EIF3C_ARATH
ID EIF3C_ARATH Reviewed; 900 AA.
AC O49160; Q9LYM6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002};
DE Short=eIF3c {ECO:0000255|HAMAP-Rule:MF_03002};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 8 {ECO:0000255|HAMAP-Rule:MF_03002};
DE AltName: Full=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03002};
DE AltName: Full=p105;
GN Name=TIF3C1; OrderedLocusNames=At3g56150; ORFNames=F18O21_110;
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], INTERACTION WITH CSN1 AND TIF3E1, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=9849901; DOI=10.1016/s0014-5793(98)01367-2;
RA Karniol B., Yahalom A., Kwok S., Tsuge T., Matsui M., Deng X.-W.,
RA Chamovitz D.A.;
RT "The Arabidopsis homologue of an eIF3 complex subunit associates with the
RT COP9 complex.";
RL FEBS Lett. 439:173-179(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
RP INTERACTION WITH TIF3H1.
RX PubMed=15548739; DOI=10.1105/tpc.104.026880;
RA Kim T.-H., Kim B.-H., Yahalom A., Chamovitz D.A., von Arnim A.G.;
RT "Translational regulation via 5' mRNA leader sequences revealed by
RT mutational analysis of the Arabidopsis translation initiation factor
RT subunit eIF3h.";
RL Plant Cell 16:3341-3356(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-40 AND SER-204, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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_03002}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex (Potential) (PubMed:9849901, PubMed:15548739). Binds to
CC the translation initiation factors TIF3C1 and TIF3H1 (PubMed:15548739,
CC PubMed:9849901). Interacts with CSN1 (Potential) (PubMed:9849901).
CC Associates with the CSN (COP9 signalosome) complex (PubMed:9849901).
CC Binds to the translation initiation factors TIF3C1 and TIF3H1
CC (PubMed:15548739, PubMed:9849901). {ECO:0000255|HAMAP-Rule:MF_03002,
CC ECO:0000269|PubMed:15548739, ECO:0000269|PubMed:9849901}.
CC -!- INTERACTION:
CC O49160; P42818: ATPK1; NbExp=2; IntAct=EBI-1635551, EBI-8107038;
CC O49160; F4K210: MAF19.20; NbExp=4; IntAct=EBI-1635551, EBI-7216904;
CC O49160; Q9C5Z3: TIF3E1; NbExp=3; IntAct=EBI-1635551, EBI-1635572;
CC O49160; Q9FR53: TOR; NbExp=3; IntAct=EBI-1635551, EBI-1382370;
CC O49160; Q9M4T6; NbExp=2; IntAct=EBI-1635551, EBI-1635581;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000255|HAMAP-
CC Rule:MF_03002}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF040102; AAC83464.1; -; mRNA.
DR EMBL; AL163763; CAB87414.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79486.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79487.1; -; Genomic_DNA.
DR EMBL; AY064006; AAL36362.1; -; mRNA.
DR EMBL; BT001961; AAN71960.1; -; mRNA.
DR PIR; T47732; T47732.
DR PIR; T50773; T50773.
DR RefSeq; NP_001190102.1; NM_001203173.1.
DR RefSeq; NP_191174.1; NM_115473.3.
DR AlphaFoldDB; O49160; -.
DR SMR; O49160; -.
DR BioGRID; 10097; 75.
DR IntAct; O49160; 13.
DR MINT; O49160; -.
DR STRING; 3702.AT3G56150.2; -.
DR iPTMnet; O49160; -.
DR PaxDb; O49160; -.
DR PRIDE; O49160; -.
DR ProteomicsDB; 222346; -.
DR EnsemblPlants; AT3G56150.1; AT3G56150.1; AT3G56150.
DR EnsemblPlants; AT3G56150.2; AT3G56150.2; AT3G56150.
DR GeneID; 824781; -.
DR Gramene; AT3G56150.1; AT3G56150.1; AT3G56150.
DR Gramene; AT3G56150.2; AT3G56150.2; AT3G56150.
DR KEGG; ath:AT3G56150; -.
DR Araport; AT3G56150; -.
DR TAIR; locus:2078456; AT3G56150.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_1_1; -.
DR InParanoid; O49160; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR PhylomeDB; O49160; -.
DR PRO; PR:O49160; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O49160; baseline and differential.
DR Genevisible; O49160; AT.
DR GO; GO:0005829; C:cytosol; HDA: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:0005852; C:eukaryotic translation initiation factor 3 complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13937; PTHR13937; 1.
DR Pfam; PF05470; eIF-3c_N; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..900
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000123527"
FT DOMAIN 604..776
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..196
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 65
FT /note="Y -> N (in Ref. 1; AAC83464)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="G -> E (in Ref. 1; AAC83464)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="K -> N (in Ref. 1; AAC83464)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="S -> F (in Ref. 1; AAC83464)"
FT /evidence="ECO:0000305"
FT CONFLICT 710..711
FT /note="IK -> VQ (in Ref. 1; AAC83464)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="L -> V (in Ref. 1; AAC83464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 900 AA; 102949 MW; 84EA72DDE49A05C5 CRC64;
MTSRFFTQVG SESEDESDYE VEVNEVQNDD VNNRYLQSGS EDDDDTDTKR VVKPAKDKRF
EEMTYTVDQM KNAMKINDWV SLQENFDKVN KQLEKVMRIT EAVKPPTLYI KTLVMLEDFL
NEALANKEAK KKMSTSNSKA LNSMKQKLKK NNKLYEDDIN KYREAPEVEE EKQPEDDDDD
DDDDDEVEDD DDSSIDGPTV DPGSDVDEPT DNLTWEKMLS KKDKLLEKLM NKDPKEITWD
WVNKKFKEIV AARGKKGTAR FELVDQLTHL TKIAKTPAQK LEILFSVISA QFDVNPGLSG
HMPINVWKKC VLNMLTILDI LVKYSNIVVD DTVEPDENET SKPTDYDGKI RVWGNLVAFL
ERVDTEFFKS LQCIDPHTRE YVERLRDEPM FLALAQNIQD YFERMGDFKA AAKVALRRVE
AIYYKPQEVY DAMRKLAELV EEEEETEEAK EESGPPTSFI VVPEVVPRKP TFPESSRAMM
DILVSLIYRN GDERTKARAM LCDINHHALM DNFVTARDLL LMSHLQDNIQ HMDISTQILF
NRTMAQLGLC AFRAGMITES HSCLSELYSG QRVRELLAQG VSQSRYHEKT PEQERMERRR
QMPYHMHLNL ELLEAVHLIC AMLLEVPNMA ANSHDAKRRV ISKNFRRLLE ISERQAFTAP
PENVRDHVMA ATRALTKGDF QKAFEVLNSL EVWRLLKNRD SILDMVKDRI KEEALRTYLF
TYSSSYESLS LDQLAKMFDV SEPQVHSIVS KMMINEELHA SWDQPTRCIV FHEVQHSRLQ
SLAFQLTEKL SILAESNERA MESRTGGGGL DLSSRRRDNN QDYAGAASGG GGYWQDKANY
GQGRQGNRSG YGGGRSSGQN GQWSGQNRGG GYAGRVGSGN RGMQMDGSSR MVSLNRGVRT
