IF2A_SCHPO
ID IF2A_SCHPO Reviewed; 306 AA.
AC P56286;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit alpha;
DE Short=eIF-2-alpha;
GN Name=tif211; ORFNames=SPAC3G9.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179; SER-273; SER-295;
RP SER-303 AND SER-305, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC -!- INTERACTION:
CC P56286; Q9USP0: tif221; NbExp=2; IntAct=EBI-16198594, EBI-1793476;
CC P56286; Q9UT76: tif222; NbExp=2; IntAct=EBI-16198594, EBI-16198490;
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000305}.
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DR EMBL; CU329670; CAA15918.1; -; Genomic_DNA.
DR PIR; T11645; T11645.
DR RefSeq; NP_594081.1; NM_001019504.2.
DR AlphaFoldDB; P56286; -.
DR SMR; P56286; -.
DR BioGRID; 279875; 8.
DR DIP; DIP-61963N; -.
DR IntAct; P56286; 3.
DR STRING; 4896.SPAC3G9.09c.1; -.
DR iPTMnet; P56286; -.
DR MaxQB; P56286; -.
DR PaxDb; P56286; -.
DR PRIDE; P56286; -.
DR EnsemblFungi; SPAC3G9.09c.1; SPAC3G9.09c.1:pep; SPAC3G9.09c.
DR GeneID; 2543455; -.
DR KEGG; spo:SPAC3G9.09c; -.
DR PomBase; SPAC3G9.09c; tif211.
DR VEuPathDB; FungiDB:SPAC3G9.09c; -.
DR eggNOG; KOG2916; Eukaryota.
DR HOGENOM; CLU_033458_0_1_1; -.
DR InParanoid; P56286; -.
DR OMA; DVNEHQR; -.
DR PhylomeDB; P56286; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-72649; Translation initiation complex formation.
DR Reactome; R-SPO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-SPO-72731; Recycling of eIF2:GDP.
DR PRO; PR:P56286; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IBA:GO_Central.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISO:PomBase.
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; ISO:PomBase.
DR GO; GO:0002183; P:cytoplasmic translational initiation; ISO:PomBase.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:PomBase.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:PomBase.
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 Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..306
FT /note="Eukaryotic translation initiation factor 2 subunit
FT alpha"
FT /id="PRO_0000137388"
FT DOMAIN 17..88
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 306 AA; 34526 MW; 6C967FF2C3BD0D1E CRC64;
MSTTSCRMYE NRFPEVDELV VVNVRQIQEM GAYVKLLEYD NIEGMVLLSE LSRRRIRSVQ
KHIRVGRNEV VVVLRVDKEK GYIDLSKRRV SPEDVVKCEE RFNKSKAVHS IMRHIAEKHN
VPLETMYTTI GWPLYRKYGH AYDAFKLAIS NPDHVFEGLE PPKSGVINDL LAQISRRLTP
QPIKIRADVE VTCFGYEGIN AIKAALKAAE DVHTEEVPIK VKLVAPPLYV LLTNALDKSL
GLKKLEEAIG AIEKSITASN GTCTVKMKPK AVSETDELEL ADLMKKFEKE NAEISGDEED
DQSGSE
