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EIF3D_XENLA
ID   EIF3D_XENLA             Reviewed;         550 AA.
AC   Q7ZTM9;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 62.
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};
GN   Name=eif3d; Synonyms=eif3s7;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: mRNA cap-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with other
CC       initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC       the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation. In the
CC       eIF-3 complex, eif3d specifically recognizes and binds the 7-
CC       methylguanosine cap of a subset of mRNAs. {ECO:0000255|HAMAP-
CC       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. {ECO:0000255|HAMAP-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; BC044692; AAH44692.1; -; mRNA.
DR   RefSeq; NP_001080587.1; NM_001087118.2.
DR   AlphaFoldDB; Q7ZTM9; -.
DR   SMR; Q7ZTM9; -.
DR   BioGRID; 98521; 2.
DR   IntAct; Q7ZTM9; 1.
DR   MaxQB; Q7ZTM9; -.
DR   DNASU; 380279; -.
DR   GeneID; 380279; -.
DR   KEGG; xla:380279; -.
DR   CTD; 380279; -.
DR   Xenbase; XB-GENE-942859; eif3d.S.
DR   OMA; PDGWGPC; -.
DR   OrthoDB; 1030308at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 380279; Expressed in spleen and 19 other tissues.
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   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..550
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D"
FT                   /id="PRO_0000364135"
FT   REGION          288..302
FT                   /note="RNA gate"
FT                   /evidence="ECO:0000250|UniProtKB:K7IM66"
FT   REGION          526..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..550
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  63945 MW;  C50248A96364B41B CRC64;
     MAKFQAPVIN DNALGWGPCA IPDQFKDMPY QPFSKGDRLG KVADWTGATY QDKRYTNKYS
     SQFGGGSQYA YFHDEDETSF QLVDTTKMQK TAYQRNRMRF AQRNLRRDKD RRNMLQFNMQ
     TLPKSAKQKE RDRLRLQKKF QKQFGVRQKW DQRSQAQLKP RDSSVEVRSD WEVKEEMDFP
     RLMKMRYMEV ADPTDIECCG AVEYYDKAFD RITTRNERPL RSIKRIFHTV TTTDDPVIRK
     LAKTQGNVFA TDAILATLMC CTRSVNSWDI VVQRVGSKIF FDKRDNSDFD LLTVSETANE
     PPQDEVNSLN SPRNLAMEAT YINHNFSQQC LRMGKEKHTF PNPNPFIEDD VDKNEVASVA
     YRYRRWKLGD DIDLVVRCEH DGVMTGANGE VSFINIKTLN EWDSKYCNGV DWRQKLDSQR
     GAVIATELKN NSYKLARWTC CALLAGSEYL KLGYVSRYNV KDSTRHVVLG TQQFKPNEFA
     NQINLSMENA WGILRCVVDI CMKLDEGKYL ILKDPNKQVI RIYSLPDGTF SSDEEEDDDD
     EDEEVEEEES
 
 
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