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Glycine-rich protein 3 (AtGRP-3)

 GRP3_ARATH              Reviewed;         145 AA.
Q9SL15; B3H766; B6EUC6; C0Z2F8; Q2V494; Q2V495; Q41189;
15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-APR-2018, entry version 84.
RecName: Full=Glycine-rich protein 3;
Short=AtGRP-3;
Flags: Precursor;
Name=GRP3; OrderedLocusNames=At2g05520; ORFNames=T20G20.13;
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), AND INDUCTION.
PubMed=2152168; DOI=10.1105/tpc.2.5.427;
de Oliveira D.E., Seurinck J., Inze D., Van Montagu M., Botterman J.;
"Differential expression of five Arabidopsis genes encoding glycine-
rich proteins.";
Plant Cell 2:427-436(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[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 6).
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]
INTERACTION WITH WAK1, SUBUNIT, DOMAIN, INDUCTION, AND TISSUE
SPECIFICITY.
PubMed=11335717; DOI=10.1074/jbc.M101283200;
Park A.R., Cho S.K., Yun U.J., Jin M.Y., Lee S.H.,
Sachetto-Martins G., Park O.K.;
"Interaction of the Arabidopsis receptor protein kinase Wak1 with a
glycine-rich protein, AtGRP-3.";
J. Biol. Chem. 276:26688-26693(2001).
[7]
FUNCTION.
PubMed=12767910; DOI=10.1016/S0006-291X(03)00851-9;
Yang E.J., Oh Y.A., Lee E.S., Park A.R., Cho S.K., Yoo Y.J.,
Park O.K.;
"Oxygen-evolving enhancer protein 2 is phosphorylated by glycine-rich
protein 3/wall-associated kinase 1 in Arabidopsis.";
Biochem. Biophys. Res. Commun. 305:862-868(2003).
-!- FUNCTION: Regulates the function of the receptor protein kinase
WAK1, and namely the phosphorylation of OEE2.
{ECO:0000269|PubMed:12767910}.
-!- SUBUNIT: Interacts (via Cys-rich C-terminus) with WAK1 (via the
extracellular domain). Component of a 500 kDa complex, composed of
GRP3 or GRP3-S, WAK1 and KAPP. {ECO:0000269|PubMed:11335717}.
-!- INTERACTION:
Q39191:WAK1; NbExp=5; IntAct=EBI-1541435, EBI-2320121;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q9SL15-1; Sequence=Displayed;
Name=2;
IsoId=Q9SL15-2; Sequence=VSP_038484;
Note=Derived from EST data. No experimental confirmation
available.;
Name=3;
IsoId=Q9SL15-3; Sequence=VSP_038483;
Note=Derived from EST data. No experimental confirmation
available.;
Name=4;
IsoId=Q9SL15-4; Sequence=VSP_038486;
Note=Derived from EST data. No experimental confirmation
available.;
Name=5;
IsoId=Q9SL15-5; Sequence=VSP_038485;
Note=Derived from EST data. No experimental confirmation
available.;
Name=6;
IsoId=Q9SL15-6; Sequence=VSP_038482;
Note=Derived from EST data. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in leaves and stems.
{ECO:0000269|PubMed:11335717}.
-!- INDUCTION: By salicylic acid. Transient induction by drought. Up-
regulated by itself. {ECO:0000269|PubMed:11335717,
ECO:0000269|PubMed:2152168}.
-!- DOMAIN: The Cys-rich C-terminus (111-145) is essential for the
interaction with WAK1. {ECO:0000269|PubMed:11335717}.
-!- MISCELLANEOUS: GRP3 and GRP3S bind to WAK1, WAK3 and WAK5, but
GRP2, GRP4,GRP6, GRP7 and GRP8 did not bind to any of the WAK
isoforms.
-!- SIMILARITY: Belongs to the GRP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S47409; AAB24075.1; -; mRNA.
EMBL; AC006220; AAD24655.1; -; Genomic_DNA.
EMBL; CP002685; AEC05945.1; -; Genomic_DNA.
EMBL; CP002685; AEC05946.1; -; Genomic_DNA.
EMBL; CP002685; AEC05947.1; -; Genomic_DNA.
EMBL; CP002685; AEC05948.1; -; Genomic_DNA.
EMBL; CP002685; AEC05950.1; -; Genomic_DNA.
EMBL; AY065139; AAL38315.1; -; mRNA.
EMBL; AY081567; AAM10129.1; -; mRNA.
EMBL; BT000704; AAN31848.1; -; mRNA.
EMBL; AK318772; BAH56887.1; -; mRNA.
PIR; E84469; E84469.
PIR; JQ1062; JQ1062.
RefSeq; NP_001031335.1; NM_001036258.2. [Q9SL15-2]
RefSeq; NP_001031336.1; NM_001036259.1. [Q9SL15-3]
RefSeq; NP_001031337.1; NM_001036260.1. [Q9SL15-4]
RefSeq; NP_001118277.1; NM_001124805.1. [Q9SL15-5]
RefSeq; NP_178620.1; NM_126575.4. [Q9SL15-1]
UniGene; At.48426; -.
ProteinModelPortal; Q9SL15; -.
BioGrid; 501; 6.
IntAct; Q9SL15; 6.
STRING; 3702.AT2G05520.1; -.
PaxDb; Q9SL15; -.
EnsemblPlants; AT2G05520.1; AT2G05520.1; AT2G05520. [Q9SL15-1]
EnsemblPlants; AT2G05520.2; AT2G05520.2; AT2G05520. [Q9SL15-2]
EnsemblPlants; AT2G05520.3; AT2G05520.3; AT2G05520. [Q9SL15-3]
EnsemblPlants; AT2G05520.4; AT2G05520.4; AT2G05520. [Q9SL15-4]
EnsemblPlants; AT2G05520.6; AT2G05520.6; AT2G05520. [Q9SL15-5]
GeneID; 815101; -.
Gramene; AT2G05520.1; AT2G05520.1; AT2G05520. [Q9SL15-1]
Gramene; AT2G05520.2; AT2G05520.2; AT2G05520. [Q9SL15-2]
Gramene; AT2G05520.3; AT2G05520.3; AT2G05520. [Q9SL15-3]
Gramene; AT2G05520.4; AT2G05520.4; AT2G05520. [Q9SL15-4]
Gramene; AT2G05520.6; AT2G05520.6; AT2G05520. [Q9SL15-5]
KEGG; ath:AT2G05520; -.
Araport; AT2G05520; -.
TAIR; locus:2058949; AT2G05520.
InParanoid; Q9SL15; -.
OMA; EDQKWRG; -.
PRO; PR:Q9SL15; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9SL15; baseline and differential.
Genevisible; Q9SL15; AT.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0008361; P:regulation of cell size; IMP:TAIR.
GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
GO; GO:0010044; P:response to aluminum ion; IMP:TAIR.
GO; GO:0009269; P:response to desiccation; IEP:TAIR.
GO; GO:0009723; P:response to ethylene; IEP:TAIR.
GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
InterPro; IPR010800; GRP.
Pfam; PF07172; GRP; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Extracellular matrix;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 145 Glycine-rich protein 3.
/FTId=PRO_0000389634.
REPEAT 59 65 1.
REPEAT 66 72 2.
REPEAT 73 79 3.
REPEAT 80 86 4.
REPEAT 87 93 5.
REPEAT 94 100 6.
REGION 37 113 6 X 7 AA tandem repeats of G-G-G-G-[NR]-
Y-Q.
COMPBIAS 43 127 Gly-rich.
COMPBIAS 116 132 Cys-rich.
VAR_SEQ 48 80 Missing (in isoform 6).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_038482.
VAR_SEQ 54 73 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_038483.
VAR_SEQ 57 63 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_038484.
VAR_SEQ 64 91 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_038485.
VAR_SEQ 64 84 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_038486.
CONFLICT 112 112 G -> R (in Ref. 1; AAB24075).
{ECO:0000305}.
CONFLICT 128 128 C -> S (in Ref. 5; BAH56887).
{ECO:0000305}.
SEQUENCE 145 AA; 14289 MW; D714BFB6B19528AD CRC64;
MASKALVLLG LFAVLLVVSE VAAASSATVN SESKETVKPD QRGYGDNGGN YNNGGGYQGG
GGNYQGGGGN YQGGGGNYQG GGGRYQGGGG RYQGGGGRYQ GGGGRQGGGG SGGSYCRHGC
CYRGYNGCSR CCSYAGEAVQ TQPGH


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