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Database: UniProt
Entry: H2NE36_PONAB
LinkDB: H2NE36_PONAB
Original site: H2NE36_PONAB 
ID   H2NE36_PONAB            Unreviewed;       869 AA.
AC   H2NE36; A0A2J8UPY3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
GN   Name=EIF4G2 {ECO:0000313|Ensembl:ENSPPYP00000004000.2};
GN   ORFNames=CR201_G0026049 {ECO:0000313|EMBL:PNJ47317.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000004000.2, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000004000.2, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ47317.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ47317.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000004000.2}
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; NDHI03003449; PNJ47317.1; -; Genomic_DNA.
DR   Ensembl; ENSPPYT00000004155.2; ENSPPYP00000004000.2; ENSPPYG00000003485.2.
DR   GeneTree; ENSGT00940000154675; -.
DR   HOGENOM; CLU_001519_3_0_1; -.
DR   TreeFam; TF101528; -.
DR   Proteomes; UP000001595; Chromosome 11.
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:UP000001595};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          505..628
FT                   /note="MI"
FT                   /evidence="ECO:0000259|PROSITE:PS51366"
FT   DOMAIN          682..866
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   869 AA;  98118 MW;  63ADF31E871EF0ED CRC64;
     VESAIAEGGA SRFSASSGGG GSRGAPQHYP KTAGNSEFLG KTPGQNAQKW IPARSTRRDD
     NSAANNSANE KERHDAIFRK VRGILNKLTP EKFDKLCLEL LNVGVESKLI LKGVILLIVD
     KALEEPKYSS LYAQLCLRLA EDAPNFDGPA AEGQPGQKQS TTFRRLLISK LQDEFENRTR
     NVDVYDKREN PLLPEEEEQR AIAKIKMLGN IKFIGELGKL DLIHESILHK CIKTLLEKKK
     RVQLKDMGED LECLCQIMRT VGPRLDHERA KSLMDQYFAR MCSLMLSKEL PARIRFLLQD
     TVELREHHWV PRKAFLDNGP KTINQIRQDA VKDLGVFIPA PMAQGMRSDF FLEGPFMPPR
     MKMDRDPLGG LADMFGQMPG SGIGTGPGVI QDRFSPTMGR HRSNQLFNGH GGHIMPPTQS
     QFGEMGGKFM KSQISLRPAQ SFLMNKNQVP KLQPQITMIP PSAQPPRTQT PPLGQTPQLG
     LKTNPPLIQE KPAKTSKKPP PSKEELLKLT ETVVTEYLNS GNANEAVNGV REMRAPKHFL
     PEMLSKVIIL SLDRSDEDKE KASSLISLLK QEGIATSDNF MQAFLNVLDQ CPKLEVDIPL
     VKSYLAQFAA RAIISELVSI SELAQPLESG THFPLFLLCL QQLAKLQDRE WLTELFQQSK
     VNMQKMLPEI DQNKDRMLEI LEGKGLSFLF PLLKLEKELL KQIKLDPSPQ TIYKWIKDNI
     SPKLHVDKGF VNILMTSFLQ YISSEVNPPS DETDSSSAPS KEQLEQEKQL LLSFKPVMQK
     FLHDHVDLQV SALYALQVHC YNSNFPKGML LRFFVHFYDM EIIEEEAFLA WKEDITQEFP
     GKGKALFQVN QWLTWLETAE EEESEEEAD
//
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