PYL3_ORYSJ
ID PYL3_ORYSJ Reviewed; 204 AA.
AC Q6EN42; K4N2F7;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Abscisic acid receptor PYL3 {ECO:0000305};
DE AltName: Full=PYR1-like protein 10 {ECO:0000303|PubMed:24743650};
DE Short=OsPYL10 {ECO:0000303|PubMed:24743650};
DE AltName: Full=PYR1-like protein 3 {ECO:0000303|PubMed:22071266};
DE Short=OsPYL3 {ECO:0000303|PubMed:22071266};
DE AltName: Full=Regulatory components of ABA receptor 3 {ECO:0000305};
GN Name=PYL3 {ECO:0000303|PubMed:22071266};
GN Synonyms=PYL10 {ECO:0000303|PubMed:24743650},
GN RCAR3 {ECO:0000303|PubMed:22071266};
GN OrderedLocusNames=Os02g0255500 {ECO:0000312|EMBL:BAF08378.1},
GN LOC_Os02g15640 {ECO:0000305};
GN ORFNames=OSJNBa0052K15.19 {ECO:0000312|EMBL:BAD29693.1},
GN P0613F08.1 {ECO:0000312|EMBL:BAD27946.1};
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].
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=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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP INTERACTION WITH PP2C30 AND PP2C53, SUBCELLULAR LOCATION, AND INDUCTION.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 30-204 IN COMPLEX WITH ABSCISIC
RP ACID, FUNCTION, INTERACTION WITH PP2C50, AND DISULFIDE BONDS.
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).
CC -!- FUNCTION: Involved in abscisic acid (ABA) signaling during seed
CC germination and abiotic stress response. Acts as positive regulator of
CC ABA-mediated inhibition of seed germination, and tolerance to drought
CC and cold stresses (PubMed:26362328). Together with PP2C50 and SAPK10,
CC may form an ABA signaling module involved in stress response
CC (PubMed:28827170). Inhibits the protein phosphatases PP2C06 and PP2C09
CC when activated by abscisic acid (ABA) (PubMed:24743650).
CC {ECO:0000269|PubMed:24743650, ECO:0000269|PubMed:26362328,
CC ECO:0000269|PubMed:28827170}.
CC -!- SUBUNIT: Monomer (PubMed:24743650). Interacts with PP2C50. Binding to
CC PP2C50 is dependent on the presence of abscisic acid (ABA)
CC (PubMed:28827170). Interacts with PP2C30 and PP2C53 (PubMed:26362328).
CC {ECO:0000269|PubMed:24743650, ECO:0000269|PubMed:26362328,
CC ECO:0000269|PubMed:28827170}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26362328}.
CC Nucleus {ECO:0000269|PubMed:26362328}.
CC -!- INDUCTION: Repressed by abscisic acid (ABA).
CC {ECO:0000269|PubMed:26362328}.
CC -!- MISCELLANEOUS: Plants overexpressing PYL3 exhibit abscisic acid (ABA)
CC hypersensitive phenotype during seed germination. Plants overexpressing
CC PYL3 exhibit tolerance to cold and drought stresses.
CC {ECO:0000269|PubMed:26362328}.
CC -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
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DR EMBL; JX970837; AFV36782.1; -; mRNA.
DR EMBL; AP004801; BAD27946.1; -; Genomic_DNA.
DR EMBL; AP006844; BAD29693.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08378.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS77948.1; -; Genomic_DNA.
DR EMBL; AK059303; BAG86955.1; -; mRNA.
DR EMBL; AK104581; BAG96806.1; -; mRNA.
DR RefSeq; XP_015627042.1; XM_015771556.1.
DR PDB; 5GWO; X-ray; 2.82 A; C/D=30-204.
DR PDB; 5GWP; X-ray; 2.58 A; C/D=30-204.
DR PDB; 5ZCG; X-ray; 2.10 A; C/D=30-204.
DR PDB; 5ZCH; X-ray; 2.47 A; C/D=30-204.
DR PDB; 5ZCL; X-ray; 2.66 A; C/D=30-204.
DR PDB; 5ZCU; X-ray; 2.41 A; C/D=30-204.
DR PDBsum; 5GWO; -.
DR PDBsum; 5GWP; -.
DR PDBsum; 5ZCG; -.
DR PDBsum; 5ZCH; -.
DR PDBsum; 5ZCL; -.
DR PDBsum; 5ZCU; -.
DR AlphaFoldDB; Q6EN42; -.
DR SMR; Q6EN42; -.
DR STRING; 4530.OS02T0255500-01; -.
DR PaxDb; Q6EN42; -.
DR PRIDE; Q6EN42; -.
DR EnsemblPlants; Os02t0255500-01; Os02t0255500-01; Os02g0255500.
DR GeneID; 4328916; -.
DR Gramene; Os02t0255500-01; Os02t0255500-01; Os02g0255500.
DR KEGG; osa:4328916; -.
DR eggNOG; ENOG502QPYH; Eukaryota.
DR HOGENOM; CLU_077517_2_0_1; -.
DR InParanoid; Q6EN42; -.
DR OMA; TEPIDQV; -.
DR OrthoDB; 1261133at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
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; IDA:UniProtKB.
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:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR GO; GO:0009845; P:seed germination; 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..204
FT /note="Abscisic acid receptor PYL3"
FT /id="PRO_0000444339"
FT REGION 40..191
FT /note="START-like"
FT /evidence="ECO:0000250|UniProtKB:Q8H1R0"
FT MOTIF 100..104
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 130..132
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 76
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:28827170,
FT ECO:0007744|PDB:5GWP"
FT BINDING 104..109
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 131..137
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 156
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 77
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT SITE 103
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 167
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 175
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT DISULFID 47..172
FT /evidence="ECO:0000269|PubMed:28827170,
FT ECO:0007744|PDB:5GWO, ECO:0007744|PDB:5GWP"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5ZCU"
FT STRAND 46..57
FT /evidence="ECO:0007829|PDB:5ZCG"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:5ZCG"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:5ZCU"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:5ZCG"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 149..161
FT /evidence="ECO:0007829|PDB:5ZCG"
FT HELIX 168..194
FT /evidence="ECO:0007829|PDB:5ZCG"
SQ SEQUENCE 204 AA; 23068 MW; 179AF01E5E15345D CRC64;
MVEVGGGAAE AAAGRRWRLA DERCDLRAAE TEYVRRFHRH EPRDHQCSSA VAKHIKAPVH
LVWSLVRRFD QPQLFKPFVS RCEMKGNIEI GSVREVNVKS GLPATRSTER LELLDDNEHI
LSVRFVGGDH RLKNYSSILT VHPEVIDGRP GTLVIESFVV DVPEGNTKDE TCYFVEALLK
CNLKSLAEVS ERLVVKDQTE PLDR
