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Database: UniProt
Entry: A0A0D9QX32_CHLSB
LinkDB: A0A0D9QX32_CHLSB
Original site: A0A0D9QX32_CHLSB 
ID   A0A0D9QX32_CHLSB        Unreviewed;       980 AA.
AC   A0A0D9QX32;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
GN   Name=EIF4G2 {ECO:0000313|Ensembl:ENSCSAP00000000921.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000000921.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000000921.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000000921.1}
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; AQIB01085255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9QX32; -.
DR   STRING; 60711.ENSCSAP00000000921; -.
DR   Ensembl; ENSCSAT00000002621.1; ENSCSAP00000000921.1; ENSCSAG00000004613.1.
DR   eggNOG; KOG0401; Eukaryota.
DR   GeneTree; ENSGT00940000154675; -.
DR   OMA; CAPLDIN; -.
DR   Proteomes; UP000029965; Chromosome 1.
DR   Bgee; ENSCSAG00000004613; Expressed in pituitary gland and 7 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0006446; P:regulation of translational initiation; IEA:Ensembl.
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:UP000029965};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          616..739
FT                   /note="MI"
FT                   /evidence="ECO:0000259|PROSITE:PS51366"
FT   DOMAIN          793..977
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   980 AA;  110166 MW;  2217A1FDC84905EE CRC64;
     MAGWQTPAGP RPWRTEARVC SDGEGARLGP RAPRREARGA SRRGGISFLP SPPLPTPSIN
     IILLKILRCQ AAKVESAIAE GGASRFSASS GGGGSRGAPQ HYPKTAGNSE FLGKTPGQNA
     QKWIPARSTR RDDNSAANNS ANEKERHDAI FRKVRGILNK LTPEKFDKLC LELLNVGVES
     KLILKGVILL IVDKALEEPK YSSLYAQLCL RLAEDAPNFD GPAAEGQPGQ KQSTTFRRLL
     ISKLQDEFEN RTRNVDVYDK RENPLLPEEE EQRAIAKIKM LGNIKFIGEL GKLDLIHESI
     LHKCIKTLLE KKKRVQLKDM GEDLECLCQI MRTVGPRLDH ERAKSLMDQY FARMCSLMLS
     KELPARIRFL LQDTVELREH HWVPRKAFLD NGPKTINQIR QDAVKDLGVF IPAPMAQGMR
     SDFFLEGPFM PPRMKIDRDP LGGLADMFGQ MPGSGIGTGP GVIQDRFSPT MGRHRSNQLF
     NGHGGHIMPP TQSQFGEMGG KFMKSQGLSQ LYHNQSQGLL SQLQGQSKDM PPRFSKKGQL
     NADEISLRPA QSFLMNKNQV PKLQPQITMI PPSAQPPRTQ TPPLGQTPQL GLKTNPPLIQ
     EKPAKTSKKP PPSKEELLKL TETVVTEYLN SGNANEAVNG VREMRAPKHF LPEMLSKVII
     LSLDRSDEDK EKASSLISLL KQEGIATSDN FMQAFLNVLD QCPKLEVDIP LVKSYLAQFA
     ARAIISELVS ISELAQPLES GTHFPLFLLC LQQLAKLQDR EWLTELFQQS KVNMQKMLPE
     IDQNKDRMLE ILEGKGLSFL FPLLKLEKEL LKQIKLDPSP QTIYKWIKDN ISPKLHVDKG
     FVNILMTSFL QYISSEVNPP SDETDSSSAP SKEQLEQEKQ LLLSFKPVMQ KFLHDHVDLQ
     VSALYALQVH CYNSNFPKGM LLRFFVHFYD MEIIEEEAFL AWKEDITQEF PGKGKALFQV
     NQWLTWLETA EEEESEEEAD
//
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