IF5Y_ARATH
ID IF5Y_ARATH Reviewed; 439 AA.
AC Q9C8F1; Q93ZX3;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable eukaryotic translation initiation factor 5-1;
DE Short=eIF-5 1;
GN OrderedLocusNames=At1g36730; ORFNames=T15P17.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal
CC initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent
CC joining of a 60S ribosomal subunit resulting in the release of eIF-2
CC and the guanine nucleotide. The subsequent joining of a 60S ribosomal
CC subunit results in the formation of a functional 80S initiation complex
CC (80S.mRNA.Met-tRNA[F]) (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; AC025782; AAG51259.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31871.1; -; Genomic_DNA.
DR EMBL; AY056208; AAL07057.1; -; mRNA.
DR EMBL; AY064061; AAL36417.1; -; mRNA.
DR EMBL; AY096371; AAM20012.1; -; mRNA.
DR PIR; C86487; C86487.
DR RefSeq; NP_174877.1; NM_103340.3.
DR AlphaFoldDB; Q9C8F1; -.
DR SMR; Q9C8F1; -.
DR STRING; 3702.AT1G36730.1; -.
DR iPTMnet; Q9C8F1; -.
DR PaxDb; Q9C8F1; -.
DR PRIDE; Q9C8F1; -.
DR ProteomicsDB; 250679; -.
DR EnsemblPlants; AT1G36730.1; AT1G36730.1; AT1G36730.
DR GeneID; 840582; -.
DR Gramene; AT1G36730.1; AT1G36730.1; AT1G36730.
DR KEGG; ath:AT1G36730; -.
DR Araport; AT1G36730; -.
DR TAIR; locus:2196376; AT1G36730.
DR eggNOG; KOG2767; Eukaryota.
DR HOGENOM; CLU_026663_1_1_1; -.
DR InParanoid; Q9C8F1; -.
DR OMA; NDFCEEL; -.
DR OrthoDB; 979826at2759; -.
DR PhylomeDB; Q9C8F1; -.
DR PRO; PR:Q9C8F1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8F1; baseline and differential.
DR Genevisible; Q9C8F1; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; IBA:GO_Central.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
DR PROSITE; PS51363; W2; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..439
FT /note="Probable eukaryotic translation initiation factor 5-
FT 1"
FT /id="PRO_0000212522"
FT DOMAIN 283..439
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 143..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..36
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9S825"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9S825"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9S825"
FT CONFLICT 250
FT /note="V -> A (in Ref. 3; AAL07057)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 48622 MW; BD94249C6CEF3F1C CRC64;
MALQNIGASN RDDAFYRYKM PRMMTKIEGR GNGIKTNVVN MVEIAKALGR PAAYTTKYFG
CELGAQSKFD EKNGTSLVNG AHDTSKLAGL LENFIKKYVQ CYGCGNPETE ILITKTQMLQ
LKCAACGFLS DVDMRDKLTS FILKNPPEQK KSSKDKKSMR RAEKERLREG EAADEEMRKL
KKEAASKKKA ATTGTSKDKV SKKKDHSPPR SLSDENDQAD SEEDDDDVQW QTDTSREAAE
KRMKEQLSAV TAEMVMLSTV EEKKPVAEVK KAPEQVHENG NSKIPENAHE KLVNEIKELL
SSGSSPTQLK TALASNSANP QEKMDALFSA LFGGTGKGFA KEVIKKKKYL LALMMMQEEA
GAPAQMGLLN GIESFCMKAS AEAAKEVALV IKGLYDEDIL DEDVIVEWYN KGVKSSPVLK
NVTPFIEWLQ NAESESEEE
