ID IF2B_ARATH Reviewed; 268 AA.
AC Q41969; F4K6W6; Q8L7Q3; Q9C5N7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 3.
DT 18-JAN-2017, entry version 134.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit beta {ECO:0000305};
DE Short=eIF2-beta {ECO:0000305};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1401 {ECO:0000305};
GN Name=EIF2B {ECO:0000305}; Synonyms=EMB1401 {ECO:0000305};
GN OrderedLocusNames=At5g20920; ORFNames=F22D1.90;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Browning K.S., Chen R.;
RT "Arabidopsis thaliana protein synthesis initiation factor eIF2 beta
RT mRNA.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G.,
RA Caboche M., Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome
RT annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-252.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8281187; DOI=10.1046/j.1365-313X.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P.,
RA Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R.,
RA Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y.,
RA de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M.,
RA Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [8]
RP PHOSPHORYLATION AT SER-42; SER-80 AND SER-112.
RX PubMed=19509420; DOI=10.1074/jbc.M109.007658;
RA Dennis M.D., Person M.D., Browning K.S.;
RT "Phosphorylation of plant translation initiation factors by CK2
RT enhances the in vitro interaction of multifactor complex components.";
RL J. Biol. Chem. 284:20615-20628(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA Meinnel T., Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis
CC by forming a ternary complex with GTP and initiator tRNA. This
CC complex binds to a 40S ribosomal subunit, followed by mRNA binding
CC to form a 43S pre-initiation complex. Junction of the 60S
CC ribosomal subunit to form the 80S initiation complex is preceded
CC by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-
CC GDP binary complex. In order for eIF-2 to recycle and catalyze
CC another round of initiation, the GDP bound to eIF-2 must exchange
CC with GTP by way of a reaction catalyzed by eIF-2B (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma
CC chain.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q41969-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q41969-2; Sequence=VSP_058490;
CC Note=May be due to a competing acceptor splice site. No
CC experimental confirmation available. {ECO:0000305};
CC -!- PTM: Phosphorylated at Ser-42, Ser-80 and Ser-112 by CK2.
CC {ECO:0000269|PubMed:19509420}.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
DR EMBL; AF353095; AAK29672.1; -; mRNA.
DR EMBL; AF296834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92904.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92905.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92906.1; -; Genomic_DNA.
DR EMBL; AY128324; AAM91527.1; -; mRNA.
DR EMBL; BT000056; AAN15375.1; -; mRNA.
DR EMBL; BX829594; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY087810; AAM65346.1; -; mRNA.
DR EMBL; Z18133; CAA79110.1; -; mRNA.
DR RefSeq; NP_001078610.1; NM_001085141.1. [Q41969-1]
DR RefSeq; NP_197592.1; NM_122100.4. [Q41969-1]
DR RefSeq; NP_974817.1; NM_203088.2. [Q41969-2]
DR UniGene; At.21465; -.
DR ProteinModelPortal; Q41969; -.
DR SMR; Q41969; -.
DR BioGrid; 17491; 32.
DR IntAct; Q41969; 32.
DR STRING; 3702.AT5G20920.1; -.
DR iPTMnet; Q41969; -.
DR PaxDb; Q41969; -.
DR PRIDE; Q41969; -.
DR EnsemblPlants; AT5G20920.1; AT5G20920.1; AT5G20920. [Q41969-1]
DR EnsemblPlants; AT5G20920.3; AT5G20920.3; AT5G20920. [Q41969-1]
DR GeneID; 832216; -.
DR Gramene; AT5G20920.1; AT5G20920.1; AT5G20920.
DR Gramene; AT5G20920.3; AT5G20920.3; AT5G20920.
DR KEGG; ath:AT5G20920; -.
DR TAIR; AT5G20920; -.
DR eggNOG; KOG2768; Eukaryota.
DR eggNOG; COG1601; LUCA.
DR HOGENOM; HOG000107197; -.
DR InParanoid; Q41969; -.
DR KO; K03238; -.
DR OMA; QNELVAD; -.
DR OrthoDB; EOG09360J8U; -.
DR PhylomeDB; Q41969; -.
DR Reactome; R-ATH-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-ATH-382556; ABC-family proteins mediated transport.
DR Reactome; R-ATH-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-ATH-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-ATH-72731; Recycling of eIF2:GDP.
DR PRO; PR:Q41969; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q41969; baseline and differential.
DR Genevisible; Q41969; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.50; -; 1.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Initiation factor; Metal-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
FT CHAIN 2 268 Eukaryotic translation initiation factor
FT 2 subunit beta.
FT /FTId=PRO_0000137411.
FT ZN_FING 222 246 C4-type. {ECO:0000255}.
FT COMPBIAS 22 28 Poly-Lys.
FT COMPBIAS 64 69 Poly-Lys.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000244|PubMed:22223895}.
FT MOD_RES 42 42 Phosphoserine; by CK2.
FT {ECO:0000269|PubMed:19509420}.
FT MOD_RES 80 80 Phosphoserine; by CK2.
FT {ECO:0000269|PubMed:19509420}.
FT MOD_RES 112 112 Phosphoserine; by CK2.
FT {ECO:0000269|PubMed:19509420}.
FT VAR_SEQ 14 14 Missing (in isoform 2).
FT /FTId=VSP_058490.
FT CONFLICT 71 71 T -> A (in Ref. 1; AAK29672 and 6;
FT AAM65346). {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 140 249 ipfam:eIF-5_eIF-2B [T]
FT MYHIT 140 249 ismart:eIF2B_5 [T]
SQ SEQUENCE 268 AA; 30663 MW; E1C17373472F4DEB CRC64;
MADEINEIRE EQEQLAPFDP SKKKKKKKVV IQEPVEDLAE SSQTEKSDSL PVNDGLESSF
TGMKKKKKKP TESSLLNNES VDAGEDLDEI ANDEQEGEEG IVLQQRYPWE GSERDYIYDE
LLGRVFNILR ENNPELAGDR RRTVMRPPQV LREGTKKTVF VNFMDLCKTM HRQPDHVMQY
LLAELGTSGS LDGQQRLVVK GRFAPKNFEG ILRRYITDYV ICLGCKSPDT ILSKENRLFF
LRCEKCGSQR SVAPIKTGFV ARVSRRKT
//
|
