ID A0A0R4J298_MOUSE Unreviewed; 587 AA.
AC A0A0R4J298;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:ENSMUSP00000137678.2,
GN ECO:0000313|MGI:MGI:109342};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000137678.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000137678.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000137678.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000137678.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000137678.2};
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 RefSeq; XP_006529228.1; XM_006529165.3.
DR AlphaFoldDB; A0A0R4J298; -.
DR SMR; A0A0R4J298; -.
DR ProteomicsDB; 361512; -.
DR Antibodypedia; 34586; 144 antibodies from 26 providers.
DR DNASU; 16865; -.
DR Ensembl; ENSMUST00000131855.2; ENSMUSP00000137678.2; ENSMUSG00000026427.17.
DR GeneID; 16865; -.
DR AGR; MGI:109342; -.
DR CTD; 1939; -.
DR MGI; MGI:109342; Eif2d.
DR VEuPathDB; HostDB:ENSMUSG00000026427; -.
DR GeneTree; ENSGT00550000074865; -.
DR OrthoDB; 102595at2759; -.
DR PhylomeDB; A0A0R4J298; -.
DR BioGRID-ORCS; 16865; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Eif2d; mouse.
DR Proteomes; UP000000589; Chromosome 1.
DR Bgee; ENSMUSG00000026427; Expressed in paneth cell and 263 other cell types or tissues.
DR ExpressionAtlas; A0A0R4J298; baseline and differential.
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:UniProtKB-KW.
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 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 1: Evidence at protein level;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Proteomics identification {ECO:0007829|EPD:A0A0R4J298,
KW ECO:0007829|MaxQB:A0A0R4J298};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 370..454
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 478..551
FT /note="SUI1"
FT /evidence="ECO:0000259|PROSITE:PS50296"
FT REGION 224..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 64496 MW; 9D588E545EA0E7C0 CRC64;
MFAKAFRVKS NTAIKGSDRR KLRADVTAAF PALGTDQISE LIPGKEELNV VKLYVHKGDS
VTVYTSGGNP ILFELEKNLY PTVYTLWAYP DILPTFITWP LVLEKLVGGA DLMLPGVVVP
PTGLPQVQQG DLCAIALVGN RAPVAIGVAA MSTAQMLASG LKGKGVSVLH TYQDHLWRSG
DKSSPPAIAP LDPTDSCEEK VHLGLQGNLK SLTLDGEEEN GQVPLREASE DTSSRAPSQD
SLDGKPLQEQ MDDLLLRCFL HALKSRVKKA DLPLLTSTLL GSHMFSCCPE GQQLDIKKSS
YKKLSKFLQH MQQEQIVQVK ELSKGVESIV AVDWRHPRIT SFVIPEPSLT SQTVQEVSRE
QPYLPPDIKS LYCVPANMTQ LFLESGHKKG STLEGSEVRK IITDYAKRNR LVDADNRNLV
KLDPILCDCI LEKNEQHLVT KLPWDCLLTR CLKNMQPAYQ VTFPGQEPIL KKGKLCPIDI
TLALKTYNKK VTVVRNLETY GLDPCSVAAI LQQRCQASTI VSPAPGAKDS LQVQVQGNQI
HHLGQLLLGE NTGTLHLPAQ YPHPHVQNKP EIPHLSCCGL PASHDSI
//
