IF4G2_PONAB
ID IF4G2_PONAB Reviewed; 907 AA.
AC Q5R7J9; Q5RB54;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2;
DE Short=eIF-4-gamma 2;
DE Short=eIF-4G 2;
DE Short=eIF4G 2;
GN Name=EIF4G2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the serine/threonine protein kinases MKNK1 and
CC MKNK2. Binds EIF4A and EIF3. Interacts with MIF4GD (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation; hyperphosphorylated during mitosis.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: This gene has been shown to be extensively edited in the
CC liver of APOBEC1 transgenic animals. Its aberrant editing could
CC contribute to the potent oncogenesis induced by overexpression of
CC APOBEC1. The aberrant edited sequence, called NAT1, is likely to be a
CC fundamental translational repressor (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858801; CAH91006.1; -; mRNA.
DR EMBL; CR860116; CAH92261.1; -; mRNA.
DR AlphaFoldDB; Q5R7J9; -.
DR SMR; Q5R7J9; -.
DR STRING; 9601.ENSPPYP00000004000; -.
DR eggNOG; KOG0401; Eukaryota.
DR InParanoid; Q5R7J9; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008135; F:translation factor activity, RNA binding; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
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; PTHR23253; 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; SSF48371; 3.
DR PROSITE; PS51366; MI; 1.
DR PROSITE; PS51363; W2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Initiation factor; Isopeptide bond; Methylation;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Repressor;
KW Translation regulation; Ubl conjugation.
FT CHAIN 1..907
FT /note="Eukaryotic translation initiation factor 4 gamma 2"
FT /id="PRO_0000316289"
FT DOMAIN 78..308
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 543..666
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 720..904
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..541
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"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 360
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 431
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 505
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 508
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT CROSSLNK 575
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT CONFLICT 41
FT /note="K -> E (in Ref. 1; CAH91006)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="G -> R (in Ref. 1; CAH91006)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="M -> V (in Ref. 1; CAH92261)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="L -> P (in Ref. 1; CAH91006)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="P -> S (in Ref. 1; CAH92261)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 907 AA; 102362 MW; 4EF050B5EEA4DF91 CRC64;
MESAIAEGGA 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 KSQGLSQLYH NQSQGLLSQL QGQSKDMPPR FSKKGQLNAD EISLRPAQSF
LMNKNQVPKL QPQITMIPPS AQPPRTQTPP LGQTPQLGLK TNPPLIQEKP AKTSKKPPPS
KEELLKLTET VVTEYLNSGN ANEAVNGVRE MRAPKHFLPE MLSKVIILSL DRSDEDKEKA
SSLISLLKQE GIATSDNFMQ AFLNVLDQCP KLEVDIPLVK SYLAQFAARA IISELVSISE
LAQPLESGTH FPLFLLCLQQ LAKLQDREWL TELFQQSKVN MQKMLPEIDQ NKDRMLEILE
GKGLSFLFPL LKLEKELLKQ IKLDPSPQTI YKWIKDNISP KLHVDKGFVN ILMTSFLQYI
SSEVNPPSDE TDSSSAPSKE QLEQEKQLLL SFKPVMQKFL HDHVDLQVSA LYALQVHCYN
SNFPKGMLLR FFVHFYDMEI IEEEAFLAWK EDITQEFPGK GKALFQVNQW LTWLETAEEE
ESEEEAD
