PYL9_ORYSJ
ID PYL9_ORYSJ Reviewed; 207 AA.
AC Q5Z8S0;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Abscisic acid receptor PYL9 {ECO:0000305};
DE AltName: Full=PYR1-like protein 2 {ECO:0000303|PubMed:24743650};
DE Short=OsPYL2 {ECO:0000303|PubMed:24743650};
DE AltName: Full=PYR1-like protein 9 {ECO:0000303|PubMed:26362328};
DE Short=OsPYL9 {ECO:0000303|PubMed:26362328};
DE AltName: Full=Regulatory components of ABA receptor 9 {ECO:0000305};
GN Name=PYL9 {ECO:0000303|PubMed:26362328};
GN Synonyms=PYL2 {ECO:0000303|PubMed:24743650},
GN RCAR9 {ECO:0000303|PubMed:26362328};
GN OrderedLocusNames=Os06g0562200 {ECO:0000312|EMBL:BAF19788.1},
GN LOC_Os06g36670 {ECO:0000305};
GN ORFNames=P0456F09.29 {ECO:0000312|EMBL:BAD53834.1},
GN P0656E03.2 {ECO:0000312|EMBL:BAD53743.1};
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, INTERACTION WITH PP2C30 AND PP2C53, SUBCELLULAR LOCATION, AND
RP 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 [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ABSCISIC ACID,
RP FUNCTION, INTERACTION WITH PP2C06, AND HOMODIMERIZATION.
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).
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). Inhibits the activity of the
CC protein phosphatases PP2C06 and PP2C09 when activated by abscisic acid
CC (ABA) (PubMed:24743650). {ECO:0000269|PubMed:24743650,
CC ECO:0000269|PubMed:26362328}.
CC -!- SUBUNIT: Homodimer. Interacts with PP2C06 (PubMed:24743650). Interacts
CC with PP2C50. Binding to PP2C50 is dependent on the presence of abscisic
CC acid (ABA) (PubMed:28827170). Interacts with PP2C30 and PP2C53. Binding
CC to PP2C30 and PP2C53 is dependent on the presence of ABA
CC (PubMed:26362328). {ECO:0000269|PubMed:24743650,
CC ECO:0000269|PubMed:26362328, 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 PYL9 exhibit abscisic acid (ABA)
CC hypersensitive phenotype during seed germination. Plants overexpressing
CC PYL9 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP003714; BAD53743.1; -; Genomic_DNA.
DR EMBL; AP003762; BAD53834.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19788.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS98256.1; -; Genomic_DNA.
DR RefSeq; XP_015641755.1; XM_015786269.1.
DR PDB; 4OIC; X-ray; 2.00 A; A=1-207.
DR PDBsum; 4OIC; -.
DR AlphaFoldDB; Q5Z8S0; -.
DR SMR; Q5Z8S0; -.
DR STRING; 4530.OS06T0562200-01; -.
DR PaxDb; Q5Z8S0; -.
DR PRIDE; Q5Z8S0; -.
DR EnsemblPlants; Os06t0562200-01; Os06t0562200-01; Os06g0562200.
DR GeneID; 4341308; -.
DR Gramene; Os06t0562200-01; Os06t0562200-01; Os06g0562200.
DR KEGG; osa:4341308; -.
DR eggNOG; ENOG502QU62; Eukaryota.
DR HOGENOM; CLU_077517_0_1_1; -.
DR InParanoid; Q5Z8S0; -.
DR OMA; ESTINTH; -.
DR OrthoDB; 1267148at2759; -.
DR PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
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:0042803; F:protein homodimerization activity; 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; IMP: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; Nucleus;
KW Protein phosphatase inhibitor; Receptor; Reference proteome;
KW Stress response.
FT CHAIN 1..207
FT /note="Abscisic acid receptor PYL9"
FT /id="PRO_0000444341"
FT REGION 31..197
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 74
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:24743650,
FT ECO:0007744|PDB:4OIC"
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 162
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 103
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 173
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:4OIC"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:4OIC"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:4OIC"
FT STRAND 44..55
FT /evidence="ECO:0007829|PDB:4OIC"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:4OIC"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4OIC"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:4OIC"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4OIC"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4OIC"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:4OIC"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:4OIC"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:4OIC"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:4OIC"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:4OIC"
FT STRAND 157..167
FT /evidence="ECO:0007829|PDB:4OIC"
FT HELIX 174..198
FT /evidence="ECO:0007829|PDB:4OIC"
SQ SEQUENCE 207 AA; 22333 MW; 31E357633F50CD76 CRC64;
MEAHVERALR EGLTEEERAA LEPAVMAHHT FPPSTTTATT AAATCTSLVT QRVAAPVRAV
WPIVRSFGNP QRYKHFVRTC ALAAGDGASV GSVREVTVVS GLPASTSTER LEMLDDDRHI
ISFRVVGGQH RLRNYRSVTS VTEFQPPAAG PGPAPPYCVV VESYVVDVPD GNTAEDTRMF
TDTVVKLNLQ MLAAVAEDSS SASRRRD