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Database: UniProt
Entry: A0A3P9N5M4_POERE
LinkDB: A0A3P9N5M4_POERE
Original site: A0A3P9N5M4_POERE 
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
//
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