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IF4G_WHEAT
ID   IF4G_WHEAT              Reviewed;        1488 AA.
AC   G5CEW6;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Eukaryotic translation initiation factor 4G;
DE            Short=eIF-4G;
DE            Short=eIF4G;
DE   AltName: Full=Eukaryotic initiation factor 4F subunit p220;
DE            Short=eIF-4F p220 subunit;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RX   PubMed=21965660; DOI=10.1074/jbc.m111.280099;
RA   Mayberry L.K., Allen M.L., Nitka K.R., Campbell L., Murphy P.A.,
RA   Browning K.S.;
RT   "Plant cap-binding complexes eukaryotic initiation factors eIF4F and
RT   eIFiso4F: molecular specificity of subunit binding.";
RL   J. Biol. Chem. 286:42566-42574(2011).
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}.
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. In higher plants two
CC       isoforms of EIF4F have been identified, named isoform EIF4F and isoform
CC       EIF(iso)4F. Isoform EIF4F has subunits p220 and p26, whereas isoform
CC       EIF(iso)4F has subunits p82 and p28. {ECO:0000269|PubMed:21965660}.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC       {ECO:0000305}.
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DR   EMBL; JN091779; AEQ49596.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5CEW6; -.
DR   SMR; G5CEW6; -.
DR   STRING; 4565.Traes_2BS_80474BB5B.1; -.
DR   eggNOG; KOG0401; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; G5CEW6; baseline.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
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   Initiation factor; Protein biosynthesis; Reference proteome;
KW   Translation regulation.
FT   CHAIN           1..1488
FT                   /note="Eukaryotic translation initiation factor 4G"
FT                   /id="PRO_0000420547"
FT   DOMAIN          883..1106
FT                   /note="MIF4G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT   DOMAIN          1299..1423
FT                   /note="MI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT   REGION          196..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..721
FT                   /note="EIF4E-binding"
FT   REGION          753..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          974..1000
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1107..1299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..296
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..535
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..679
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..781
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1107..1132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1179..1193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1242..1257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1271..1291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1488 AA;  162229 MW;  4031EFB00C8C8528 CRC64;
     MMHQGQTMMY PSVAHPIPPQ LGNVNLNMAS QYPQQQQNKL VAPRKSSNIK ITDPNTNKEV
     VLGRPSPNVA AQPQQVSGVA TQPMVYYTNP QQTSYNQSGT YYSGTAGVVP TGSQGRFGYP
     ATQAGQSIPF MNPSMSNTVP ASHKDNIAGP APSGQSQLIG KPQGGLHMEK PVPSVKISMP
     AGRSDASKFR VADHAVQHRQ KDNEVISGAM VSNKPVSEKE SKAPSIPEKH SKESKAPSAV
     EKHPTAVTQP LPIQAAKPET DAATANSPSF LTGADEKKES LPMTDSLKDN KKNATRNDTK
     NLPQQPQSAS PAEELKGQTS VKLGDDVVGH METKSFDSEK VDLTSKVSGL TSATSESSIS
     PILGKSEADS TSVNAADVPA MVISSAKLSS ASTGEPQAVE SLGVAAVKSK EIEITHQISP
     ESSDGKIMSD STENESHDFT VDLAEQASLA TSKPGNSDAT SFVTDPQELP KECTTSVPED
     HSLMNTSHNK DTQTLSASVD ASDVSEVNSG TSSESTSQST NDKDIRSSIQ ETGLAVSGIT
     PGMLPVNHSV ASEGQVKHAD GAKDESSTEQ SSAVPTGSVR PLSREKPTAE LARTKSTAGR
     KKKRKEMLSK ADAAGSSDLY NAYKGPQEQS ESVATSDGAD SSSTVDGTHV LPEESEREVM
     CEDDGKKKVE PDDWEDAADM STPKLQSSDS GNQASAVQLP DSDMTEANGR KKYSRDFLLT
     FAHQYSSLPV GIRMDTVTST LFKDLAGKSY VIDREPHPSS ARGSDRPTSR GDRRGPAMDD
     DKWLKSGVPY SPNRDAHMDL TNGPAINYRG GPGGAHGVLR NPRGALLVGP QSNAPQVPRS
     GSDADRWQQK GLIPSPVTPM QVMHKAEKKY VVGKVSDEEQ AKQRQLKAIL NKLTPQNFDK
     LFEQVKEVNI DNVSTLTGVI SQIFDKALME PTFCEMYANF CSHLAGALPD FSEDNEKITF
     KRLLLNKCQE EFERGEREEA EADKTEEEGE IKQTKEEREE KRVKARRRML GNIRLIGELY
     KKRMLTERIM HECIKKLLGN YQNPDEENIE ALCKLMSTIG EMIDHPKAKE HMDAYFDRMR
     NLSTSQLISS RVRFLLRDSI DLRKNKWQQR RKVDGPKKID EVHRDAAQER HAQSSRSRGP
     VVSSLPRRGA PSMDYGSRGS AAPLVSPGPQ QRGRGFGNQD IRYEQERHQF DRTVPLPQRS
     VKDEAITLGP QGGLARGMSL RGQPPVSNSE LPSVVDQRRI LSGPNGYNSV PSTTREDTSS
     RIPDRFSGRI ATAAQSASSS HRPASQEGRS GNKSYSEEEL REKSIATIRE YYSAKDEKEV
     ALCIEELNAP SFYPSLVSLW VNDSFERKDM ERELLAKLFV GLYNGGYNLL SKPQLIEGLS
     SVLASLEDAL SDSPRAAEYL GRLLARFVVE KILVLQDVGK LIEEGGEEPG HLVQEGIAAD
     VLGAVLEWIR TEKGDSFLKE AKTSSNLKLE DFRPQHLKRS KLDAFMLT
 
 
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