IF2A_DICDI
ID IF2A_DICDI Reviewed; 341 AA.
AC Q869N9; Q55AH4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 1;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit alpha;
DE Short=eIF-2-alpha;
GN Name=eif2s1; Synonyms=eif2a; ORFNames=DDB_G0271862;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 173-181 AND 233-240, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA. This complex
CC binds to a 40S ribosomal subunit, followed by mRNA binding to form a
CC 43S preinitiation complex. Junction of the 60S ribosomal subunit to
CC form the 80S initiation complex is preceded by hydrolysis of the GTP
CC bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for
CC eIF-2 to recycle and catalyze another round of initiation, the GDP
CC bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by
CC eIF-2B. {ECO:0000250|UniProtKB:P05198}.
CC -!- SUBUNIT: Eukaryotic translation initiation factor 2 (eIF-2) is a
CC heterotrimer composed of an alpha, a beta and a gamma subunit.
CC {ECO:0000250|UniProtKB:P05198}.
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000305}.
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DR EMBL; AAFI02000007; EAL71510.1; -; Genomic_DNA.
DR RefSeq; XP_645435.1; XM_640343.1.
DR AlphaFoldDB; Q869N9; -.
DR SMR; Q869N9; -.
DR STRING; 44689.DDB0229412; -.
DR PaxDb; Q869N9; -.
DR EnsemblProtists; EAL71510; EAL71510; DDB_G0271862.
DR GeneID; 8618175; -.
DR KEGG; ddi:DDB_G0271862; -.
DR dictyBase; DDB_G0271862; eif2s1.
DR eggNOG; KOG2916; Eukaryota.
DR HOGENOM; CLU_033458_0_1_1; -.
DR InParanoid; Q869N9; -.
DR OMA; DVNEHQR; -.
DR PhylomeDB; Q869N9; -.
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:Q869N9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IBA:GO_Central.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IBA:GO_Central.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IBA:GO_Central.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR CDD; cd04452; S1_IF2_alpha; 1.
DR Gene3D; 1.10.150.190; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.70.1130; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR044126; S1_IF2_alpha.
DR InterPro; IPR024055; TIF2_asu_C.
DR InterPro; IPR024054; TIF2_asu_middle_sf.
DR InterPro; IPR011488; TIF_2_asu.
DR PANTHER; PTHR10602; PTHR10602; 1.
DR Pfam; PF07541; EIF_2_alpha; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF110993; SSF110993; 1.
DR SUPFAM; SSF116742; SSF116742; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Initiation factor; Protein biosynthesis;
KW Reference proteome; RNA-binding; Translation regulation.
FT CHAIN 1..341
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 1"
FT /id="PRO_0000328067"
FT DOMAIN 18..89
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 301..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..330
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 39059 MW; 1EA6E75906652D7A CRC64;
MVFENDCRMY EKKYPEENEL VMVRIESIGD MGVYVSLLEY NNIEGMILLS EISRRRIRSI
NKLVRVGKTE AVVVVRVDKD KGYIDLSKRR VTPEEYAQCE ERFHKSKAVH GIVRYVATKL
STEDNVVKTK HLYTKFVWPL YTKYGHAYEA FKLSITEPSV FNGFDIAENE RKVLMETIIQ
KLKPQPHKVR ADLEITCYDY EGIDAIKHAI TASQNHALSV LKAPEDGKFD EKAFGVVTIK
LVAPPLYVMV GTFDEKEKGL SMVGQCVDVL SEEITKKNGN LTIKAAPRIV GAVDDQELRD
LMEQLEVENQ DGDGEEHEDD DDDDDDEEEE EKPKEKKSSR K
