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