IF32_ARATH
ID IF32_ARATH Reviewed; 312 AA.
AC O82234;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Translation initiation factor IF3-2, chloroplastic {ECO:0000305};
DE Short=AtIF3-2 {ECO:0000303|PubMed:25630975};
DE AltName: Full=AtINFC-2 {ECO:0000303|PubMed:25630975};
DE AltName: Full=Protein SUPPRESSOR OF VARIEGATION 9 {ECO:0000303|PubMed:27535792};
DE Flags: Precursor;
GN Name=IF3-2 {ECO:0000303|PubMed:25630975};
GN Synonyms=SVR9 {ECO:0000303|PubMed:27535792};
GN OrderedLocusNames=At2g24060 {ECO:0000312|Araport:AT2G24060};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=25630975; DOI=10.1007/s11120-015-0074-4;
RA Nesbit A.D., Whippo C., Hangarter R.P., Kehoe D.M.;
RT "Translation initiation factor 3 families: what are their roles in
RT regulating cyanobacterial and chloroplast gene expression?";
RL Photosyn. Res. 126:147-159(2015).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27535792; DOI=10.1104/pp.15.02040;
RA Zheng M., Liu X., Liang S., Fu S., Qi Y., Zhao J., Shao J., An L., Yu F.;
RT "Chloroplast translation initiation factors regulate leaf variegation and
RT development.";
RL Plant Physiol. 172:1117-1130(2016).
CC -!- FUNCTION: Chloroplast translation initiation factor that is essential
CC for the coordination of leaf and chloroplast development
CC (PubMed:27535792). IF-3 binds to the 30S ribosomal subunit and shifts
CC the equilibrum between 70S ribosomes and their 50S and 30S subunits in
CC favor of the free subunits, thus enhancing the availability of 30S
CC subunits on which protein synthesis initiation begins (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_00080, ECO:0000269|PubMed:27535792}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00080}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:25630975, ECO:0000269|PubMed:27535792}.
CC -!- TISSUE SPECIFICITY: Highly expressed in young, newly emerged leaves.
CC {ECO:0000269|PubMed:27535792}.
CC -!- DISRUPTION PHENOTYPE: Chloroplast development defect, and leaf
CC developmental abnormalities, such as virescent and serrated leaf
CC phenotype, disorganized mesophyll cells, and altered cotyledon venation
CC patterns. {ECO:0000269|PubMed:27535792}.
CC -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000255|HAMAP-
CC Rule:MF_00080}.
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DR EMBL; AC005170; AAC63674.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07524.1; -; Genomic_DNA.
DR EMBL; AY072160; AAL59982.1; -; mRNA.
DR EMBL; AY096414; AAM20054.1; -; mRNA.
DR EMBL; AY088131; AAM65676.1; -; mRNA.
DR PIR; B84632; B84632.
DR RefSeq; NP_179984.1; NM_127968.3.
DR AlphaFoldDB; O82234; -.
DR SMR; O82234; -.
DR STRING; 3702.AT2G24060.1; -.
DR World-2DPAGE; 0003:O82234; -.
DR PaxDb; O82234; -.
DR PRIDE; O82234; -.
DR ProteomicsDB; 228872; -.
DR EnsemblPlants; AT2G24060.1; AT2G24060.1; AT2G24060.
DR GeneID; 816940; -.
DR Gramene; AT2G24060.1; AT2G24060.1; AT2G24060.
DR KEGG; ath:AT2G24060; -.
DR Araport; AT2G24060; -.
DR TAIR; locus:2061380; AT2G24060.
DR eggNOG; ENOG502QUHV; Eukaryota.
DR HOGENOM; CLU_054919_3_1_1; -.
DR InParanoid; O82234; -.
DR OMA; IKKPQEP; -.
DR OrthoDB; 1344007at2759; -.
DR PhylomeDB; O82234; -.
DR PRO; PR:O82234; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82234; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IMP:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR Gene3D; 3.10.20.80; -; 1.
DR Gene3D; 3.30.110.10; -; 1.
DR HAMAP; MF_00080; IF_3; 1.
DR InterPro; IPR036788; T_IF-3_C_sf.
DR InterPro; IPR036787; T_IF-3_N_sf.
DR InterPro; IPR019813; Translation_initiation_fac3_CS.
DR InterPro; IPR001288; Translation_initiation_fac_3.
DR InterPro; IPR019815; Translation_initiation_fac_3_C.
DR InterPro; IPR019814; Translation_initiation_fac_3_N.
DR PANTHER; PTHR10938; PTHR10938; 1.
DR Pfam; PF00707; IF3_C; 1.
DR Pfam; PF05198; IF3_N; 1.
DR SUPFAM; SSF54364; SSF54364; 1.
DR SUPFAM; SSF55200; SSF55200; 1.
DR TIGRFAMs; TIGR00168; infC; 1.
DR PROSITE; PS00938; IF3; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Initiation factor; Plastid; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..312
FT /note="Translation initiation factor IF3-2, chloroplastic"
FT /id="PRO_0000439376"
FT REGION 253..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 35142 MW; B6BF8BA67EB56202 CRC64;
MAGITSSTVG FNAVFTGITK TVSSHSLFSV DSKLCSLRLS KTELSFTNLT PSPRRAFAVT
CRFGGGGGGY RFSGDNRRGR PKEAEIDEAL DISSIRSATV RLIDGQQNML GLVSKDEAVR
MADDAELDLV ILSPDADPPV VKMMDYSKYR YEQQKRKKDQ QKKTTRMDLK ELKMGYNIDQ
HDYSVRLRAA QKFLQDGDKV KVIVSMKGRE NEFRNIAIEL LRRFQTEIGE LATEESKNFR
DRNMFIILVP NKEMIRKPQE PPTRKKKKTA ENEASASAAE ITAEPEPEPE PEPEPEPEPE
PEPEPEPLQI DS
