ID A0A3P9N5M4_POERE Unreviewed; 845 AA.
AC A0A3P9N5M4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000004855.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000004855.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000004855.1};
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3P9N5M4; -.
DR Ensembl; ENSPRET00000004921.1; ENSPREP00000004855.1; ENSPREG00000003216.1.
DR GeneTree; ENSGT00940000154675; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000003216; Expressed in head and 1 other cell type or tissue.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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:UP000242638};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 482..605
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 659..842
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 96224 MW; BCBF70C3C81536C0 CRC64;
GGRGAPQHYP KTVGNSEFLG KTPGQSVQRW VPSRSTRRDA NSSNEKERHD AIFRKVRGIL
NKLTPEKFDK LCLELLNVGV DSKLVLKGII LLIVDKALEE PKYSSLYAQL CLRLAEDAPN
FDGPSSEIQT SQKQSTTFRR LLISKLQDEF ENRTRNVEIY DKHDNPLTSE EEEQRAIAKI
KMLGNIKFIG ELGKLDLIHE SILHKCIKTL LEKKKRVQLK DMGEDLECLC QIMRTVGPRL
DHEKAKSLMD QYFGRMRSLM NNKELPARIR FLLQDTVELR ENNWVPRKAF IDNGPKTINQ
IRQDAVKDLG VFIPAPMSQG MRMDFFLESP FMPNRMKLDR ETLGGLADMF GQMPGSGIGT
GPGVIQDRYS PTMGRHRTNP LFNGHSGHIA PPQQSQFDMG PKSFVKSNQI SLRPAQSFLL
NKNQVPKLQP QIPTMMPPSA QPPRTQTPPL GQPPQLGLKT NPPPIQEKPQ KTNKKPPPAK
EELLKTTEAI MTEYLNTKNL IEAVCGVREM KAPKHFLPEM LSKIIVCSLD RPDEDKEHAS
TLIHALRADG LITGENFMQA FLSVLDLCPK IELDVPLVKS YLAQFAARAV MAELVSVAEL
AHPLENGTHF PLFLLCLQQT AKLKDREWLT ELFQQSKVNM QKMLPEIDQN KDRMLEVLEG
KGLSFLFPLL KLEKELLKQI KADPSPQSIY KWIKDNISPR LHTDKGFVNI LMTSFLQYIS
QELCMAESDD QLAAPSKEQL EQEKQLLLAF KPVMQKFLHD HTELQVSALY ALQVHCNASS
FPKGMLLRYF VNFYDMEIIE EEAFLAWKED ITQEFPGKGK ALFQVNQWLT WLETAEEEES
EEEAD
//