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Receptor for activated C kinase 1A (Guanine nucleotide-binding protein subunit beta-like protein A) (WD-40 repeat auxin-dependent protein ARCA)

 GBLPA_ARATH             Reviewed;         327 AA.
O24456; C0Z2G7; Q9LDI1;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 2.
07-NOV-2018, entry version 137.
RecName: Full=Receptor for activated C kinase 1A {ECO:0000303|PubMed:16829549};
AltName: Full=Guanine nucleotide-binding protein subunit beta-like protein A;
AltName: Full=WD-40 repeat auxin-dependent protein ARCA;
Name=RACK1A {ECO:0000303|PubMed:16829549};
Synonyms=ARCA {ECO:0000303|Ref.1};
OrderedLocusNames=At1g18080 {ECO:0000312|Araport:AT1G18080};
ORFNames=T10F20.9 {ECO:0000312|EMBL:AAF97825.1},
T10O22.6 {ECO:0000312|EMBL:AAF78369.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
Vahlkamp L., Palme K.;
"AtArcA, the Arabidopsis thaliana homolog of the tobacco ArcA gene.";
(er) Plant Gene Register PGR97-145(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=16829549; DOI=10.1093/jxb/erl035;
Chen J.G., Ullah H., Temple B., Liang J., Guo J., Alonso J.M.,
Ecker J.R., Jones A.M.;
"RACK1 mediates multiple hormone responsiveness and developmental
processes in Arabidopsis.";
J. Exp. Bot. 57:2697-2708(2006).
[8]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=18947417; DOI=10.1186/1471-2229-8-108;
Guo J., Chen J.G.;
"RACK1 genes regulate plant development with unequal genetic
redundancy in Arabidopsis.";
BMC Plant Biol. 8:108-108(2008).
[9]
INTERACTION WITH NUDT7, AND SUBCELLULAR LOCATION.
PubMed=22068106;
Olejnik K., Bucholc M., Anielska-Mazur A., Lipko A., Kujawa M.,
Modzelan M., Augustyn A., Kraszewska E.;
"Arabidopsis thaliana Nudix hydrolase AtNUDT7 forms complexes with the
regulatory RACK1A protein and Ggamma subunits of the signal
transducing heterotrimeric G protein.";
Acta Biochim. Pol. 58:609-616(2011).
[10]
INTERACTION WITH OFUT20.
PubMed=23435172; DOI=10.4161/psb.24012;
Kundu N., Dozier U., Deslandes L., Somssich I.E., Ullah H.;
"Arabidopsis scaffold protein RACK1A interacts with diverse
environmental stress and photosynthesis related proteins.";
Plant Signal. Behav. 8:E24012-E24012(2013).
[11]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 4-327, FUNCTION, AND
DISRUPTION PHENOTYPE.
PubMed=18715992; DOI=10.1110/ps.035121.108;
Ullah H., Scappini E.L., Moon A.F., Williams L.V., Armstrong D.L.,
Pedersen L.C.;
"Structure of a signal transduction regulator, RACK1, from Arabidopsis
thaliana.";
Protein Sci. 17:1771-1780(2008).
[12]
FUNCTION, AND INTERACTION WITH GB1; MEKK1; MKK4; MKK5; MPK3 AND MPK6.
PubMed=25731164; DOI=10.1038/nature14243;
Cheng Z., Li J.F., Niu Y., Zhang X.C., Woody O.Z., Xiong Y.,
Djonovic S., Millet Y., Bush J., McConkey B.J., Sheen J.,
Ausubel F.M.;
"Pathogen-secreted proteases activate a novel plant immune pathway.";
Nature 521:213-216(2015).
-!- FUNCTION: Major component of the RACK1 regulatory proteins that
play a role in multiple signal transduction pathways. Involved in
multiple hormone responses and developmental processes
(PubMed:16829549, PubMed:18715992, PubMed:18947417). MAPK cascade
scaffolding protein involved in the protease IV and ArgC signaling
pathway but not the flg22 pathway (PubMed:25731164).
{ECO:0000269|PubMed:16829549, ECO:0000269|PubMed:18715992,
ECO:0000269|PubMed:18947417, ECO:0000269|PubMed:25731164}.
-!- SUBUNIT: Homodimer and heterodimer with RACK1B or RACK1C
(Probable). Interacts with NUDT7 (PubMed:22068106). Interacts with
GB1, MEKK1, MKK4, MKK5, MPK3 and MPK6, but not with GPA1 or MPK4
(PubMed:25731164). Interacts with OFUT20 (PubMed:23435172).
{ECO:0000269|PubMed:22068106, ECO:0000269|PubMed:23435172,
ECO:0000269|PubMed:25731164, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22068106}.
Nucleus {ECO:0000269|PubMed:22068106}. Note=Detected in the
cytoplasm and nucleus when interacting with NUDT7.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O24456-1; Sequence=Displayed;
Name=2;
IsoId=O24456-2; Sequence=VSP_040397;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:16829549, ECO:0000269|PubMed:18947417}.
-!- DISRUPTION PHENOTYPE: Shorter hypocotyls in etiolated seedlings,
epinastic cotyledons, reduced rosette leaf production by half and
late flowering under short-day conditions. Reduced sensitivity to
gibberellin and brassinosteroid in seed germination,
hypersensitivity to abscisic acid in seed germination and early
seedling development, and hyposensitivity to auxin in adventitious
and lateral root formation. Plants show a significant resistance
to water stress conditions by limiting water loss through the
guard cells. {ECO:0000269|PubMed:16829549,
ECO:0000269|PubMed:18715992, ECO:0000269|PubMed:18947417}.
-!- SIMILARITY: Belongs to the WD repeat G protein beta family.
Ribosomal protein RACK1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U77381; AAB82647.1; -; mRNA.
EMBL; AC034107; AAF97825.1; -; Genomic_DNA.
EMBL; AC069551; AAF78369.1; -; Genomic_DNA.
EMBL; CP002684; AEE29673.1; -; Genomic_DNA.
EMBL; AY035007; AAK59512.1; -; mRNA.
EMBL; AY063016; AAL34190.1; -; mRNA.
EMBL; AK318781; BAH56896.1; -; mRNA.
EMBL; AY088480; AAM66016.1; -; mRNA.
RefSeq; NP_173248.1; NM_101670.3. [O24456-1]
UniGene; At.22612; -.
UniGene; At.67882; -.
PDB; 3DM0; X-ray; 2.40 A; A=1-327.
PDBsum; 3DM0; -.
ProteinModelPortal; O24456; -.
SMR; O24456; -.
BioGrid; 23627; 94.
IntAct; O24456; 1.
STRING; 3702.AT1G18080.1; -.
iPTMnet; O24456; -.
PaxDb; O24456; -.
PRIDE; O24456; -.
EnsemblPlants; AT1G18080.1; AT1G18080.1; AT1G18080. [O24456-1]
GeneID; 838388; -.
Gramene; AT1G18080.1; AT1G18080.1; AT1G18080. [O24456-1]
KEGG; ath:AT1G18080; -.
Araport; AT1G18080; -.
TAIR; locus:2194060; AT1G18080.
eggNOG; KOG0279; Eukaryota.
eggNOG; ENOG410XQGZ; LUCA.
HOGENOM; HOG000091643; -.
InParanoid; O24456; -.
KO; K14753; -.
OMA; KAQVPYC; -.
OrthoDB; EOG09360EGR; -.
PhylomeDB; O24456; -.
EvolutionaryTrace; O24456; -.
PRO; PR:O24456; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; O24456; baseline and differential.
Genevisible; O24456; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
GO; GO:0019899; F:enzyme binding; IBA:GO_Central.
GO; GO:0005078; F:MAP-kinase scaffold activity; IMP:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
GO; GO:0032947; F:protein-containing complex scaffold activity; IDA:TAIR.
GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
GO; GO:0071215; P:cellular response to abscisic acid stimulus; IEP:TAIR.
GO; GO:0010476; P:gibberellin mediated signaling pathway; IMP:TAIR.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
GO; GO:0009967; P:positive regulation of signal transduction; IMP:UniProtKB.
GO; GO:0006417; P:regulation of translation; IGI:TAIR.
GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
GO; GO:0009749; P:response to glucose; IMP:TAIR.
GO; GO:0042254; P:ribosome biogenesis; IGI:TAIR.
GO; GO:0009845; P:seed germination; IGI:TAIR.
GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF00400; WD40; 7.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 4.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
Ribosomal protein; Transducer; WD repeat.
CHAIN 1 327 Receptor for activated C kinase 1A.
/FTId=PRO_0000127748.
REPEAT 13 44 WD 1.
REPEAT 61 91 WD 2.
REPEAT 103 133 WD 3.
REPEAT 148 180 WD 4.
REPEAT 192 222 WD 5.
REPEAT 233 262 WD 6.
REPEAT 293 323 WD 7.
VAR_SEQ 195 245 Missing (in isoform 2).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_040397.
CONFLICT 178 178 V -> M (in Ref. 1; AAB82647).
{ECO:0000305}.
STRAND 4 12 {ECO:0000244|PDB:3DM0}.
STRAND 18 22 {ECO:0000244|PDB:3DM0}.
STRAND 29 35 {ECO:0000244|PDB:3DM0}.
STRAND 38 44 {ECO:0000244|PDB:3DM0}.
STRAND 54 60 {ECO:0000244|PDB:3DM0}.
STRAND 66 71 {ECO:0000244|PDB:3DM0}.
STRAND 75 82 {ECO:0000244|PDB:3DM0}.
STRAND 85 91 {ECO:0000244|PDB:3DM0}.
TURN 92 95 {ECO:0000244|PDB:3DM0}.
STRAND 96 102 {ECO:0000244|PDB:3DM0}.
STRAND 108 113 {ECO:0000244|PDB:3DM0}.
STRAND 120 124 {ECO:0000244|PDB:3DM0}.
STRAND 129 132 {ECO:0000244|PDB:3DM0}.
STRAND 138 142 {ECO:0000244|PDB:3DM0}.
STRAND 153 158 {ECO:0000244|PDB:3DM0}.
STRAND 162 164 {ECO:0000244|PDB:3DM0}.
STRAND 166 171 {ECO:0000244|PDB:3DM0}.
STRAND 176 180 {ECO:0000244|PDB:3DM0}.
TURN 181 183 {ECO:0000244|PDB:3DM0}.
STRAND 186 190 {ECO:0000244|PDB:3DM0}.
STRAND 197 202 {ECO:0000244|PDB:3DM0}.
STRAND 206 213 {ECO:0000244|PDB:3DM0}.
STRAND 219 222 {ECO:0000244|PDB:3DM0}.
TURN 223 226 {ECO:0000244|PDB:3DM0}.
STRAND 227 230 {ECO:0000244|PDB:3DM0}.
STRAND 238 243 {ECO:0000244|PDB:3DM0}.
STRAND 245 254 {ECO:0000244|PDB:3DM0}.
STRAND 257 262 {ECO:0000244|PDB:3DM0}.
TURN 263 266 {ECO:0000244|PDB:3DM0}.
STRAND 267 272 {ECO:0000244|PDB:3DM0}.
STRAND 298 303 {ECO:0000244|PDB:3DM0}.
STRAND 307 314 {ECO:0000244|PDB:3DM0}.
STRAND 317 323 {ECO:0000244|PDB:3DM0}.
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


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