EIF3K_ARATH
ID EIF3K_ARATH Reviewed; 226 AA.
AC Q9SZA3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit K {ECO:0000255|HAMAP-Rule:MF_03010};
DE Short=eIF3k {ECO:0000255|HAMAP-Rule:MF_03010};
DE AltName: Full=eIF-3 p25 {ECO:0000255|HAMAP-Rule:MF_03010};
GN Name=TIF3K1; OrderedLocusNames=At4g33250; ORFNames=F17M5.10;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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).
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_03010}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03010}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03010}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit K family. {ECO:0000255|HAMAP-
CC Rule:MF_03010}.
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DR EMBL; AF291713; AAG53637.1; -; mRNA.
DR EMBL; AL035678; CAB38783.1; -; Genomic_DNA.
DR EMBL; AL161583; CAB80042.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86197.1; -; Genomic_DNA.
DR EMBL; AY050928; AAK93605.1; -; mRNA.
DR EMBL; AY037191; AAK59776.1; -; mRNA.
DR EMBL; AY091670; AAM10269.1; -; mRNA.
DR EMBL; AY091164; AAM14103.1; -; mRNA.
DR PIR; T05976; T05976.
DR RefSeq; NP_195051.1; NM_119479.4.
DR AlphaFoldDB; Q9SZA3; -.
DR SMR; Q9SZA3; -.
DR BioGRID; 14746; 21.
DR STRING; 3702.AT4G33250.1; -.
DR PaxDb; Q9SZA3; -.
DR PRIDE; Q9SZA3; -.
DR ProteomicsDB; 220407; -.
DR DNASU; 829461; -.
DR EnsemblPlants; AT4G33250.1; AT4G33250.1; AT4G33250.
DR GeneID; 829461; -.
DR Gramene; AT4G33250.1; AT4G33250.1; AT4G33250.
DR KEGG; ath:AT4G33250; -.
DR Araport; AT4G33250; -.
DR TAIR; locus:2119131; AT4G33250.
DR eggNOG; KOG3252; Eukaryota.
DR HOGENOM; CLU_076723_2_0_1; -.
DR InParanoid; Q9SZA3; -.
DR OMA; WKHQGQG; -.
DR OrthoDB; 1576799at2759; -.
DR PhylomeDB; Q9SZA3; -.
DR PRO; PR:Q9SZA3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZA3; baseline and differential.
DR Genevisible; Q9SZA3; AT.
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; ISS:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.40.250; -; 1.
DR HAMAP; MF_03010; eIF3k; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR InterPro; IPR009374; eIF3k.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR016020; Transl_init_fac_sub12_N_euk.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13022; PTHR13022; 1.
DR Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50250; PCI; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..226
FT /note="Eukaryotic translation initiation factor 3 subunit
FT K"
FT /id="PRO_0000123551"
FT DOMAIN 44..202
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 226 AA; 25728 MW; BDDE9A85101AC50F CRC64;
MGVEIQSPQE QSSYTVEQLV ALNPFNPEIL PDLENYVNVT SQTYSLEVNL CLLRLYQFEP
ERMNTHIVAR ILVKALMAMP TPDFSLCLFL IPERVQMEEQ FKSLIVLSHY LETGRFQQFW
DEAAKNRHIL EAVPGFEQAI QAYASHLLSL SYQKVPRSVL AEAVNMDGAS LDKFIEQQVT
NSGWIVEKEG GSIVLPQNEF NHPELKKNTG ENVPLEHIAR IFPILG
