IF4G_CUCME
ID IF4G_CUCME Reviewed; 1888 AA.
AC A0A1S3C4H6; A0A1S3C501;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Eukaryotic translation initiation factor 4G {ECO:0000305};
DE Short=eIF-4G {ECO:0000305};
DE Short=eIF4G {ECO:0000305};
DE AltName: Full=Protein synthesis initiation factor 4G {ECO:0000305};
GN Name=eIF4G {ECO:0000303|PubMed:28522457};
GN ORFNames=LOC103496918 {ECO:0000312|RefSeq:XP_008457179.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. DHL92;
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 995-1084 IN COMPLEX WITH EIF4E,
RP MUTAGENESIS OF TYR-1050; LEU-1055; LEU-1056; PHE-1069; ILE-1075 AND
RP LEU-1078, AND INTERACTION WITH EIF4E.
RC STRAIN=cv. C46;
RX PubMed=28522457; DOI=10.1104/pp.17.00193;
RA Miras M., Truniger V., Silva C., Verdaguer N., Aranda M.A., Querol-Audi J.;
RT "Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal
RT Bipartite Binding Mode for Protein Translation.";
RL Plant Physiol. 174:1476-1491(2017).
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.
CC {ECO:0000250|UniProtKB:Q76E23}.
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 EIF4G (By similarity). Interacts
CC directly with eIF4E (PubMed:28522457). In higher plants two isoforms of
CC EIF4F have been identified, named isoform EIF4F and isoform EIF(iso)4F.
CC Isoform EIF4F has subunits p220 and p26, whereas isoform EIF(iso)4F has
CC subunits p82 and p28 (By similarity). {ECO:0000250|UniProtKB:Q76E23,
CC ECO:0000269|PubMed:28522457}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=X1 {ECO:0000303|PubMed:22753475};
CC IsoId=A0A1S3C4H6-1; Sequence=Displayed;
CC Name=2; Synonyms=X2 {ECO:0000303|PubMed:22753475};
CC IsoId=A0A1S3C4H6-2; Sequence=VSP_061242;
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000305}.
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DR RefSeq; XP_008457179.1; XM_008458957.2.
DR PDB; 5ME5; X-ray; 1.90 A; B=995-1084.
DR PDBsum; 5ME5; -.
DR SMR; A0A1S3C4H6; -.
DR GeneID; 103496918; -.
DR KEGG; cmo:103496918; -.
DR eggNOG; KOG0401; Eukaryota.
DR OrthoDB; 594395at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR23253; PTHR23253; 2.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS51366; MI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Initiation factor;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..1888
FT /note="Eukaryotic translation initiation factor 4G"
FT /id="PRO_0000454072"
FT DOMAIN 1239..1462
FT /note="MIF4G"
FT /evidence="ECO:0000255"
FT DOMAIN 1700..1824
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1093
FT /note="EIF4E-binding"
FT /evidence="ECO:0000269|PubMed:28522457,
FT ECO:0007744|PDB:5ME5"
FT REGION 1083..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1462..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1639..1691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 92..93
FT /note="Missing (in isoform 2)"
FT /id="VSP_061242"
FT MUTAGEN 1050
FT /note="Y->A: Impaired eIF4E binding; when associated with
FT A-1055, A-1056, D-1069, D-1075 and D-1078."
FT /evidence="ECO:0000269|PubMed:28522457"
FT MUTAGEN 1055
FT /note="L->A: Impaired eIF4E binding; when associated with
FT A-1050, A-1056, D-1069, D-1075 and D-1078."
FT /evidence="ECO:0000269|PubMed:28522457"
FT MUTAGEN 1056
FT /note="L->A: Impaired eIF4E binding; when associated with
FT A-1050, A-1055, D-1069, D-1075 and D-1078."
FT /evidence="ECO:0000269|PubMed:28522457"
FT MUTAGEN 1069
FT /note="F->D: Impaired eIF4E binding; when associated with
FT A-1050, A-1055, A-1056, D-1075 and D-1078."
FT /evidence="ECO:0000269|PubMed:28522457"
FT MUTAGEN 1075
FT /note="I->D: Impaired eIF4E binding; when associated with
FT A-1050, A-1055, A-1056, D-1069 and D-1078."
FT /evidence="ECO:0000269|PubMed:28522457"
FT MUTAGEN 1078
FT /note="L->D: Impaired eIF4E binding; when associated with
FT A-1050, A-1055, A-1056, D-1069 and D-1075."
FT /evidence="ECO:0000269|PubMed:28522457"
FT HELIX 1052..1057
FT /evidence="ECO:0007829|PDB:5ME5"
FT HELIX 1058..1061
FT /evidence="ECO:0007829|PDB:5ME5"
FT HELIX 1073..1078
FT /evidence="ECO:0007829|PDB:5ME5"
SQ SEQUENCE 1888 AA; 204786 MW; 4DDF6CA7C2912AA5 CRC64;
MSFNQSRSDK NEGYTQYRKS GRSNNFNPQR GSSGTHSKPG GAGGSAPTSS IASNRSFKKT
NNAQGGQSRG GLPAVNSTDS SNAPNPRGVQ NGAVAKPPEG PHSQRSTRDV PKAPTSQSAP
LSSDGPAPTT PAKGTGDQPK EFAFQFGSIS PGFMNGMQLP VRTSSAPPNL DEQKRDQARH
ESFRPVPPMP IPLAPKPQTQ RKDTGAGDQP NVGQQLQQKD TGIINQPNTG DAHTVQKAKK
DMQASPNHPT NQTQKPTTPM SGISMTMPYH PPQVPVPFGG PNQQMQSQGL TPTSLHMSIP
VPLQIGSSPQ VQQPMFVPGL HPHPMQPQGI IHQGQGLGFA TQIGSQLPPQ LSNLGMNVTS
QYPQQQGGKF GGPRKSAVRI TDPKTHEELI FDNKQSNAYA DTGTSGPRPP YNLPSQTQPL
PYAPSHAMNY YPNSYNPNPL YFASPSSLPL PSGQSAPNSQ PHRFNYPVSQ GSQNVPYIDM
HVKKPSGGPM HGISDPPNRE HTRDTHTFQP PAPSGTVHVT IKMPTDPTGG KGSDTLPNKL
PTTEEGKSQK PSSPSVDLIP PSQRAVDTTS ESSLHDSKLG REPSGIKSSP VISKQFTDGP
PMVSLESQDS SSVQSSLTAS SEESELAVAH SEVRRENLLG SDLHKDHQKK TSKKGYAQSL
QHQISGQASS ALGVPCQVQD TTSPLVSEAV EAKSLIIPAV VGGKSVSVSA VTSDPLESKD
AGLVSVAHSS SPENPGLGNV KNLDLISDDN QDTSSKEKNS EPVVLKIEEQ GQATFSEPPV
DLKNSENVLD HDVSKSVEVA EKTERNLIVS SATVSNEVLT SETAQRAVDE PVSCNAEADV
SASVSSSSTV PENSQDDKLV VDSSGRYDNM SSNEVLKNVV KSDQPSEPAL NPGLSEGKND
GEVLDTVGTC ANSSQGVSGT KDKSVVETSR VKGTTGKAKK RLKAILQMAD AAGTTSDLYN
AYKRPEEKKE TVAHSESIER TESRSSSVDT EQESNEAIKE DAGALSKAEP DDWEDAADIA
TPDLESANGD GVGTSMLDSG DRTGDMAKKY SRDFLLKFAE QFLDLPHNFE VTSDIESLMS
THTNVSHHHD RDPYPSPGRV DRPSSGGSRL DRRGSNLVDD DRWSKLPGPF APGQDPRLDL
AYGATAGFRP GQGPNFGVLR NPRAQAPVQY AGGILAGPMQ SMGPQGGLQR NNSDADRWQR
ATNFQKGLIP SPLTPLQTMH KAKKKYEVGK VSDEEETKQR QLKAILNKLT PQNFEKLFEQ
VKAVNIDNGR TLTGVISQIF DKALMEPTFC EMYANFCFHL AGELPDLSED NEKITFKRLL
LNKCQEEFER GEREQEEANK VEEEGEVKQS EEEREEKRIK ARRRMLGNIR LIGELYKKKM
LTERIMHECI KKLLGEYQNP DEEDVEALCK LMSTIGEMID HPRAKDYMDS YFEIMTMLSN
NMKLSSRVRF MLKDAIDLRK NKWQQRRKVE GPKKIEEVHR DAAQERQAQT GRFGRGPSIN
SSARRGGPPM DYGPRGSVVS SPGNQMGGFR AFLHQPRGYG GNQDARQDER QSYEARTLSV
TSQRAGGDES ITLGPQGGLA RGMSIRGPQP SSAAPADMSP LPGDLRSAPI ASLNGYSSAS
ERATLTSKED LISRHMPERF AGPTSMDHIS SPERYSNYGN KDLRHSGRSF DRSRPISPAT
PPGPALTPSL PSEKVLSEDR LQQLSLTAIK EFYSARDEKE VALCIKELNS PAFHPTMISL
WVTDVFERTN LERDLLAKLV VNLSRPNNGT LNQAHLVKGF EAVLGNLEDS VNDAPRAPEY
LGQILGKVIT ESMVSLREVA DLICQGGEVP GNLLQSGLGA DVLGNILKTI KTEKGEGFLT
DLRTNSNLRL ETFLPPDPVK SRVLEEFI
