ID F7GX41_MACMU Unreviewed; 532 AA.
AC F7GX41;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 04-NOV-2026, entry version 72.
DE RecName: Full=Eukaryotic translation initiation factor 2D {ECO:0000256|ARBA:ARBA00013816};
DE AltName: Full=Ligatin {ECO:0000256|ARBA:ARBA00030186};
GN Name=EIF2D {ECO:0000313|Ensembl:ENSMMUP00000003401.3,
GN ECO:0000313|VGNC:VGNC:72258};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000003401.3, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Ensembl:ENSMMUP00000003401.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000003401.3};
RA Graves T., Eichler E.E., Wilson R.K.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000003401.3}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000003401.3};
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; F7GX41; -.
DR SMR; F7GX41; -.
DR Ensembl; ENSMMUT00000003597.4; ENSMMUP00000003401.3; ENSMMUG00000002528.4.
DR VEuPathDB; HostDB:ENSMMUG00000002528; -.
DR VGNC; VGNC:72258; EIF2D.
DR GeneTree; ENSGT00550000074865; -.
DR HOGENOM; CLU_012487_2_0_1; -.
DR Proteomes; UP000006718; Chromosome 1.
DR Bgee; ENSMMUG00000002528; Expressed in adipose tissue and 21 other cell types or tissues.
DR ExpressionAtlas; F7GX41; baseline.
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; 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 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:UP000006718}.
FT DOMAIN 349..433
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 457..530
FT /note="SUI1"
FT /evidence="ECO:0000259|PROSITE:PS50296"
FT REGION 225..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 58563 MW; 7BCF4DFD1A6F00E0 CRC64;
MFAKAFRVKS NTAIKGSDRR KLRADVTTAF PTLGTDQVSE LVPGKEELNI VKLYAYKGDA
VTVYVSGGNP ILFELEKNLY PTVYTLWSYP DLLPTFTTWP LVLEKLVGGA DLMLPGLVMP
PAGLPQVQKG DLCAISLVGN RAPVAIGVAA MSTAEMLTSG LKGRGFSVLH TYQDHLWRSG
NKSSPPSIAP LALDSADLSE EKGSVQVDST LQGDMRHMIL EGEEENGEAH QACEEKSLSE
APEDTSTGGL NQDSTDSKTL QEQMDELLQQ CFLHALKCRV KKLSKFLQQM QQEQIIQVKE
LSKGVESIVA VDWKHPRITS FVIPEPSPTS QTIQEGSREQ PYHPPDIKPL YCVPASMTLL
FQESGHKKGS FLEGSEVRTI IINYAKKNDL VDADNKNLVK LDPILCDCIL EKNEQHTVMK
LPWDSLLTRC LEKLQPAYQV TFPGQEPIVK KGKICPIDIT LAQRASNKKV TVVRNLEAYG
LDPYSVAAIL QQRCQASTTV TSAPGAKDSL QVQIQGNQVH HLGWLLLGEH PL
//
