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Database: UniProt
Entry: A0A2R9A2L4_PANPA
LinkDB: A0A2R9A2L4_PANPA
Original site: A0A2R9A2L4_PANPA 
ID   A0A2R9A2L4_PANPA        Unreviewed;       869 AA.
AC   A0A2R9A2L4;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
GN   Name=EIF4G2 {ECO:0000313|Ensembl:ENSPPAP00000011532.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000011532.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000011532.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000011532.1}
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; AJFE02062104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2R9A2L4; -.
DR   SMR; A0A2R9A2L4; -.
DR   Ensembl; ENSPPAT00000034190.1; ENSPPAP00000011532.1; ENSPPAG00000028909.1.
DR   GeneTree; ENSGT00940000154675; -.
DR   OMA; CAPLDIN; -.
DR   Proteomes; UP000240080; Chromosome 11.
DR   Bgee; ENSPPAG00000028909; Expressed in heart and 6 other cell types or tissues.
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:UP000240080};
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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