PYL5_ORYSJ
ID PYL5_ORYSJ Reviewed; 209 AA.
AC Q6I5C3; K4NDW6;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Abscisic acid receptor PYL5 {ECO:0000305};
DE AltName: Full=PYR1-like protein 11 {ECO:0000303|PubMed:24743650};
DE Short=OsPYL11 {ECO:0000303|PubMed:24743650};
DE AltName: Full=PYR1-like protein 5 {ECO:0000303|PubMed:22071266};
DE Short=OsPYL5 {ECO:0000303|PubMed:22071266};
DE AltName: Full=Regulatory components of ABA receptor 5 {ECO:0000305};
GN Name=PYL5 {ECO:0000303|PubMed:22071266};
GN Synonyms=PYL11 {ECO:0000303|PubMed:24743650},
GN RCAR5 {ECO:0000303|PubMed:22071266};
GN OrderedLocusNames=Os05g0213500 {ECO:0000312|EMBL:BAS92815.1},
GN LOC_Os05g12260 {ECO:0000305};
GN ORFNames=OSJNBb0067H15.8 {ECO:0000312|EMBL:AAT47101.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PP2C30, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Dongjin;
RX PubMed=22071266; DOI=10.1093/jxb/err338;
RA Kim H., Hwang H., Hong J.W., Lee Y.N., Ahn I.P., Yoon I.S., Yoo S.D.,
RA Lee S., Lee S.C., Kim B.G.;
RT "A rice orthologue of the ABA receptor, OsPYL/RCAR5, is a positive
RT regulator of the ABA signal transduction pathway in seed germination and
RT early seedling growth.";
RL J. Exp. Bot. 63:1013-1024(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=24474809; DOI=10.1093/jxb/ert397;
RA Kim H., Lee K., Hwang H., Bhatnagar N., Kim D.Y., Yoon I.S., Byun M.O.,
RA Kim S.T., Jung K.H., Kim B.G.;
RT "Overexpression of PYL5 in rice enhances drought tolerance, inhibits
RT growth, and modulates gene expression.";
RL J. Exp. Bot. 65:453-464(2014).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=24743650; DOI=10.1371/journal.pone.0095246;
RA He Y., Hao Q., Li W., Yan C., Yan N., Yin P.;
RT "Identification and characterization of ABA receptors in Oryza sativa.";
RL PLoS ONE 9:E95246-E95246(2014).
RN [9]
RP INTERACTION WITH PP2C30 AND PP2C53, AND SUBCELLULAR LOCATION.
RX PubMed=26362328; DOI=10.1186/s12284-015-0061-6;
RA Tian X., Wang Z., Li X., Lv T., Liu H., Wang L., Niu H., Bu Q.;
RT "Characterization and functional analysis of pyrabactin resistance-like
RT abscisic acid receptor family in rice.";
RL Rice 8:28-28(2015).
RN [10]
RP INTERACTION WITH PP2C50.
RX PubMed=28827170; DOI=10.1016/j.molp.2017.08.003;
RA Han S., Min M.K., Lee S.Y., Lim C.W., Bhatnagar N., Lee Y., Shin D.,
RA Chung K.Y., Lee S.C., Kim B.G., Lee S.;
RT "Modulation of ABA signaling by altering VxGL motif of PP2Cs in Oryza
RT sativa.";
RL Mol. Plant 10:1190-1205(2017).
RN [11]
RP INTERACTION WITH PP2C51, AND SUBCELLULAR LOCATION.
RX PubMed=28000033; DOI=10.1007/s11103-016-0568-2;
RA Bhatnagar N., Min M.K., Choi E.H., Kim N., Moon S.J., Yoon I., Kwon T.,
RA Jung K.H., Kim B.G.;
RT "The protein phosphatase 2C clade A protein OsPP2C51 positively regulates
RT seed germination by directly inactivating OsbZIP10.";
RL Plant Mol. Biol. 93:389-401(2017).
CC -!- FUNCTION: Intracellular abscisic acid (ABA) receptor that functions as
CC a positive regulator of ABA signaling pathway (PubMed:22071266,
CC PubMed:24474809). Together with ABI5, PP2C30 and SAPK2, is part of an
CC ABA signaling unit that modulates seed germination and early seedling
CC growth (PubMed:22071266). Acts as positive regulator of abiotic stress-
CC responsive gene expression (PubMed:24474809). Inhibits the protein
CC phosphatases PP2C06 and PP2C09 when activated by ABA (PubMed:24743650).
CC {ECO:0000269|PubMed:22071266, ECO:0000269|PubMed:24474809,
CC ECO:0000269|PubMed:24743650}.
CC -!- SUBUNIT: Monomer (PubMed:24743650). Interacts with PP2C30. Binding to
CC PP2C30 is dependent on the presence of abscisic acid (ABA)
CC (PubMed:22071266, PubMed:26362328). Interacts with PP2C51. Binding to
CC PP2C51 is dependent on the presence of ABA (PubMed:28000033). Interacts
CC with PP2C50. Binding to PP2C50 is dependent on the presence of ABA
CC (PubMed:28827170). Interacts with PP2C53 (PubMed:26362328).
CC {ECO:0000269|PubMed:22071266, ECO:0000269|PubMed:24743650,
CC ECO:0000269|PubMed:26362328, ECO:0000269|PubMed:28000033,
CC ECO:0000269|PubMed:28827170}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22071266,
CC ECO:0000269|PubMed:26362328, ECO:0000269|PubMed:28000033}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:26362328}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf sheaths and leaf blades.
CC Expressed at low levels in roots, flowers and seeds.
CC {ECO:0000269|PubMed:24474809}.
CC -!- INDUCTION: Repressed by abscisic acid (ABA) and drought stress.
CC {ECO:0000269|PubMed:24474809}.
CC -!- MISCELLANEOUS: Plants overexpressing PYL5 exhibit abscisic acid (ABA)
CC hypersensitive phenotypes (PubMed:22071266). Plants overexpressing PYL5
CC exhibit tolerance to salt and drought stresses, but are hypersensitive
CC to osmotic stress and ABA during vegetative growth (PubMed:24474809).
CC {ECO:0000269|PubMed:22071266, ECO:0000269|PubMed:24474809}.
CC -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
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DR EMBL; JX970836; AFV36781.1; -; mRNA.
DR EMBL; AC136226; AAT47101.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF16837.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92815.1; -; Genomic_DNA.
DR EMBL; AK065280; BAG89445.1; -; mRNA.
DR RefSeq; XP_015640707.1; XM_015785221.1.
DR PDB; 6UOP; EM; 1.35 A; A=24-29.
DR PDB; 6UOQ; EM; 1.01 A; A=24-29.
DR PDB; 6UOR; EM; 0.90 A; A=24-29.
DR PDB; 6UOS; EM; 0.90 A; A=24-29.
DR PDB; 6UOU; EM; 1.00 A; A=24-29.
DR PDB; 6UOW; EM; 1.20 A; A=24-29.
DR PDBsum; 6UOP; -.
DR PDBsum; 6UOQ; -.
DR PDBsum; 6UOR; -.
DR PDBsum; 6UOS; -.
DR PDBsum; 6UOU; -.
DR PDBsum; 6UOW; -.
DR AlphaFoldDB; Q6I5C3; -.
DR SMR; Q6I5C3; -.
DR STRING; 4530.OS05T0213500-01; -.
DR PaxDb; Q6I5C3; -.
DR PRIDE; Q6I5C3; -.
DR EnsemblPlants; Os05t0213500-01; Os05t0213500-01; Os05g0213500.
DR GeneID; 4338104; -.
DR Gramene; Os05t0213500-01; Os05t0213500-01; Os05g0213500.
DR KEGG; osa:4338104; -.
DR eggNOG; ENOG502QPYH; Eukaryota.
DR HOGENOM; CLU_077517_2_0_1; -.
DR InParanoid; Q6I5C3; -.
DR OMA; VNDSEMY; -.
DR OrthoDB; 1261133at2759; -.
DR PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0010427; F:abscisic acid binding; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR GO; GO:0009845; P:seed germination; IMP:UniProtKB.
DR GO; GO:0090351; P:seedling development; IMP:UniProtKB.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR019587; Polyketide_cyclase/dehydratase.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF10604; Polyketide_cyc2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Cytoplasm; Disulfide bond;
KW Nucleus; Protein phosphatase inhibitor; Receptor; Reference proteome;
KW Stress response.
FT CHAIN 1..209
FT /note="Abscisic acid receptor PYL5"
FT /id="PRO_0000444340"
FT REGION 44..196
FT /note="START-like"
FT /evidence="ECO:0000250|UniProtKB:Q8H1R0"
FT MOTIF 105..109
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 135..137
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 80
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:Q8H1R0"
FT BINDING 109..114
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 136..142
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 161
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 81
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT SITE 108
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 172
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 180
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT DISULFID 51..177
FT /note="Reversible"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
SQ SEQUENCE 209 AA; 22215 MW; B6C75FBD3D80800A CRC64;
MVGLVGGGGW RVGDDAAGGG GGGAVAAGAA AAAEAEHMRR LHSHAPGEHQ CSSALVKHIK
APVHLVWSLV RSFDQPQRYK PFVSRCVVRG GDLEIGSVRE VNVKTGLPAT TSTERLELLD
DDEHILSVKF VGGDHRLRNY SSIVTVHPES IDGRPGTLVI ESFVVDVPDG NTKDETCYFV
EAVIKCNLTS LAEVSERLAV QSPTSPLEQ
