PYL5_ARATH
ID PYL5_ARATH Reviewed; 203 AA.
AC Q9FLB1;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Abscisic acid receptor PYL5;
DE AltName: Full=ABI1-binding protein 3;
DE AltName: Full=PYR1-like protein 5;
DE AltName: Full=Regulatory components of ABA receptor 8;
GN Name=PYL5; Synonyms=ABIP3, RCAR8; OrderedLocusNames=At5g05440;
GN ORFNames=K18I23.25;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH HAB1; ABI1 AND ABI2.
RX PubMed=19898420; DOI=10.1038/nature08613;
RA Melcher K., Ng L.-M., Zhou X.E., Soon F.-F., Xu Y., Suino-Powell K.M.,
RA Park S.-Y., Weiner J.J., Fujii H., Chinnusamy V., Kovach A., Li J.,
RA Wang Y., Li J., Peterson F.C., Jensen D.R., Yong E.-L., Volkman B.F.,
RA Cutler S.R., Zhu J.-K., Xu H.E.;
RT "A gate-latch-lock mechanism for hormone signalling by abscisic acid
RT receptors.";
RL Nature 462:602-608(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HAB1.
RX PubMed=19624469; DOI=10.1111/j.1365-313x.2009.03981.x;
RA Santiago J., Rodrigues A., Saez A., Rubio S., Antoni R., Dupeux F.,
RA Park S.-Y., Marquez J.A., Cutler S.R., Rodriguez P.L.;
RT "Modulation of drought resistance by the abscisic acid receptor PYL5
RT through inhibition of clade A PP2Cs.";
RL Plant J. 60:575-588(2009).
RN [7]
RP INTERACTION WITH ABI1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19874541; DOI=10.1111/j.1365-313x.2009.04054.x;
RA Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C.,
RA Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I.;
RT "PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C-
RT interacting proteins in Arabidopsis.";
RL Plant J. 61:290-299(2010).
RN [8]
RP FUNCTION, AND GENE FAMILY.
RX PubMed=19407143; DOI=10.1126/science.1172408;
RA Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A.,
RA Grill E.;
RT "Regulators of PP2C phosphatase activity function as abscisic acid
RT sensors.";
RL Science 324:1064-1068(2009).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19407142; DOI=10.1126/science.1173041;
RA Park S.-Y., Fung P., Nishimura N., Jensen D.R., Fujii H., Zhao Y.,
RA Lumba S., Santiago J., Rodrigues A., Chow T.F., Alfred S.E., Bonetta D.,
RA Finkelstein R., Provart N.J., Desveaux D., Rodriguez P.L., McCourt P.,
RA Zhu J.-K., Schroeder J.I., Volkman B.F., Cutler S.R.;
RT "Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family
RT of START proteins.";
RL Science 324:1068-1071(2009).
RN [10]
RP FUNCTION, MONOMER, AND GENE FAMILY.
RX PubMed=21658606; DOI=10.1016/j.molcel.2011.05.011;
RA Hao Q., Yin P., Li W., Wang L., Yan C., Lin Z., Wu J.Z., Wang J., Yan S.F.,
RA Yan N.;
RT "The molecular basis of ABA-independent inhibition of PP2Cs by a subclass
RT of PYL proteins.";
RL Mol. Cell 42:662-672(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS), FUNCTION, INTERACTION WITH ABA, AND
RP GENE FAMILY.
RX PubMed=23844015; DOI=10.1371/journal.pone.0067477;
RA Zhang X., Jiang L., Wang G., Yu L., Zhang Q., Xin Q., Wu W., Gong Z.,
RA Chen Z.;
RT "Structural insights into the abscisic acid stereospecificity by the ABA
RT receptors PYR/PYL/RCAR.";
RL PLoS ONE 8:E67477-E67477(2013).
CC -!- FUNCTION: Receptor for abscisic acid (ABA) required for ABA-mediated
CC responses such as stomatal closure and germination inhibition. Inhibits
CC the activity of group-A protein phosphatases type 2C (PP2Cs) in an ABA-
CC independent manner but more efficiently when activated by ABA. Confers
CC enhanced sensitivity to ABA (PubMed:19407143, PubMed:19624469,
CC PubMed:23844015, PubMed:21658606). Can be activated by both (-)-ABA and
CC (+)-ABA (PubMed:23844015). {ECO:0000269|PubMed:19407143,
CC ECO:0000269|PubMed:19624469, ECO:0000269|PubMed:21658606,
CC ECO:0000269|PubMed:23844015}.
CC -!- SUBUNIT: Monomer (PubMed:21658606). Homodimer. Binds ABA on one subunit
CC only. Binds to CARs protein in an ABA-independent manner, both at the
CC plasma membrane and in the nucleus (By similarity). Binds both (-)-ABA
CC and (+)-ABA (PubMed:23844015). Interacts with HAB1, ABI1 and ABI2, and
CC possibly with other PP2Cs (PubMed:19624469, PubMed:19874541,
CC PubMed:19898420). {ECO:0000250|UniProtKB:O49686,
CC ECO:0000269|PubMed:19624469, ECO:0000269|PubMed:19874541,
CC ECO:0000269|PubMed:19898420, ECO:0000269|PubMed:21658606,
CC ECO:0000269|PubMed:23844015}.
CC -!- INTERACTION:
CC Q9FLB1; P49597: ABI1; NbExp=12; IntAct=EBI-2363181, EBI-782526;
CC Q9FLB1; O04719: ABI2; NbExp=4; IntAct=EBI-2363181, EBI-537680;
CC Q9FLB1; O04719-1: ABI2; NbExp=2; IntAct=EBI-2363181, EBI-15803514;
CC Q9FLB1; Q9LNW3: AIP1; NbExp=3; IntAct=EBI-2363181, EBI-1573499;
CC Q9FLB1; Q9ZW21: At2g29380; NbExp=3; IntAct=EBI-2363181, EBI-4441103;
CC Q9FLB1; A0A178VYJ2: At2g42490; NbExp=3; IntAct=EBI-2363181, EBI-25529042;
CC Q9FLB1; O82754: At4g23050; NbExp=3; IntAct=EBI-2363181, EBI-1238561;
CC Q9FLB1; Q9FLC1: At5g05330; NbExp=3; IntAct=EBI-2363181, EBI-25529069;
CC Q9FLB1; Q9CAJ0: HAB1; NbExp=11; IntAct=EBI-2363181, EBI-2309302;
CC Q9FLB1; Q9LNP9: HAB2; NbExp=5; IntAct=EBI-2363181, EBI-15803614;
CC Q9FLB1; Q9SN12: MYB77; NbExp=3; IntAct=EBI-2363181, EBI-2324225;
CC Q9FLB1; P49598: PP2CA; NbExp=3; IntAct=EBI-2363181, EBI-1764934;
CC Q9FLB1; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2363181, EBI-4426178;
CC Q9FLB1; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-2363181, EBI-15192297;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19624469}. Nucleus
CC {ECO:0000269|PubMed:19624469}. Cell membrane
CC {ECO:0000250|UniProtKB:O49686}. Note=Localizes at the plasma membrane
CC in the presence of a CAR protein. {ECO:0000250|UniProtKB:O80920}.
CC -!- DOMAIN: Upon interaction with ABA, the 'latch' and 'gate' loops change
CC in conformation leading to a tight dimerization and the creation a
CC surface that enables the receptor to dock into and inhibit the PP2C
CC active site. {ECO:0000250|UniProtKB:Q8VZS8}.
CC -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
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DR EMBL; AB010692; BAB09987.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90874.1; -; Genomic_DNA.
DR EMBL; AY052251; AAK97721.1; -; mRNA.
DR EMBL; AY060510; AAL31123.1; -; mRNA.
DR EMBL; BT000728; AAN31870.1; -; mRNA.
DR EMBL; AY084767; AAM61335.1; -; mRNA.
DR RefSeq; NP_196163.1; NM_120626.3.
DR PDB; 4JDL; X-ray; 2.60 A; A/B/C=1-203.
DR PDBsum; 4JDL; -.
DR AlphaFoldDB; Q9FLB1; -.
DR SMR; Q9FLB1; -.
DR BioGRID; 15706; 15.
DR DIP; DIP-53483N; -.
DR IntAct; Q9FLB1; 13.
DR MINT; Q9FLB1; -.
DR STRING; 3702.AT5G05440.1; -.
DR PaxDb; Q9FLB1; -.
DR PRIDE; Q9FLB1; -.
DR ProteomicsDB; 224809; -.
DR EnsemblPlants; AT5G05440.1; AT5G05440.1; AT5G05440.
DR GeneID; 830427; -.
DR Gramene; AT5G05440.1; AT5G05440.1; AT5G05440.
DR KEGG; ath:AT5G05440; -.
DR Araport; AT5G05440; -.
DR TAIR; locus:2153549; AT5G05440.
DR eggNOG; ENOG502QWFG; Eukaryota.
DR HOGENOM; CLU_077517_0_0_1; -.
DR InParanoid; Q9FLB1; -.
DR OMA; IKRVCLT; -.
DR OrthoDB; 1400653at2759; -.
DR PhylomeDB; Q9FLB1; -.
DR PRO; PR:Q9FLB1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLB1; baseline and differential.
DR Genevisible; Q9FLB1; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010427; F:abscisic acid binding; IDA:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
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; Cell membrane; Cytoplasm;
KW Membrane; Nucleus; Protein phosphatase inhibitor; Receptor;
KW Reference proteome.
FT CHAIN 1..203
FT /note="Abscisic acid receptor PYL5"
FT /id="PRO_0000391740"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..201
FT /note="START-like"
FT MOTIF 113..117
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 143..145
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 117..122
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 144..150
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 166
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 116
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 177
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 185
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:4JDL"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:4JDL"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:4JDL"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:4JDL"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4JDL"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4JDL"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:4JDL"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4JDL"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4JDL"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:4JDL"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:4JDL"
FT HELIX 181..199
FT /evidence="ECO:0007829|PDB:4JDL"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:4JDL"
SQ SEQUENCE 203 AA; 22662 MW; 5A446F5E40D5AF11 CRC64;
MRSPVQLQHG SDATNGFHTL QPHDQTDGPI KRVCLTRGMH VPEHVAMHHT HDVGPDQCCS
SVVQMIHAPP ESVWALVRRF DNPKVYKNFI RQCRIVQGDG LHVGDLREVM VVSGLPAVSS
TERLEILDEE RHVISFSVVG GDHRLKNYRS VTTLHASDDE GTVVVESYIV DVPPGNTEEE
TLSFVDTIVR CNLQSLARST NRQ
