EIF2D_RABIT
ID EIF2D_RABIT Reviewed; 566 AA.
AC P0CL18;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Eukaryotic translation initiation factor 2D;
DE Short=eIF2d;
DE AltName: Full=Ligatin;
GN Name=EIF2D; Synonyms=LGTN;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=20713520; DOI=10.1101/gad.1957510;
RA Skabkin M.A., Skabkina O.V., Dhote V., Komar A.A., Hellen C.U.,
RA Pestova T.V.;
RT "Activities of ligatin and MCT-1/DENR in eukaryotic translation initiation
RT and ribosomal recycling.";
RL Genes Dev. 24:1787-1801(2010).
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:0000269|PubMed:20713520}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eIF2D family. {ECO:0000305}.
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 RefSeq; XP_002717595.1; XM_002717549.3.
DR AlphaFoldDB; P0CL18; -.
DR SMR; P0CL18; -.
DR STRING; 9986.ENSOCUP00000013278; -.
DR GeneID; 100345187; -.
DR KEGG; ocu:100345187; -.
DR CTD; 1939; -.
DR eggNOG; KOG2522; Eukaryota.
DR HOGENOM; CLU_012487_2_0_1; -.
DR InParanoid; P0CL18; -.
DR OMA; MFLKPYR; -.
DR OrthoDB; 401807at2759; -.
DR TreeFam; TF105830; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:Ensembl.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IEA:Ensembl.
DR GO; GO:0032790; P:ribosome disassembly; IEA:Ensembl.
DR CDD; cd11608; eIF2D_C; 1.
DR InterPro; IPR039757; EIF2D.
DR InterPro; IPR039759; eIF2D_SUI1.
DR InterPro; IPR041366; Pre-PUA.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR001950; SUI1.
DR InterPro; IPR036877; SUI1_dom_sf.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR PANTHER; PTHR12217; PTHR12217; 1.
DR Pfam; PF17832; Pre-PUA; 1.
DR Pfam; PF01253; SUI1; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR SUPFAM; SSF55159; SSF55159; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS50296; SUI1; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..566
FT /note="Eukaryotic translation initiation factor 2D"
FT /id="PRO_0000405564"
FT DOMAIN 93..173
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT DOMAIN 365..449
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT DOMAIN 473..546
FT /note="SUI1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
FT REGION 211..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P41214"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41214"
SQ SEQUENCE 566 AA; 62209 MW; 0220287998C38CC1 CRC64;
MFAKAFRVKS NTAIKGSDRR KLRADVAAAF PTLGTDQVSE LVPGKEELNT VKLYAHRGDA
VTVYVSGGNP ILFELEKNLY PTVYMLWSHP DLLPTFTTWP LVLEKLVGGA DLMLPGLVVP
PAGLPQVQKG DLCAIALVGN RAPVAIGVAA MSTEEMLTSG LKGRGFSVLH TYQDHLWRSG
DKSSPPSIAP LVVDPADLND DKESVQVNPV LQGEEEGNGE TALSEATSAG GQDQDPTDSR
TLQEQMDELL QQCFLHALKC RIQKADLPLL TSTLLGSHMF SCCPEGHQLD IKKSSYKKLS
KFLQHMQQEQ IVQVKELSRG VESVVAVDWR HPRITSFVIP EPSLTSQSVQ EGSREQPYRP
PDIKPLYCVP ASMTLLFQES GHKKGSVLEG SEVRAIIINY AKKNDLVDAD NKNLVKLDPV
LCDCLLEKHE QHSIMKLPWD SLVTRCLEKL QPAYQVTFPG QEPVVKKGKI CPIDITLAQR
ASNKKVTVVR NLEAYGLDPG SVAATLQQRC QASTTVTPAP GAKDSLQVQI QGNQVHHLGR
LLLEEYHLPR KYIQGLEHAP KASKKK
