ID A0A455C865_PHYMC Unreviewed; 701 AA.
AC A0A455C865;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
GN Name=EIF4G2 {ECO:0000313|RefSeq:XP_028357332.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028357332.1};
RN [1] {ECO:0000313|RefSeq:XP_028357332.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028357332.1};
RG RefSeq;
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 RefSeq; XP_028357332.1; XM_028501531.2.
DR AlphaFoldDB; A0A455C865; -.
DR KEGG; pcad:102986567; -.
DR InParanoid; A0A455C865; -.
DR OrthoDB; 92033at2759; -.
DR Proteomes; UP000248484; Chromosome 16.
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 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 Initiation factor {ECO:0000313|RefSeq:XP_028357332.1};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Protein biosynthesis {ECO:0000313|RefSeq:XP_028357332.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 337..460
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 514..698
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 292..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 79610 MW; 58C27D495ECC8AFA CRC64;
MLGNIKFIGE LGKLDLIHES ILHKCIKTLL EKKKRVQLKD MGEDLECLCQ IMRTVGPRLD
HERAKSLMDQ YFARMCSLML SKELPARIRF LLQDTVELRE HHWVPRKAFL DNGPKTINQI
RQDAVKDLGV FIPAPMAQGM RSDFFLEGPF MPPRMKMDRD PLGGLADMFG QMPGSGIGTG
PGVIQDRFSP TMGRHRSNQL FNGHGGHIMP PTQSQFGEMG GKFMKSQGLS QLYHNQSQGL
LSQLQGQSKD MPPRFSKKGQ LNADEISLRP AQSFLMNKNQ VPKLQPQITM IPPSAQPPRT
QTPPLGQTPQ LGLKTNPPLI QEKPAKTSKK PPPSKEELLK LTETVVTEYL NSGNANEAVN
GVREMRAPKH FLPEMLSKVI ILSLDRSDED KEKASSLISL LKQEGIATSD NFMQAFLNVL
DQCPKLEVDI PLVKSYLAQF AARAIISELV SISELAQPLE SGTHFPLFLL CLQQLAKLQD
REWLTELFQQ SKVNMQKMLP EIDQNKDRML EILEGKGLSF LFPLLKLEKE LLKQIKLDPS
PQTIYKWIKD NISPKLHVDK GFVNILMTSF LQYISSEVNP PSDEPDSSSA PSKEQLEQEK
QLLLSFKPVM QKFLHDHVDL QVSALYALQV HCYNSNFPKG MLLRFFVHFY DMEIIEEEAF
LAWKEDITQE FPGKGKALFQ VNQWLTWLET AEEEESEEEA D
//
