ID H2Q102_PANTR Unreviewed; 584 AA.
AC H2Q102; A0A2J8QVU9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
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|EMBL:JAA06204.1,
GN ECO:0000313|Ensembl:ENSPTRP00000003204.5, ECO:0000313|VGNC:VGNC:528};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000003204.5, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000003204.5, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA06204.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA06204.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA34438.1}, and Skin {ECO:0000313|EMBL:JAA25920.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000003204.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 EMBL; AACZ04071427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01005134; JAA06204.1; -; mRNA.
DR EMBL; GABD01007180; JAA25920.1; -; mRNA.
DR EMBL; GABE01010301; JAA34438.1; -; mRNA.
DR RefSeq; NP_001189416.1; NM_001202487.1.
DR STRING; 9598.ENSPTRP00000003204; -.
DR PaxDb; 9598-ENSPTRP00000003204; -.
DR Ensembl; ENSPTRT00000003484.6; ENSPTRP00000003204.5; ENSPTRG00000001913.7.
DR GeneID; 457682; -.
DR KEGG; ptr:457682; -.
DR CTD; 1939; -.
DR VGNC; VGNC:528; EIF2D.
DR eggNOG; KOG2522; Eukaryota.
DR GeneTree; ENSGT00550000074865; -.
DR HOGENOM; CLU_012487_2_0_1; -.
DR OMA; MFLKPYR; -.
DR OrthoDB; 102595at2759; -.
DR TreeFam; TF105830; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000001913; Expressed in hindlimb stylopod muscle and 21 other cell types or tissues.
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; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
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 CDD; cd11610; eIF2D_N; 1.
DR CDD; cd21156; PUA_eIF2d-like; 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; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
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; PF01253; SUI1; 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 2: Evidence at transcript level;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:JAA06204.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277}.
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"
FT REGION 223..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 64746 MW; 0B6DB082F7F146B0 CRC64;
MFAKAFRVKS NTAIKGSDRR KLRADVTTTF PTLGTDQVSE LVPGKEELNI VKLYAHKGDA
VTVYVSGGNP ILFELEKNLY PTVYTLWSYP DLLPTFTTWP LVLEKLVGGA DLMLPGLVMP
PAGLPQVQKG DLCAISLVGN RAPVAIGVAA MSTAEMLTSG LKGRGFSVLH TYQDHLWRSG
NKSSPPSIAP LAMDSADLSE EKGSVQMDST LQGDMRHMTL EGEEENGEVH QAREDKSLSE
APEDTSTRGL NQDSTDSKTL QEQMDELLQQ CFLHALKCRV KKADLPLLTS TFLGSHMFSC
CPEGRQLDIK KSSYKKLSKF LQQMQQEQII QVKELSKGVE SIVAVDWKHP RITSFVIPEP
SPTSQTIQEG SREQPYHPPD IKPLYCVPAS MTLLFQESGH KKGSFLEGSE IRTIVINYAK
KNDLVDADNK NLVKLDPILC DCILEKNEQH TVMKLPWDSL LTRCLEKLQP AYQVTFPGQE
PIVKKGRICP IDITLAQRAS NKKVTVVRNL EAYGLDPYSV AAILQQRCQA STTVTPAPGA
KDSLQVQIQG NQVHHLGWLL LEEYQLPRKH IQGLEKAPKP GKKK
//
