GRP3_ARATH
ID GRP3_ARATH Reviewed; 145 AA.
AC Q9SL15; B3H766; B6EUC6; C0Z2F8; Q2V494; Q2V495; Q41189;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Glycine-rich protein 3;
DE Short=AtGRP-3;
DE Flags: Precursor;
GN Name=GRP3; OrderedLocusNames=At2g05520; ORFNames=T20G20.13;
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), AND INDUCTION.
RX PubMed=2152168; DOI=10.1105/tpc.2.5.427;
RA de Oliveira D.E., Seurinck J., Inze D., Van Montagu M., Botterman J.;
RT "Differential expression of five Arabidopsis genes encoding glycine-rich
RT proteins.";
RL Plant Cell 2:427-436(1990).
RN [2]
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 [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 6).
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 INTERACTION WITH WAK1, SUBUNIT, DOMAIN, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11335717; DOI=10.1074/jbc.m101283200;
RA Park A.R., Cho S.K., Yun U.J., Jin M.Y., Lee S.H., Sachetto-Martins G.,
RA Park O.K.;
RT "Interaction of the Arabidopsis receptor protein kinase Wak1 with a
RT glycine-rich protein, AtGRP-3.";
RL J. Biol. Chem. 276:26688-26693(2001).
RN [7]
RP FUNCTION.
RX PubMed=12767910; DOI=10.1016/s0006-291x(03)00851-9;
RA Yang E.J., Oh Y.A., Lee E.S., Park A.R., Cho S.K., Yoo Y.J., Park O.K.;
RT "Oxygen-evolving enhancer protein 2 is phosphorylated by glycine-rich
RT protein 3/wall-associated kinase 1 in Arabidopsis.";
RL Biochem. Biophys. Res. Commun. 305:862-868(2003).
CC -!- FUNCTION: Regulates the function of the receptor protein kinase WAK1,
CC and namely the phosphorylation of OEE2. {ECO:0000269|PubMed:12767910}.
CC -!- SUBUNIT: Interacts (via Cys-rich C-terminus) with WAK1 (via the
CC extracellular domain). Component of a 500 kDa complex, composed of GRP3
CC or GRP3-S, WAK1 and KAPP. {ECO:0000269|PubMed:11335717}.
CC -!- INTERACTION:
CC Q9SL15; Q39191: WAK1; NbExp=5; IntAct=EBI-1541435, EBI-2320121;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9SL15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SL15-2; Sequence=VSP_038484;
CC Name=3;
CC IsoId=Q9SL15-3; Sequence=VSP_038483;
CC Name=4;
CC IsoId=Q9SL15-4; Sequence=VSP_038486;
CC Name=5;
CC IsoId=Q9SL15-5; Sequence=VSP_038485;
CC Name=6;
CC IsoId=Q9SL15-6; Sequence=VSP_038482;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in leaves and stems.
CC {ECO:0000269|PubMed:11335717}.
CC -!- INDUCTION: By salicylic acid. Transient induction by drought. Up-
CC regulated by itself. {ECO:0000269|PubMed:11335717,
CC ECO:0000269|PubMed:2152168}.
CC -!- DOMAIN: The Cys-rich C-terminus (111-145) is essential for the
CC interaction with WAK1. {ECO:0000269|PubMed:11335717}.
CC -!- MISCELLANEOUS: GRP3 and GRP3S bind to WAK1, WAK3 and WAK5, but GRP2,
CC GRP4,GRP6, GRP7 and GRP8 did not bind to any of the WAK isoforms.
CC -!- SIMILARITY: Belongs to the GRP family. {ECO:0000305}.
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DR EMBL; S47409; AAB24075.1; -; mRNA.
DR EMBL; AC006220; AAD24655.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05945.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05946.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05947.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05948.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05950.1; -; Genomic_DNA.
DR EMBL; AY065139; AAL38315.1; -; mRNA.
DR EMBL; AY081567; AAM10129.1; -; mRNA.
DR EMBL; BT000704; AAN31848.1; -; mRNA.
DR EMBL; AK318772; BAH56887.1; -; mRNA.
DR PIR; E84469; E84469.
DR PIR; JQ1062; JQ1062.
DR RefSeq; NP_001031335.1; NM_001036258.2. [Q9SL15-2]
DR RefSeq; NP_001031336.1; NM_001036259.1. [Q9SL15-3]
DR RefSeq; NP_001031337.1; NM_001036260.1. [Q9SL15-4]
DR RefSeq; NP_001118277.1; NM_001124805.1. [Q9SL15-5]
DR RefSeq; NP_178620.1; NM_126575.4. [Q9SL15-1]
DR AlphaFoldDB; Q9SL15; -.
DR BioGRID; 501; 6.
DR IntAct; Q9SL15; 6.
DR STRING; 3702.AT2G05520.1; -.
DR PaxDb; Q9SL15; -.
DR PRIDE; Q9SL15; -.
DR ProteomicsDB; 220599; -. [Q9SL15-1]
DR EnsemblPlants; AT2G05520.1; AT2G05520.1; AT2G05520. [Q9SL15-1]
DR EnsemblPlants; AT2G05520.2; AT2G05520.2; AT2G05520. [Q9SL15-2]
DR EnsemblPlants; AT2G05520.3; AT2G05520.3; AT2G05520. [Q9SL15-3]
DR EnsemblPlants; AT2G05520.4; AT2G05520.4; AT2G05520. [Q9SL15-4]
DR EnsemblPlants; AT2G05520.6; AT2G05520.6; AT2G05520. [Q9SL15-5]
DR GeneID; 815101; -.
DR Gramene; AT2G05520.1; AT2G05520.1; AT2G05520. [Q9SL15-1]
DR Gramene; AT2G05520.2; AT2G05520.2; AT2G05520. [Q9SL15-2]
DR Gramene; AT2G05520.3; AT2G05520.3; AT2G05520. [Q9SL15-3]
DR Gramene; AT2G05520.4; AT2G05520.4; AT2G05520. [Q9SL15-4]
DR Gramene; AT2G05520.6; AT2G05520.6; AT2G05520. [Q9SL15-5]
DR KEGG; ath:AT2G05520; -.
DR Araport; AT2G05520; -.
DR TAIR; locus:2058949; AT2G05520.
DR eggNOG; ENOG502S5AC; Eukaryota.
DR HOGENOM; CLU_105596_2_0_1; -.
DR InParanoid; Q9SL15; -.
DR OMA; CYNAGEA; -.
DR PRO; PR:Q9SL15; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SL15; baseline and differential.
DR Genevisible; Q9SL15; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0008361; P:regulation of cell size; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0010044; P:response to aluminum ion; IMP:TAIR.
DR GO; GO:0009269; P:response to desiccation; IEP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR InterPro; IPR010800; GRP.
DR PANTHER; PTHR37389; PTHR37389; 2.
DR Pfam; PF07172; GRP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Extracellular matrix; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..145
FT /note="Glycine-rich protein 3"
FT /id="PRO_0000389634"
FT REPEAT 59..65
FT /note="1"
FT REPEAT 66..72
FT /note="2"
FT REPEAT 73..79
FT /note="3"
FT REPEAT 80..86
FT /note="4"
FT REPEAT 87..93
FT /note="5"
FT REPEAT 94..100
FT /note="6"
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..113
FT /note="6 X 7 AA tandem repeats of G-G-G-G-[NR]-Y-Q"
FT VAR_SEQ 48..80
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_038482"
FT VAR_SEQ 54..73
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038483"
FT VAR_SEQ 57..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038484"
FT VAR_SEQ 64..91
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_038485"
FT VAR_SEQ 64..84
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038486"
FT CONFLICT 112
FT /note="G -> R (in Ref. 1; AAB24075)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="C -> S (in Ref. 5; BAH56887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 14289 MW; D714BFB6B19528AD CRC64;
MASKALVLLG LFAVLLVVSE VAAASSATVN SESKETVKPD QRGYGDNGGN YNNGGGYQGG
GGNYQGGGGN YQGGGGNYQG GGGRYQGGGG RYQGGGGRYQ GGGGRQGGGG SGGSYCRHGC
CYRGYNGCSR CCSYAGEAVQ TQPGH
