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EIF3I_ARATH
ID   EIF3I_ARATH             Reviewed;         328 AA.
AC   Q38884; O82342; Q94K09; Q9C5Z0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   25-MAY-2022, entry version 150.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit I {ECO:0000255|HAMAP-Rule:MF_03008};
DE            Short=eIF3i {ECO:0000255|HAMAP-Rule:MF_03008};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 2 {ECO:0000255|HAMAP-Rule:MF_03008};
DE   AltName: Full=TGF-beta receptor-interacting protein 1;
DE            Short=TRIP-1;
DE   AltName: Full=eIF-3-beta {ECO:0000255|HAMAP-Rule:MF_03008};
DE   AltName: Full=eIF3 p36 {ECO:0000255|HAMAP-Rule:MF_03008};
GN   Name=TIF3I1; OrderedLocusNames=At2g46280; ORFNames=T3F17.7;
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 [MRNA].
RX   PubMed=7566156; DOI=10.1038/377548a0;
RA   Chen R.H., Miettinen P.J., Maruka E.M., Choy L., Derynck R.;
RT   "A WD-domain protein that is associated with and phosphorylated by the type
RT   II TGF-beta receptor.";
RL   Nature 377:548-552(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11042177; DOI=10.1074/jbc.m007236200;
RA   Burks E.A., Bezerra P.P., Le H., Gallie D.R., Browning K.S.;
RT   "Plant initiation factor 3 subunit composition resembles mammalian
RT   initiation factor 3 and has a novel subunit.";
RL   J. Biol. Chem. 276:2122-2131(2001).
RN   [3]
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   [4]
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   [5]
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: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis of a
CC       specialized repertoire of mRNAs and, together with other initiation
CC       factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC       ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03008}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03008}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q38884-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit I family. {ECO:0000255|HAMAP-
CC       Rule:MF_03008}.
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DR   EMBL; U36765; AAC49079.1; -; mRNA.
DR   EMBL; AF285835; AAG53616.1; -; mRNA.
DR   EMBL; AC005397; AAC62878.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10670.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10671.1; -; Genomic_DNA.
DR   EMBL; AF370485; AAK43862.1; -; mRNA.
DR   EMBL; AY064633; AAL47346.1; -; mRNA.
DR   PIR; H84900; H84900.
DR   PIR; S60256; S60256.
DR   RefSeq; NP_182151.1; NM_130191.6. [Q38884-1]
DR   RefSeq; NP_850450.1; NM_180119.3. [Q38884-1]
DR   AlphaFoldDB; Q38884; -.
DR   SMR; Q38884; -.
DR   BioGRID; 4571; 27.
DR   IntAct; Q38884; 2.
DR   STRING; 3702.AT2G46280.1; -.
DR   PaxDb; Q38884; -.
DR   PRIDE; Q38884; -.
DR   ProteomicsDB; 221938; -. [Q38884-1]
DR   EnsemblPlants; AT2G46280.1; AT2G46280.1; AT2G46280. [Q38884-1]
DR   EnsemblPlants; AT2G46280.2; AT2G46280.2; AT2G46280. [Q38884-1]
DR   GeneID; 819236; -.
DR   Gramene; AT2G46280.1; AT2G46280.1; AT2G46280. [Q38884-1]
DR   Gramene; AT2G46280.2; AT2G46280.2; AT2G46280. [Q38884-1]
DR   KEGG; ath:AT2G46280; -.
DR   Araport; AT2G46280; -.
DR   TAIR; locus:2063009; AT2G46280.
DR   eggNOG; KOG0643; Eukaryota.
DR   HOGENOM; CLU_043845_0_1_1; -.
DR   InParanoid; Q38884; -.
DR   OMA; VWFSHNG; -.
DR   PhylomeDB; Q38884; -.
DR   PRO; PR:Q38884; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q38884; baseline and differential.
DR   Genevisible; Q38884; AT.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IPI:TAIR.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_03008; eIF3i; 1.
DR   InterPro; IPR027525; eIF3i.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..328
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   I"
FT                   /id="PRO_0000051039"
FT   REPEAT          8..49
FT                   /note="WD 1"
FT   REPEAT          50..89
FT                   /note="WD 2"
FT   REPEAT          146..185
FT                   /note="WD 3"
FT   REPEAT          191..230
FT                   /note="WD 4"
FT   REPEAT          288..327
FT                   /note="WD 5"
FT   CONFLICT        21..23
FT                   /note="EGD -> QPH (in Ref. 2; AAG53616)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107
FT                   /note="L -> F (in Ref. 2; AAG53616)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126..128
FT                   /note="RIA -> AYC (in Ref. 1; AAC49079)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166
FT                   /note="G -> C (in Ref. 1; AAC49079)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255
FT                   /note="Q -> E (in Ref. 1; AAC49079)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        275
FT                   /note="Y -> C (in Ref. 1; AAC49079)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        304
FT                   /note="S -> G (in Ref. 5; AAK43862/AAL47346)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        311
FT                   /note="D -> G (in Ref. 1; AAC49079)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   328 AA;  36388 MW;  4ABFE9866A09CFAF CRC64;
     MRPILMKGHE RPLTFLRYNR EGDLLFSCAK DHTPTLWFAD NGERLGTYRG HNGAVWCCDV
     SRDSSRLITG SADQTAKLWD VKSGKELFTF KFNAPTRSVD FAVGDRLAVI TTDHFVDRTA
     AIHVKRIAED PEEQDAESVL VLHCPDGKKR INRAVWGPLN QTIVSGGEDK VIRIWDAETG
     KLLKQSDEEV GHKKDITSLC KAADDSHFLT GSLDKTAKLW DMRTLTLLKT YTTVVPVNAV
     SLSPLLNHVV LGGGQDASAV TTTDHRAGKF EAKFYDKILQ EEIGGVKGHF GPINALAFNP
     DGKSFSSGGE DGYVRLHHFD SDYFNIKI
 
 
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