IF4G1_RABIT
ID IF4G1_RABIT Reviewed; 1402 AA.
AC P41110;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 1;
DE Short=eIF-4-gamma 1;
DE Short=eIF-4G 1;
DE Short=eIF-4G1;
DE AltName: Full=p220;
GN Name=EIF4G1; Synonyms=EIF4G;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 479-500.
RC STRAIN=New Zealand white; TISSUE=Brain;
RX PubMed=8396129; DOI=10.1016/s0021-9258(19)36499-3;
RA Lamphear B.J., Yan R., Yang F., Waters D., Liebig H.-D., Klump H.,
RA Kuechler E., Skern T., Rhoads R.E.;
RT "Mapping the cleavage site in protein synthesis initiation factor eIF-4
RT gamma of the 2A proteases from human Coxsackievirus and rhinovirus.";
RL J. Biol. Chem. 268:19200-19203(1993).
RN [2]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1429670; DOI=10.1016/s0021-9258(18)50080-6;
RA Yan R., Rychlik W., Etchison D., Rhoads R.E.;
RT "Amino acid sequence of the human protein synthesis initiation factor eIF-4
RT gamma.";
RL J. Biol. Chem. 267:23226-23231(1992).
CC -!- FUNCTION: Component of the protein complex eIF4F, which is involved in
CC the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal
CC secondary structure and recruitment of mRNA to the ribosome. As a
CC member of the eIF4F complex, required for endoplasmic reticulum stress-
CC induced ATF4 mRNA translation (By similarity).
CC {ECO:0000250|UniProtKB:Q04637}.
CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions. It is
CC composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. Interacts with
CC eIF3, mutually exclusive with EIF4A1 or EIFA2, EIF4E and through its N-
CC terminus with PAPBC1. Interacts through its C-terminus with the
CC serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a
CC scaffold protein, holding these enzymes in place to phosphorylate
CC EIF4E. Interacts with EIF4E3. Interacts with CIRBP and MIF4GD.
CC Interacts with RBM4. Interacts with HNRNPD/AUF1; the interaction
CC requires RNA (By similarity). Directly interacts with EIF4G1 in an RNA-
CC independent manner (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q04637}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q04637}.
CC -!- PTM: Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-
CC 988 by PRKCA induces binding to MKNK1.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000305}.
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DR EMBL; L22090; AAA31242.1; -; mRNA.
DR PIR; I46707; I46707.
DR AlphaFoldDB; P41110; -.
DR SMR; P41110; -.
DR STRING; 9986.ENSOCUP00000005299; -.
DR PRIDE; P41110; -.
DR eggNOG; KOG0401; Eukaryota.
DR eggNOG; KOG3571; Eukaryota.
DR InParanoid; P41110; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0036493; P:positive regulation of translation in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR037584; EIF4G1.
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 PANTHER; PTHR23253:SF10; PTHR23253:SF10; 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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Initiation factor;
KW Methylation; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW RNA-binding; Translation regulation.
FT CHAIN 1..1402
FT /note="Eukaryotic translation initiation factor 4 gamma 1"
FT /id="PRO_0000213323"
FT DOMAIN 567..793
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 1044..1166
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 1231..1401
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 490
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 499
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 836
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 846
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 899
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 950
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 988
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 990
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 997
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1012
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1014
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
SQ SEQUENCE 1402 AA; 154051 MW; 7FD85D7E30519230 CRC64;
MSGARTVSTP TPPQTGGGVE PQANGETPQV AVIVRSDDRS QGAIIGGRPG LPGPEHSPSE
SQPSSPSPTP SPPPILEPGS EPNLAVLSLP GDTMTSGMIQ MPVEEPAPIS REAGEPYCLS
PEPTPLAEPI LEVEVTLSKP VPVSEFSSSP IQVLTPLASH KMEIHEPNGV VPSEDLEPEV
ESSPELAPPP PPACLSESPV PIAPTTQPEE LLNGAPSPPA VDLSPVCEPE DQAKEDTASA
TPPAVPSATP ATAPPATSPA QEEEGEEEEE EEEGEAGAAE SDKGGEDLHP TESTPVPGHL
PQNVEAVAAT QVAVSVPKRR RKIKELNKKE AVGDLLDAFK EVNPAVPEVE NQPPAGNNPT
PESEGSSGPS RPEEADETWD AKEDKIHNAE NIQPGEQKYE YKSDQWRPLN LEEKKRYDRE
FLLGFQFIFC QYAEAGGLPH ISDVVLEKAN KTPLRPLDPS RLSGINCGPD FTPSFANLGR
PALSSRGPPR GGPGGELPRG AAGLGPRRSL QPRPPKGARK LIASVIMTED IKLNKAEKAW
KPSSKRTAAD KDRGEEDADG SKTQDLFRRV RSILNKLTPQ MFQQLMKQVT QLAIDTEGAS
KGSLTSSLRR PFQNPTSQWP SQHVPLPHGA ESATTEKPTV TVNFRKLLLN RCQKEFEKDK
DDDEVFEKKQ KEMDEAATAE ERERLKEELE EARDIARRCS LGNIKFIGEL FKLKMLTEAI
MHDCVVKLLR HDEESLEFLC RLLTTIGKDL DFEKAKPRMD QYFNQMEKII KEKKTSSRIR
FMLQDVLDLR QSNWVPRRGD QGPKTIDQIH KEAEMEEHRE HIKVQQLMAK GSDKRRGGPP
GPPISRGLPL VDDGGWNTVP ISKGSRPIDT SRLTKITKPG SIDSNNQLFA PGGRLSWGKG
SSGSGAKPSD AASEVSRPAT STLNRFSALQ QAVPTESTDN RRVVQRSSLS RERGGKAGEP
RRRLERSERG GDRGDRLDRA RTPATKRSFS KEVEERSRER PSQPEGLRKA ASLTEDRDRG
RDAAKREAAL PPVSCAKAAL SEEELEKKSK AIIEEYLHLN DMKEAVQCVQ ELASPSLLFI
FVRHGIESTL ERSAIARERM GQLLHQLLCA GHLSTAQYYQ GLYEILELAE DMEIDIPHVW
LYLAELVTPI MQEGGVPMGE LFREITKHLR PLGKAASLLL EILRLLCKSK GPKKVAYCGV
RLGSAGKNFC LEGQDVGAFI TEQKVEYTLG EESEAPGQRA LSSEELSRQL EKVLKEGSSN
QRVFDWIEAN LSEQQIASNT LVRALMTAVC YSAIIFETPL RVDVAVLKGD RICYRNTCVI
AEGAARLYAL QALVVTLEQP ANLLRMFFDA LYDEDVVKEE AFYSWESSKD PAEQQGKGVA
LKSVTAFFKW LREVEEEESD HN
