ID A0A2U3XAS9_LEPWE Unreviewed; 701 AA.
AC A0A2U3XAS9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
GN Name=EIF4G2 {ECO:0000313|RefSeq:XP_006728585.1,
GN ECO:0000313|RefSeq:XP_030873303.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006728585.1};
RN [1] {ECO:0000313|RefSeq:XP_006728585.1, ECO:0000313|RefSeq:XP_030873303.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006728585.1,
RC ECO:0000313|RefSeq:XP_030873303.1};
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_006728585.1; XM_006728522.2.
DR RefSeq; XP_030873303.1; XM_031017443.1.
DR STRING; 9713.A0A2U3XAS9; -.
DR GeneID; 102741628; -.
DR KEGG; lww:102741628; -.
DR CTD; 1982; -.
DR OrthoDB; 92033at2759; -.
DR Proteomes; UP000245341; Unplaced.
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_006728585.1,
KW ECO:0000313|RefSeq:XP_030873303.1};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Protein biosynthesis {ECO:0000313|RefSeq:XP_006728585.1,
KW ECO:0000313|RefSeq:XP_030873303.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341};
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; C42BF4EC7EB634BD 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 NSGNANEAVS
GVREMRAPKH FLPEMLSKVI ILSLDRSDED KEKASSLISL LKQEGIATSD NFMQAFLNVL
DQCPKLEVDI PLVKSYLAQF AARAIISELV SISELAQPLE SGTHFPLFLL CLQQLAKLQD
REWLTELFQQ SKVNMQKMLP EIDQNKDRML EILEGKGLSF LFPLLKLEKE LLKQIKLDPS
PQTIYKWIKD NISPKLHVDK GFVNILMTSF LQYISSEVNP PSDETDSSSA PSKEQLEQEK
QLLLSFKPVM QKFLHDHVDL QVSALYALQV HCYHSNFPKG MLLRFFVHFY DMEIIEEEAF
LAWKEDITQE FPGKGKALFQ VNQWLTWLET AEEEESEEEA D
//
