IF2G_DICDI
ID IF2G_DICDI Reviewed; 460 AA.
AC Q54XD8; O76854;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 3;
DE EC=3.6.5.3;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit gamma;
DE Short=eIF-2-gamma;
GN Name=eif2s3; Synonyms=eif2G; ORFNames=DDB_G0278967;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 135-459.
RA Knetsch M.L.W., Batra R., Manstein D.J.;
RT "Identification of translation initiation factor 2 gamma from Dictyostelium
RT discoideum.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF-2),
CC involved in the early steps of protein synthesis. In the presence of
CC GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and
CC then recruits the 40S ribosomal complex and initiation factors eIF-1,
CC eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a
CC step that determines the rate of protein translation. The 43S PIC binds
CC to mRNA and scans downstream to the initiation codon, where it forms a
CC 48S initiation complex by codon-anticodon base pairing. This leads to
CC the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-
CC 5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release
CC of Pi, which makes GTP hydrolysis irreversible, causes the release of
CC the eIF-2-GDP binary complex from the 40S subunit, an event that is
CC essential for the subsequent joining of the 60S ribosomal subunit to
CC form an elongation-competent 80S ribosome. In order for eIF-2 to
CC recycle and catalyze another round of initiation, the GDP bound to eIF-
CC 2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP
CC exchange factor (GEF) eIF-2B. {ECO:0000250|UniProtKB:P32481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P32481};
CC -!- SUBUNIT: Eukaryotic translation initiation factor 2 (eIF-2) is a
CC heterotrimeric G-protein composed of an alpha, a beta and a gamma
CC subunit. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-
CC tRNAi form a multifactor complex (MFC) that may bind to the 40S
CC ribosome. {ECO:0000250|UniProtKB:P32481}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; AAFI02000026; EAL67905.1; -; Genomic_DNA.
DR EMBL; AJ010980; CAA09448.1; -; mRNA.
DR RefSeq; XP_641922.1; XM_636830.1.
DR AlphaFoldDB; Q54XD8; -.
DR SMR; Q54XD8; -.
DR STRING; 44689.DDB0215353; -.
DR PaxDb; Q54XD8; -.
DR EnsemblProtists; EAL67905; EAL67905; DDB_G0278967.
DR GeneID; 8621837; -.
DR KEGG; ddi:DDB_G0278967; -.
DR dictyBase; DDB_G0278967; eif2s3.
DR eggNOG; KOG0466; Eukaryota.
DR HOGENOM; CLU_027154_0_1_1; -.
DR InParanoid; Q54XD8; -.
DR OMA; NIGMVGH; -.
DR PhylomeDB; Q54XD8; -.
DR Reactome; R-DDI-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DDI-381042; PERK regulates gene expression.
DR Reactome; R-DDI-382556; ABC-family proteins mediated transport.
DR Reactome; R-DDI-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DDI-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-DDI-72731; Recycling of eIF2:GDP.
DR PRO; PR:Q54XD8; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044127; eIF2g_dom_2.
DR InterPro; IPR044128; eIF2g_GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Hydrolase; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..460
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 3"
FT /id="PRO_0000328073"
FT DOMAIN 33..241
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 42..49
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 128..131
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 184..187
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 219..221
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 45..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 184..187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 219..221
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT CONFLICT 135..136
FT /note="LM -> AR (in Ref. 2; CAA09448)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="L -> M (in Ref. 2; CAA09448)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="V -> D (in Ref. 2; CAA09448)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="V -> A (in Ref. 2; CAA09448)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="C -> S (in Ref. 2; CAA09448)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="K -> N (in Ref. 2; CAA09448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 50130 MW; 53E4B681AEA5A70C CRC64;
MATKNKPNLS VQDVKLLNVN ELTPLTPNVI SRQATINIGT IGHVAHGKST VVKAISGVLT
VRFTSEFKRN ITIKLGYANA KIYKCDNPQC ERPGCYKSAR SNTEDNPQCE RPGCGGRMTL
LRHVSFVDCP GHDVLMATML NGAAVMDAAL LLIAGNESCP QPQTSEHIAA IEIMNLKNII
ILQNKIDLVK EAAAQEQYGQ ILKFIQGTIA ENAPIIPISA QMKYNIDVIC EYIVKKIPIP
VRDFTSDPRM IVIRSFDVNK PGSRVDEIKG GVAGGSILKG VLKIGDEIEV RPGVISKELD
GKIKCSPIFC RIISLFAEEN ELQYAVPGGL IGVGTKIDPT LCRADRLVGQ VLGSVGKLPE
IFVALEVNFF LLRRLLGVKS DGDKQSKVKK LSKEDTLMVN IGSTSTGCRV VAVKHDLAKL
QLLTPVCSQE GEKIALSRRV DKNWRLIGWG EIKKGTVLTN
