
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