ID G3RDI1_GORGO Unreviewed; 1603 AA.
AC G3RDI1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Eukaryotic translation initiation factor 4 gamma 1 {ECO:0000313|Ensembl:ENSGGOP00000013587.3};
GN Name=EIF4G1 {ECO:0000313|Ensembl:ENSGGOP00000013587.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000013587.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000013587.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000013587.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000013587.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000256|ARBA:ARBA00005775}.
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DR EMBL; CABD030025990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030025991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004038170.2; XM_004038122.2.
DR RefSeq; XP_004038173.2; XM_004038125.2.
DR STRING; 9593.ENSGGOP00000013587; -.
DR Ensembl; ENSGGOT00000013978.3; ENSGGOP00000013587.3; ENSGGOG00000013919.3.
DR GeneID; 101151159; -.
DR CTD; 1981; -.
DR eggNOG; KOG0401; Eukaryota.
DR GeneTree; ENSGT00940000154648; -.
DR InParanoid; G3RDI1; -.
DR OMA; PRGGPNM; -.
DR OrthoDB; 92033at2759; -.
DR TreeFam; TF101527; -.
DR Proteomes; UP000001519; Chromosome 3.
DR Bgee; ENSGGOG00000013919; Expressed in testis and 5 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005840; C:ribosome; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; ISS:AgBase.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IEA:Ensembl.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:1905537; P:positive regulation of eukaryotic translation initiation factor 4F complex assembly; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:1904377; P:positive regulation of protein localization to cell periphery; IEA:Ensembl.
DR GO; GO:0036493; P:positive regulation of translation in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:Ensembl.
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:SF10; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 1; 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; ARM repeat; 3.
DR PROSITE; PS51366; MI; 1.
DR PROSITE; PS51363; W2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT DOMAIN 1245..1367
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 1437..1603
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..280
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..479
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1603 AA; 175909 MW; 1A9DB3F0A40B3552 CRC64;
MNKAPQSTGP PPAPSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQG GFRSLQHFYP
SRAQPPSSAA SRVQSAAPAR PGPAAHVYPA GSQVMMIPSQ ISYPASQGAY YIPGQGRSTY
VVPTQQYPVQ PGAPGFYPGA SPTEFGTYAG AYYPAQGVQQ FPTGVAPAPV LMNQPPQIAP
KRERKTIRIR DPNQGGKDIT EEIMSGARTA STPTPPQTGG GLEPQANGET PQVAVIVRPD
DRSQGAIIAD RPGLPGPEHS PSESQPSSPS PTPSPSPVLE PGSEPNLAVL SIPGDTMTTI
QMSVEESTPI SRETGEPYRL SPEPTPLAEP ILEVEVTLSK PVPESEFSSS PLQAPTPLAS
HTVEIHEPNG MVPSEDLEPE VESSAELAPP PACPSESPVP IAPTAQPEEL LNGAPSPPAV
DLSPVSEPEE QAKEVTASVA PPTIPSATPA TAPSATSPAQ EEEMEEEEEE EEGEAGEAES
EKGGEELLPP ESTPIPANLS QNLEAAAATQ VAVSVPKRRR KIKELNKKEA VGDLLDAFKE
VNPAVPEVEN QPPAGSNPGP ESEGSSVPPR PEEADETWDS KEDKIHNAEN IQPGEQKYEY
KSDQWKPLNL EEKKRYDREF LLGFQFIFAS MQKPEGLPHI SDVVLDKANK TPLRPLDPTR
LQGINCGPDF TPSFANLGRT TLSTRGPPRG GPGGELPRGP AGLGPRRSQQ GPRKEPRKII
ATVLMTEDIK LNKAEKAWKP SSKRTAADKD RGEEDADGSK TQDLFRRVRS ILNKLTPQMF
QQLMKQVTQL AIDTEERLKG VIDLIFEKAI SEPNFSVAYA NMCRCLMALK VPTTEKPTVT
VNFRKLLLNR CQKEFEKDKD DDEVFEKKQK EMDEAASAEE RGRLKEELEE ARDIARRRSL
GNIKFIGELF KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFEKAKPRMD
QYFNQMEKII KEKKTSSRIR FMLQDVLDLR GSNWVPRRGD QGPKTIDQIH KEAEMEEHRE
HIKVQQLMAK GSDKRRGGPP GPPISRGLPL VDDGGWNTVP ISKGSRPIDT SRLTKITKPG
SIDSNNQLFA PGGRLSWGKG SSGGSGAKPS DAASEAARPA TSTLNRFSAL QQAVPTESTD
NRRVVQRSSL SRERGEKAGD RGDRLERSER GGDRGDRLDR ARTPATKRSF SKEVEERSRE
RPSQPEGLRK AASLTEDRDR GRDAVKREAA LPSVSPPKAA LSEEELEKKS KAIIEEYLHL
NDMKEAVQCV QELASPSLLF IFVRHGVEST LERSAIAREH MGQLLHQLLC AGHLSTAQYY
QGLYEILELA EDMEIDIPHV WLYLAELVTP ILQEGGVPMG ELFREITKPL RPLGKAASLL
LEILGLLCKS MGPKKVGTLW REAGLSWKEF LPEGQDIGAF VAEQKVEYTL GEESEAPGQR
ALPSEELNRQ LEKLLKEGSS NQRVFDWIEA NLSEQQIVSN TLVRALMTAV CYSAIIFETP
LRVDVAVLKA RAKLLQKYLC DEQKELQALY ALQALVVTLE QPPNLLRMFF DALYDEDVVK
EDAFYSWESS KDPAEQQGKG VALKSVTAFF KWLREAEEES DHN
//