IF4G2_BOVIN
ID IF4G2_BOVIN Reviewed; 907 AA.
AC Q95L46; A8R456; O18948;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 112.
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;
DE AltName: Full=p97;
GN Name=EIF4G2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000312|EMBL:AAL30507.1};
RN [1] {ECO:0000312|EMBL:AAL30507.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAL30507.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 514-649.
RA Smith T.P.L., Bennett G.L.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 539-639.
RC TISSUE=Vascular smooth muscle;
RX PubMed=10483320; DOI=10.1024/0301-1526.28.3.164;
RA Alfke H., Stumm G., Schnieder I., Klose K.J., Schlegel J.;
RT "Differential gene expression of vascular smooth muscle cells. Detection by
RT RNA arbitrarily primed polymerase chain reaction.";
RL VASA 28:164-168(1999).
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|UniProtKB:P78344}.
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|UniProtKB:P78344}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000305}.
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DR EMBL; BC122631; AAI22632.1; -; mRNA.
DR EMBL; AF420315; AAL30507.1; -; Genomic_DNA.
DR EMBL; AF011353; AAB64296.1; -; mRNA.
DR RefSeq; NP_001093329.1; NM_001099859.1.
DR AlphaFoldDB; Q95L46; -.
DR SMR; Q95L46; -.
DR STRING; 9913.ENSBTAP00000049614; -.
DR PaxDb; Q95L46; -.
DR PRIDE; Q95L46; -.
DR GeneID; 286870; -.
DR KEGG; bta:286870; -.
DR CTD; 1982; -.
DR eggNOG; KOG0401; Eukaryota.
DR InParanoid; Q95L46; -.
DR OrthoDB; 594395at2759; -.
DR Proteomes; UP000009136; 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_0000213324"
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 557
FT /note="N -> Y (in Ref. 1; AAI22632)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="Q -> R (in Ref. 3; AAB64296)"
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
