ID F7IPX2_CALJA Unreviewed; 584 AA.
AC F7IPX2; U3DKK3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 04-NOV-2026, entry version 77.
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:ENSCJAP00000034651.3};
OS Callithrix jacchus (White-tufted-ear marmoset) (Simia Jacchus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000034651.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000034651.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000034651.3}
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 RefSeq; XP_002760777.2; XM_002760731.7.
DR AlphaFoldDB; F7IPX2; -.
DR STRING; 9483.ENSCJAP00000034651; -.
DR Ensembl; ENSCJAT00000036595.4; ENSCJAP00000034651.3; ENSCJAG00000018600.5.
DR GeneID; 100385063; -.
DR KEGG; cjc:100385063; -.
DR CTD; 1939; -.
DR eggNOG; KOG2522; Eukaryota.
DR GeneTree; ENSGT00550000074865; -.
DR OrthoDB; 199771at2759; -.
DR Proteomes; UP000008225; Chromosome 19.
DR Bgee; ENSCJAG00000018600; Expressed in ovary and 6 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; 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 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:UP000008225}.
FT DOMAIN 383..467
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 491..564
FT /note="SUI1"
FT /evidence="ECO:0000259|PROSITE:PS50296"
SQ SEQUENCE 584 AA; 64476 MW; 7EDCDC33D7FCCF38 CRC64;
MFAKAFRVKS NTAIKGSDRR KLRADVTTAF PTLGTDQVSE LVPGKEDLNI VKLYAHKGDA
VTVYVSGGNP ILFELEKNLY PTVYTLWSYP DLLPTFTTWP PVLEKLVGGA DLMLPGLVMP
PAGLPQIQKG DLCAISLVGN RAPVAIGVAA MSTAEMLTSG LKGRGFSVLH TYQDHLWRSG
NKSSLPSIAP LALNSADVCE EKGAVQVDST LRGDMRHMTL EGEEENGEVH QVCEEKSLSE
ASEDTSIGGL NQDSTDGKTL QEQMDELLQR CFLHALKCRV KKADLPLLTS TFLGSHMFSC
CPEGRQVDIK KSSYKKLSKF LQQMQQEQII QVKELSKGVE SIVAVDWKHP RITSFVMPEP
SPTSQTIQEG SREQPYHPPD IKPLYCVPAS MTLLFQESGH KKGSFLEGSE VRSIIINYAK
KNDLVDTDNK NLVKLDPVLC DCILEKNEQH TVMKLPWDSL LARCLEKLQP AYQVTFPGQG
PVVKKGKICP IDITLAQRAS NKKVTVVRNL EAYGLDPYSV AAILQQRCQA STTVTPSPGA
KDSLQVQIQG NQVHHLSWLL LEEYQLPRKH IQGLEKAPKP GKKK
//
