IF2C_ARATH
ID IF2C_ARATH Reviewed; 1026 AA.
AC Q9SHI1; B9DI35; Q9ASQ3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Translation initiation factor IF-2, chloroplastic;
DE Flags: Precursor;
GN OrderedLocusNames=At1g17220; ORFNames=F20D23.8;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 231-1026.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD50011.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007651; AAD50011.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE29560.1; -; Genomic_DNA.
DR EMBL; AF367343; AAK32930.1; -; mRNA.
DR EMBL; BT001007; AAN46761.1; -; mRNA.
DR EMBL; AK317746; BAH20402.1; -; mRNA.
DR PIR; D86308; D86308.
DR RefSeq; NP_173165.1; NM_101583.4.
DR AlphaFoldDB; Q9SHI1; -.
DR SMR; Q9SHI1; -.
DR STRING; 3702.AT1G17220.1; -.
DR iPTMnet; Q9SHI1; -.
DR PaxDb; Q9SHI1; -.
DR PRIDE; Q9SHI1; -.
DR ProteomicsDB; 228846; -.
DR EnsemblPlants; AT1G17220.1; AT1G17220.1; AT1G17220.
DR GeneID; 838293; -.
DR Gramene; AT1G17220.1; AT1G17220.1; AT1G17220.
DR KEGG; ath:AT1G17220; -.
DR Araport; AT1G17220; -.
DR TAIR; locus:2020427; AT1G17220.
DR eggNOG; KOG1145; Eukaryota.
DR HOGENOM; CLU_006301_7_1_1; -.
DR InParanoid; Q9SHI1; -.
DR OMA; CGIGVED; -.
DR OrthoDB; 1124591at2759; -.
DR PRO; PR:Q9SHI1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SHI1; baseline and differential.
DR Genevisible; Q9SHI1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; GTP-binding; Initiation factor; Nucleotide-binding; Plastid;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..1026
FT /note="Translation initiation factor IF-2, chloroplastic"
FT /id="PRO_0000014477"
FT DOMAIN 499..672
FT /note="tr-type G"
FT REGION 158..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..515
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 533..537
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 558..561
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 612..615
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 648..650
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 177..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..276
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 508..515
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 558..562
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 612..615
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 779
FT /note="R -> G (in Ref. 3; AAN46761/AAK32930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1026 AA; 109747 MW; 9D2E8620C2E7BB1D CRC64;
MPSMLVLVGT MPSLASLVSL GGACASVSGT SSSDASYALV KRVSLSRRSV KGTKKWLCRY
SVSSSTTTTT ADFIADQNNN SVSIDSNSFR GSKDGDDSEV VLKQTPKPVL KPPVARVERG
LGVNTAPWSK DLSNGGKFDG EEERNKVIES LGEVLDKAEK LEIPKPGNKE GGEAVKPSQP
SANSSNSRNG SYANASDGGT RKTKTMKSVW RKGDAVAAVQ KVVKESPKIF NRGVQTEPRT
REEGEVNAKA GTPLAPPQPP FRPQPPVRPQ PMLQGKPMVA PPVKKSPILK DLGMAAKPLV
SEEVDSSVKS KERKPILVDK FASKKKGVDP AASQAVLAPT KPGKGPPSNK FRVEHRNKKN
ASASPRRRIV AEDDGDDDAS ISRSGRKGRK WSKASRKAVR LQAAKDAAPV KAEILEVEEE
GMSIEDLAYN LAIGEGDILG YLYSKGIRPD GVHTLDREMV KMICRDYDVE VLDADSVKVE
EMAKKRQTFD EEDLDKLEDR PPVITIMGHV DHGKTTLLDY IRKSKVAASE AGGITQGIGA
YKVSVPVDGK LQSCVFLDTP GHEAFGAMRA RGARVTDIAI IVVAADDGIR PQTNEAIAHA
KAAAVPIVIA INKIDKEGAS PDRVMQELSS IGLMPEDWGG DVPMVQISAL KGENVDDLLE
TVMLVAELQE LKANPHRNAK GIVIEAGLDK AKGPFATFIV QKGTLKRGDV VVCGEAFGKV
RALFDHSGER VDEAGPSIPV QVIGLNNVPI AGDEFEIVSS LDVAREMAEA RAVSLRDERI
SAKAGDGKVT LSSLASAVSA KKMSGLDLHQ LNIILKVDVQ GSIEAVRQAL QVLPQENVTL
KFLLQATGDV SNSDVDLASA SEAIVFGFNV KASGSVKKAA ENKGVEIRLY RVIYELIDDV
RNAMEGLLES VEEQIPIGSA EVRATFSSGS GRVAGCMVNE GKFVKDCGIR VVRKGKTVHV
GVLDSLKRVK ENVKEVSAGL ECGIGMDDYD DWIEGDIIEA FNAVQKRRTL EEASASMSAA
IEEAGV
