GBLPA_ARATH
ID GBLPA_ARATH Reviewed; 327 AA.
AC O24456; C0Z2G7; Q9LDI1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Receptor for activated C kinase 1A {ECO:0000303|PubMed:16829549};
DE AltName: Full=Guanine nucleotide-binding protein subunit beta-like protein A;
DE AltName: Full=WD-40 repeat auxin-dependent protein ARCA;
GN Name=RACK1A {ECO:0000303|PubMed:16829549};
GN Synonyms=ARCA {ECO:0000303|Ref.1};
GN OrderedLocusNames=At1g18080 {ECO:0000312|Araport:AT1G18080};
GN ORFNames=T10F20.9 {ECO:0000312|EMBL:AAF97825.1},
GN T10O22.6 {ECO:0000312|EMBL:AAF78369.1};
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Vahlkamp L., Palme K.;
RT "AtArcA, the Arabidopsis thaliana homolog of the tobacco ArcA gene.";
RL (er) Plant Gene Register PGR97-145(1997).
RN [2]
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 [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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16829549; DOI=10.1093/jxb/erl035;
RA Chen J.G., Ullah H., Temple B., Liang J., Guo J., Alonso J.M., Ecker J.R.,
RA Jones A.M.;
RT "RACK1 mediates multiple hormone responsiveness and developmental processes
RT in Arabidopsis.";
RL J. Exp. Bot. 57:2697-2708(2006).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18947417; DOI=10.1186/1471-2229-8-108;
RA Guo J., Chen J.G.;
RT "RACK1 genes regulate plant development with unequal genetic redundancy in
RT Arabidopsis.";
RL BMC Plant Biol. 8:108-108(2008).
RN [9]
RP INTERACTION WITH NUDT7, AND SUBCELLULAR LOCATION.
RX PubMed=22068106;
RA Olejnik K., Bucholc M., Anielska-Mazur A., Lipko A., Kujawa M.,
RA Modzelan M., Augustyn A., Kraszewska E.;
RT "Arabidopsis thaliana Nudix hydrolase AtNUDT7 forms complexes with the
RT regulatory RACK1A protein and Ggamma subunits of the signal transducing
RT heterotrimeric G protein.";
RL Acta Biochim. Pol. 58:609-616(2011).
RN [10]
RP INTERACTION WITH OFUT20.
RX PubMed=23435172; DOI=10.4161/psb.24012;
RA Kundu N., Dozier U., Deslandes L., Somssich I.E., Ullah H.;
RT "Arabidopsis scaffold protein RACK1A interacts with diverse environmental
RT stress and photosynthesis related proteins.";
RL Plant Signal. Behav. 8:E24012-E24012(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 4-327, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18715992; DOI=10.1110/ps.035121.108;
RA Ullah H., Scappini E.L., Moon A.F., Williams L.V., Armstrong D.L.,
RA Pedersen L.C.;
RT "Structure of a signal transduction regulator, RACK1, from Arabidopsis
RT thaliana.";
RL Protein Sci. 17:1771-1780(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH GB1; MEKK1; MKK4; MKK5; MPK3 AND MPK6.
RX PubMed=25731164; DOI=10.1038/nature14243;
RA Cheng Z., Li J.F., Niu Y., Zhang X.C., Woody O.Z., Xiong Y., Djonovic S.,
RA Millet Y., Bush J., McConkey B.J., Sheen J., Ausubel F.M.;
RT "Pathogen-secreted proteases activate a novel plant immune pathway.";
RL Nature 521:213-216(2015).
CC -!- FUNCTION: Major component of the RACK1 regulatory proteins that play a
CC role in multiple signal transduction pathways. Involved in multiple
CC hormone responses and developmental processes (PubMed:16829549,
CC PubMed:18715992, PubMed:18947417). MAPK cascade scaffolding protein
CC involved in the protease IV and ArgC signaling pathway but not the
CC flg22 pathway (PubMed:25731164). {ECO:0000269|PubMed:16829549,
CC ECO:0000269|PubMed:18715992, ECO:0000269|PubMed:18947417,
CC ECO:0000269|PubMed:25731164}.
CC -!- SUBUNIT: Homodimer and heterodimer with RACK1B or RACK1C (Probable).
CC Interacts with NUDT7 (PubMed:22068106). Interacts with GB1, MEKK1,
CC MKK4, MKK5, MPK3 and MPK6, but not with GPA1 or MPK4 (PubMed:25731164).
CC Interacts with OFUT20 (PubMed:23435172). {ECO:0000269|PubMed:22068106,
CC ECO:0000269|PubMed:23435172, ECO:0000269|PubMed:25731164, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22068106}. Nucleus
CC {ECO:0000269|PubMed:22068106}. Note=Detected in the cytoplasm and
CC nucleus when interacting with NUDT7.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O24456-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O24456-2; Sequence=VSP_040397;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16829549,
CC ECO:0000269|PubMed:18947417}.
CC -!- DISRUPTION PHENOTYPE: Shorter hypocotyls in etiolated seedlings,
CC epinastic cotyledons, reduced rosette leaf production by half and late
CC flowering under short-day conditions. Reduced sensitivity to
CC gibberellin and brassinosteroid in seed germination, hypersensitivity
CC to abscisic acid in seed germination and early seedling development,
CC and hyposensitivity to auxin in adventitious and lateral root
CC formation. Plants show a significant resistance to water stress
CC conditions by limiting water loss through the guard cells.
CC {ECO:0000269|PubMed:16829549, ECO:0000269|PubMed:18715992,
CC ECO:0000269|PubMed:18947417}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal
CC protein RACK1 subfamily. {ECO:0000305}.
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; U77381; AAB82647.1; -; mRNA.
DR EMBL; AC034107; AAF97825.1; -; Genomic_DNA.
DR EMBL; AC069551; AAF78369.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29673.1; -; Genomic_DNA.
DR EMBL; AY035007; AAK59512.1; -; mRNA.
DR EMBL; AY063016; AAL34190.1; -; mRNA.
DR EMBL; AK318781; BAH56896.1; -; mRNA.
DR EMBL; AY088480; AAM66016.1; -; mRNA.
DR RefSeq; NP_173248.1; NM_101670.3. [O24456-1]
DR PDB; 3DM0; X-ray; 2.40 A; A=1-327.
DR PDBsum; 3DM0; -.
DR AlphaFoldDB; O24456; -.
DR SMR; O24456; -.
DR BioGRID; 23627; 295.
DR IntAct; O24456; 1.
DR STRING; 3702.AT1G18080.1; -.
DR iPTMnet; O24456; -.
DR PaxDb; O24456; -.
DR PRIDE; O24456; -.
DR ProteomicsDB; 248613; -. [O24456-1]
DR EnsemblPlants; AT1G18080.1; AT1G18080.1; AT1G18080. [O24456-1]
DR GeneID; 838388; -.
DR Gramene; AT1G18080.1; AT1G18080.1; AT1G18080. [O24456-1]
DR KEGG; ath:AT1G18080; -.
DR Araport; AT1G18080; -.
DR TAIR; locus:2194060; AT1G18080.
DR eggNOG; KOG0279; Eukaryota.
DR HOGENOM; CLU_000288_57_7_1; -.
DR InParanoid; O24456; -.
DR OMA; CKAMLWD; -.
DR PhylomeDB; O24456; -.
DR EvolutionaryTrace; O24456; -.
DR PRO; PR:O24456; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O24456; baseline and differential.
DR Genevisible; O24456; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IMP:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IEP:TAIR.
DR GO; GO:0010476; P:gibberellin mediated signaling pathway; IMP:TAIR.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009967; P:positive regulation of signal transduction; IMP:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IGI:TAIR.
DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
DR GO; GO:0009749; P:response to glucose; IMP:TAIR.
DR GO; GO:0042254; P:ribosome biogenesis; IGI:TAIR.
DR GO; GO:0009845; P:seed germination; IGI:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045223; Asc1/RACK1.
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 PANTHER; PTHR19868; PTHR19868; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Nucleus; Reference proteome;
KW Repeat; Ribonucleoprotein; Ribosomal protein; Transducer; WD repeat.
FT CHAIN 1..327
FT /note="Receptor for activated C kinase 1A"
FT /id="PRO_0000127748"
FT REPEAT 13..44
FT /note="WD 1"
FT REPEAT 61..91
FT /note="WD 2"
FT REPEAT 103..133
FT /note="WD 3"
FT REPEAT 148..180
FT /note="WD 4"
FT REPEAT 192..222
FT /note="WD 5"
FT REPEAT 233..262
FT /note="WD 6"
FT REPEAT 293..323
FT /note="WD 7"
FT VAR_SEQ 195..245
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_040397"
FT CONFLICT 178
FT /note="V -> M (in Ref. 1; AAB82647)"
FT /evidence="ECO:0000305"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3DM0"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3DM0"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3DM0"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:3DM0"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:3DM0"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:3DM0"
SQ SEQUENCE 327 AA; 35748 MW; 9DA103C4300FE96B CRC64;
MAEGLVLKGT MRAHTDMVTA IATPIDNADI IVSASRDKSI ILWKLTKDDK AYGVAQRRLT
GHSHFVEDVV LSSDGQFALS GSWDGELRLW DLAAGVSTRR FVGHTKDVLS VAFSLDNRQI
VSASRDRTIK LWNTLGECKY TISEGGEGHR DWVSCVRFSP NTLQPTIVSA SWDKTVKVWN
LSNCKLRSTL AGHTGYVSTV AVSPDGSLCA SGGKDGVVLL WDLAEGKKLY SLEANSVIHA
LCFSPNRYWL CAATEHGIKI WDLESKSIVE DLKVDLKAEA EKADNSGPAA TKRKVIYCTS
LNWSADGSTL FSGYTDGVIR VWGIGRY
