ID W5M8G5_LEPOC Unreviewed; 940 AA.
AC W5M8G5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000004673.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000004673.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Appears to play a role in the switch from cap-dependent to
CC IRES-mediated translation during mitosis, apoptosis and viral
CC infection. Cleaved by some caspases and viral proteases.
CC {ECO:0000256|ARBA:ARBA00037759}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000256|ARBA:ARBA00005775}.
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DR EMBL; AHAT01008208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M8G5; -.
DR STRING; 7918.ENSLOCP00000004673; -.
DR Ensembl; ENSLOCT00000004681.1; ENSLOCP00000004673.1; ENSLOCG00000003911.1.
DR eggNOG; KOG0401; Eukaryota.
DR GeneTree; ENSGT00940000154675; -.
DR HOGENOM; CLU_001519_3_0_1; -.
DR InParanoid; W5M8G5; -.
DR OMA; CAPLDIN; -.
DR Proteomes; UP000018468; Linkage group LG27.
DR Bgee; ENSLOCG00000003911; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR CDD; cd11559; W2_eIF4G1_like; 1.
DR Gene3D; 1.25.40.180; -; 3.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR PANTHER; PTHR23253:SF82; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 2; 1.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00515; eIF5C; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
DR PROSITE; PS51366; MI; 1.
DR PROSITE; PS51363; W2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 577..700
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 754..937
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 49..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 106376 MW; 7B5249EFD9EDCDF4 CRC64;
VEEPFCLMSL SLPPSSFSPP HPLNIILLKI LRCQAAKVES VIAEGGASRF SASSGGGGGR
GAPQHYPKTV GNSEYLGKTP GPSVQRWVPS RSTRRDVNST NEKERHDAIF RKVRGILNKL
TPEKFDKLCL ELLNVGVDSK LVLKGIILLI VDKALEEPKY SSLYAQLCLR LAEDAPNFDG
PSPEVQPTQK QSTTFRRLLI SKLQDEFENR TRNVEVYDKH DNPLTADEEE QRAIAKIKML
GNIKFIGELG KLDLIHESIL HKCIKTLLEK KKRVQLKDMG EDLECLCQIM RTVGPRLDHE
KAKSLMDQYF ARMRSLMTHK ELPARIRFLL QDTVELRENN WVPRKAFIDN GPKTINQIRQ
EAVKDLGVFI PAHMSQGMRS DFFLEGPFMP PRMKIEREGL GGLSDMFGQM PGSGIGTGPG
VIQDRFSPTM GRHRSNPLFN GHGGHIAPVP QSQFEMGGKP FMKSNQGQNQ HFHNQNQGHS
SQQQAQSKDM PPRFIKKGQL NADEISLRPA QSFLMNKNQV PKLQPQIPTM IPPSAQPPRT
QTPPLGQPPQ LGLKTNPPPI QEKPAKNSKR PPPAREELLK MTETIVTEYL NSKNINDAVN
GVREMKAPKH FLPEMLSKII ICSLDRSDDD KEHASTLINS LRSEGLITGE NFMQAFLNVL
DQCPKIEVDI PLVKSYLAQF AARAIIAELV NIAELAQPLE NGTHFPLFLL CLQQTAKLKD
REWLTELFQQ SKVNMQKMLP EIDQNKDRML EILEGKGLSF LFPLLKLEKE LLKQIKADPS
PQAIYKWIKD NISPKLHTDK GFVNILMTSF LQYISHEMSI AEGDDQLSAP SKEQLDQEKQ
LLLSFKPVMQ KFLHDHVDLQ VSALYALQVH CNNNGFPKGM LLRYFVNFYD MEIIEEEAFL
AWKEDITQEF PGKGKALFQV NQWLTWLETA EEEESDEEAD
//
