ID G3NEF2_GASAC Unreviewed; 585 AA.
AC G3NEF2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 27-NOV-2024, sequence version 2.
DT 04-NOV-2026, entry version 66.
DE RecName: Full=Eukaryotic translation initiation factor 2D {ECO:0000256|ARBA:ARBA00013816};
DE AltName: Full=Ligatin {ECO:0000256|ARBA:ARBA00030186};
OS Gasterosteus aculeatus aculeatus (three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=481459 {ECO:0000313|Ensembl:ENSGACP00000003703.2, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000003703.2, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Benthic {ECO:0000313|Ensembl:ENSGACP00000003703.2,
RC ECO:0000313|Proteomes:UP000007635};
RX PubMed=33598708;
RA Nath S., Shaw D.E., White M.A.;
RT "Improved contiguity of the threespine stickleback genome using long-read
RT sequencing.";
RL G3 (Bethesda) 11:0-0(2021).
RN [2] {ECO:0000313|Ensembl:ENSGACP00000003703.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2026) to UniProtKB.
CC -!- FUNCTION: Translation initiation factor that is able to deliver tRNA to
CC the P-site of the eukaryotic ribosome in a GTP-independent manner. The
CC binding of Met-tRNA(I) occurs after the AUG codon finds its position in
CC the P-site of 40S ribosomes, the situation that takes place during
CC initiation complex formation on some specific RNAs. Its activity in
CC tRNA binding with 40S subunits does not require the presence of the
CC aminoacyl moiety. Possesses the unique ability to deliver non-Met
CC (elongator) tRNAs into the P-site of the 40S subunit. In addition to
CC its role in initiation, can promote release of deacylated tRNA and mRNA
CC from recycled 40S subunits following ABCE1-mediated dissociation of
CC post-termination ribosomal complexes into subunits.
CC {ECO:0000256|ARBA:ARBA00025522}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the eIF2D family.
CC {ECO:0000256|ARBA:ARBA00010359}.
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DR AlphaFoldDB; G3NEF2; -.
DR Ensembl; ENSGACT00000003715.2; ENSGACP00000003703.2; ENSGACG00000002815.3.
DR GeneTree; ENSGT00550000074865; -.
DR Proteomes; UP000007635; Chromosome XII.
DR Bgee; ENSGACG00000002815; Expressed in muscle tissue and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:InterPro.
DR CDD; cd11608; eIF2D_C; 1.
DR CDD; cd11610; eIF2D_N; 1.
DR CDD; cd21156; PUA_eIF2d-like; 1.
DR FunFam; 3.10.400.20:FF:000002; Eukaryotic translation initiation factor 2D; 1.
DR FunFam; 3.30.780.10:FF:000007; Putative eukaryotic translation initiation factor 2d; 1.
DR Gene3D; 3.10.400.20; -; 1.
DR Gene3D; 3.30.780.10; SUI1-like domain; 1.
DR InterPro; IPR039757; EIF2D.
DR InterPro; IPR048247; eIF2D_N.
DR InterPro; IPR039759; eIF2D_SUI1.
DR InterPro; IPR041366; Pre-PUA.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR048248; PUA_eIF2d-like.
DR InterPro; IPR001950; SUI1.
DR InterPro; IPR036877; SUI1_dom_sf.
DR InterPro; IPR058886; SWIB_eIF2D.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR InterPro; IPR057429; WH_eIF2D.
DR NCBIfam; TIGR00451; unchar_dom_2; 1.
DR PANTHER; PTHR12217; EUKARYOTIC TRANSLATION INITIATION FACTOR 2D; 1.
DR PANTHER; PTHR12217:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 2D; 1.
DR Pfam; PF17832; Pre-PUA; 1.
DR Pfam; PF26292; PUA_elF2D; 1.
DR Pfam; PF01253; SUI1; 1.
DR Pfam; PF26291; SWIB_eIF2D; 1.
DR Pfam; PF25304; WHD_eIF2D; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF55159; eIF1-like; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS50296; SUI1; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT DOMAIN 385..469
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 493..566
FT /note="SUI1"
FT /evidence="ECO:0000259|PROSITE:PS50296"
FT REGION 178..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..218
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..252
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 65220 MW; 7E9E652DF4C90347 CRC64;
MWCGDLLIDL PECRRKLKAD VSAAFPSLTA DELCELIPNK EELNVVKIYA HKGDAVTLYV
LHKNPLFFEL EKRLYPTVYV LWRHPALLPT FRTWPPVLEK LIGGADLMLP GVVAPSGGLP
NVKRGDCCSV TLVNNRAPVA VGNAASSSEE MLSAGMKGRG VCVLHAYMDH LWAFGDKSGP
PSFPDAEGEG QEANGEDYEV DDTQEEAERC EEEEEEQLSS EKVKDQPCCG SEALSLAVQE
EQRADEEEEA DQEDQKMPQE TMDALLLQCF LHALKRKVKK SELPLLTSTF LRNHMFSCCP
SGKQLDIKKS SYKKLSKFLQ AMQKQHNLIR VKELTKGVES IVEVDWNNKE LRYFKVVEET
NGDAAAAAQD GGEAEPPYHP PEITTLYSVS ARLEPLFLDA NKRKGTILQP AEVRHIVTEY
VKKNELVDEN NKNYVTVDPT LCDCLLEKSE YQEVQSLKWD DLFGRALGKM AECYEVVFPG
HAPVRKKGHM EPIDVSVASR GSNKKVTLIK NLDAYGLDPA AVGAALQRRV QASSVLQPVP
GSKDKVVVQI QGNQIHQVGR LLTDYYQIPR KYIQGLDKAP KSGKK
//
