EIF2D_RAT
ID EIF2D_RAT Reviewed; 570 AA.
AC Q5PPG7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Eukaryotic translation initiation factor 2D;
DE Short=eIF2d;
DE AltName: Full=Ligatin;
GN Name=Eif2d; Synonyms=Lgtn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eIF2D family. {ECO:0000305}.
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DR EMBL; BC087701; AAH87701.1; -; mRNA.
DR RefSeq; NP_001017489.1; NM_001017489.1.
DR AlphaFoldDB; Q5PPG7; -.
DR SMR; Q5PPG7; -.
DR STRING; 10116.ENSRNOP00000006768; -.
DR iPTMnet; Q5PPG7; -.
DR PhosphoSitePlus; Q5PPG7; -.
DR jPOST; Q5PPG7; -.
DR PaxDb; Q5PPG7; -.
DR PRIDE; Q5PPG7; -.
DR Ensembl; ENSRNOT00000006768; ENSRNOP00000006768; ENSRNOG00000004910.
DR GeneID; 498225; -.
DR KEGG; rno:498225; -.
DR UCSC; RGD:1561765; rat.
DR CTD; 1939; -.
DR RGD; 1561765; Eif2d.
DR eggNOG; KOG2522; Eukaryota.
DR GeneTree; ENSGT00550000074865; -.
DR HOGENOM; CLU_012487_2_0_1; -.
DR InParanoid; Q5PPG7; -.
DR OMA; MFLKPYR; -.
DR OrthoDB; 401807at2759; -.
DR PhylomeDB; Q5PPG7; -.
DR TreeFam; TF105830; -.
DR PRO; PR:Q5PPG7; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000004910; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5PPG7; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0001731; P:formation of translation preinitiation complex; ISO:RGD.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:RGD.
DR GO; GO:0032790; P:ribosome disassembly; ISO:RGD.
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 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 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..570
FT /note="Eukaryotic translation initiation factor 2D"
FT /id="PRO_0000130614"
FT DOMAIN 93..173
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT DOMAIN 370..454
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT DOMAIN 478..551
FT /note="SUI1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
FT REGION 178..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..243
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 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61211"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61211"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41214"
SQ SEQUENCE 570 AA; 62669 MW; 97434C5FD17DD457 CRC64;
MFAKAFRVKS NTAIKGSDRR KLRADVTVAF PTLGTDQVSE LIPGKEELNV VKLYAHKGDA
VTVYTSGGNP ILFELEKNLY PTVYTLWSHP DLLPAFITWP LVLEKLVGGA DLMLPGVVVP
PTGLPQVQQG DLCAIALVGN RAPVAVGVAA MSTAQMLASG LKGKGISVLH TYQDHLWRSG
DKSSPPAIAP LDPTDSCEEK ADLGLHGNLR SLSLEGEEEN GQVPNPEASD DPNSRALSQD
SVDGKPLQEQ MDELLEQCFL HALKSRVKKA DLPLLTSTLL GSHMFSCCPE GQQLDIKKSS
YKKLSKFLQH MQQEQIVQVK ELSKGVESIV AVDWRHPRIT SFIVPEPSLA SQTVQEGSRE
KPYLPPDIKS LYCVPANMTQ LFLESGHKKG STLEGSEVRR IITDYAKRNN LVDADNRNLV
KLDPILCDCI LEKNEQHLVM KLPWDSLLTR CLKNLQPAYQ VTFPGQEPII KKGKLCPIDI
TLVLKTYNKK VTVVRNLETY GLDPCSVAAI LQQRCQASTI VSPAPGAKDS LQVQVQGNQI
HHLGQLLLEE YRLPGKYIQG LEKAPKPGKK
