ID A0AAQ4QYP8_GASAC Unreviewed; 554 AA.
AC A0AAQ4QYP8;
DT 02-OCT-2024, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2024, sequence version 1.
DT 04-NOV-2026, entry version 10.
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:ENSGACP00000055618.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000055618.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Benthic {ECO:0000313|Ensembl:ENSGACP00000055618.1,
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:ENSGACP00000055618.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0AAQ4QYP8; -.
DR Ensembl; ENSGACT00000065868.1; ENSGACP00000055618.1; ENSGACG00000002815.3.
DR GeneTree; ENSGT00550000074865; -.
DR OMA; AACNNTE; -.
DR Proteomes; UP000007635; Chromosome XII.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; IPR057429; WH_eIF2D.
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 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 354..438
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 462..535
FT /note="SUI1"
FT /evidence="ECO:0000259|PROSITE:PS50296"
FT REGION 144..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..187
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 62041 MW; C6766382260E4A1D CRC64;
MFARQFRVKS NTAIKGSDRR KLKADVSAAF PSLTADELCE LIPNKEELNV VKIYAHKGDA
VTLYVLHKNP LFFELEKRLY PTVYVLWRHP ALLPTFRTWP PVLEKLIGGA DLMLPGVVAP
SGGLPNVKRG DCCSVTLVNN RAFGDKSGPP SFPDAEGEGQ EANGEDYEVD DTQEEAERCE
EEEEEQLSSE KVKDQPCCGS EALSLAVQEE QRADEEEEAD QEDQKMPQET MDALLLQCFL
HALKRKVKKS ELPLLTSTFL RNHMFSCCPS GKQLDIKKSS YKKLSKFLQA MQKQHNLIRV
KELTKGVESI VEVDWNNKEL RYFKVVEETN GDAAAAAQDG GEAEPPYHPP EITTLYSVSA
RLEPLFLDAN KRKGTILQPA EVRHIVTEYV KKNELVDENN KNYVTVDPTL CDCLLEKSEY
QEVQSLKWDD LFGRALGKMA ECYEVVFPGH APVRKKGHME PIDVSVASRG SNKKVTLIKN
LDAYGLDPAA VGAALQRRVQ ASSVLQPVPG SKDKVVVQIQ GNQIHQVGRL LTDYYQIPRK
YIQGLDKAPK SGKK
//
