PYL6_ARATH
ID PYL6_ARATH Reviewed; 215 AA.
AC Q8S8E3; Q9S718;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Abscisic acid receptor PYL6;
DE AltName: Full=ABI1-binding protein 5;
DE AltName: Full=PYR1-like protein 6;
DE AltName: Full=Regulatory components of ABA receptor 9;
GN Name=PYL6; Synonyms=ABIP5, RCAR9; OrderedLocusNames=At2g40330;
GN ORFNames=T3G21, T7M7.15;
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 [GENOMIC DNA].
RX PubMed=10207155;
RA Wang M.L., Belmonte S., Kim U., Dolan M., Morris J.W., Goodman H.M.;
RT "A cluster of ABA-regulated genes on Arabidopsis thaliana BAC T07M07.";
RL Genome Res. 9:325-333(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP 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 [8]
RP 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 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 [11]
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 [12]
RP FUNCTION, AND 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).
RN [13]
RP INTERACTION WITH CAR1 AND CAR4, AND SUBCELLULAR LOCATION.
RX PubMed=25465408; DOI=10.1105/tpc.114.129973;
RA Rodriguez L., Gonzalez-Guzman M., Diaz M., Rodrigues A.,
RA Izquierdo-Garcia A.C., Peirats-Llobet M., Fernandez M.A., Antoni R.,
RA Fernandez D., Marquez J.A., Mulet J.M., Albert A., Rodriguez P.L.;
RT "C2-domain abscisic acid-related proteins mediate the interaction of
RT PYR/PYL/RCAR abscisic acid receptors with the plasma membrane and regulate
RT abscisic acid sensitivity in Arabidopsis.";
RL Plant Cell 26:4802-4820(2014).
RN [14]
RP FUNCTION, INTERACTION WITH MYC2, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27357749; DOI=10.1038/srep28941;
RA Aleman F., Yazaki J., Lee M., Takahashi Y., Kim A.Y., Li Z., Kinoshita T.,
RA Ecker J.R., Schroeder J.I.;
RT "An ABA-increased interaction of the PYL6 ABA receptor with MYC2
RT Transcription Factor: A putative link of ABA and JA signaling.";
RL Sci. Rep. 6:28941-28941(2016).
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
CC (PubMed:23844015, PubMed:21658606). Can be activated by both (-)-ABA
CC and (+)-ABA (PubMed:23844015). May link ABA and jasmonate signaling
CC pathways by modifying MYC2 transcriptional activity, and regulation of
CC JAZ6 and JAZ8 gene expression by MYC2 (PubMed:27357749).
CC {ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:23844015,
CC ECO:0000269|PubMed:27357749}.
CC -!- SUBUNIT: Monomer (PubMed:21658606). Homodimer. Binds ABA on one subunit
CC only (By similarity). Interacts with HAB1, ABI1 and ABI2, and possibly
CC with other PP2Cs (PubMed:19624469, PubMed:19874541, PubMed:19898420).
CC Binds to CARs protein in an ABA-independent manner, both at the plasma
CC membrane and in the nucleus. Interacts directly with CAR1 and CAR4
CC (PubMed:25465408). Interacts with MYC2 in the nucleus. Interaction with
CC MYC2 is increased in the presence of abscisic acid (PubMed:27357749).
CC {ECO:0000250|UniProtKB:O49686, ECO:0000269|PubMed:19624469,
CC ECO:0000269|PubMed:19874541, ECO:0000269|PubMed:19898420,
CC ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:25465408,
CC ECO:0000269|PubMed:27357749}.
CC -!- INTERACTION:
CC Q8S8E3; P49597: ABI1; NbExp=9; IntAct=EBI-2363192, EBI-782526;
CC Q8S8E3; O04719: ABI2; NbExp=4; IntAct=EBI-2363192, EBI-537680;
CC Q8S8E3; O04719-1: ABI2; NbExp=2; IntAct=EBI-2363192, EBI-15803514;
CC Q8S8E3; Q9SFD5: ADA2A; NbExp=3; IntAct=EBI-2363192, EBI-979206;
CC Q8S8E3; Q9LNW3: AIP1; NbExp=3; IntAct=EBI-2363192, EBI-1573499;
CC Q8S8E3; Q8VYZ1: At1g33050; NbExp=3; IntAct=EBI-2363192, EBI-25529097;
CC Q8S8E3; A0A1P8AVS2: At1g72340; NbExp=3; IntAct=EBI-2363192, EBI-25528474;
CC Q8S8E3; Q9ZW21: At2g29380; NbExp=3; IntAct=EBI-2363192, EBI-4441103;
CC Q8S8E3; Q9ZPY4: At2g46550; NbExp=3; IntAct=EBI-2363192, EBI-25529212;
CC Q8S8E3; Q9SZE1: At4g29120; NbExp=3; IntAct=EBI-2363192, EBI-25528671;
CC Q8S8E3; Q9FLC1: At5g05330; NbExp=3; IntAct=EBI-2363192, EBI-25529069;
CC Q8S8E3; A0A178UGU3: AXX17_At5g13230; NbExp=3; IntAct=EBI-2363192, EBI-25529113;
CC Q8S8E3; Q9SAD4: ESR1; NbExp=3; IntAct=EBI-2363192, EBI-1536756;
CC Q8S8E3; Q8L743: G6PD3; NbExp=3; IntAct=EBI-2363192, EBI-2355237;
CC Q8S8E3; Q9CAJ0: HAB1; NbExp=9; IntAct=EBI-2363192, EBI-2309302;
CC Q8S8E3; Q9LNP9: HAB2; NbExp=5; IntAct=EBI-2363192, EBI-15803614;
CC Q8S8E3; Q9SN12: MYB77; NbExp=3; IntAct=EBI-2363192, EBI-2324225;
CC Q8S8E3; Q9LS24: NAC096; NbExp=3; IntAct=EBI-2363192, EBI-1238916;
CC Q8S8E3; Q38845: PP2AA1; NbExp=3; IntAct=EBI-2363192, EBI-1645478;
CC Q8S8E3; P49598: PP2CA; NbExp=3; IntAct=EBI-2363192, EBI-1764934;
CC Q8S8E3; O82277: TCP10; NbExp=3; IntAct=EBI-2363192, EBI-3133327;
CC Q8S8E3; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-2363192, EBI-4424877;
CC Q8S8E3; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-2363192, EBI-4426144;
CC Q8S8E3; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2363192, EBI-4426178;
CC Q8S8E3; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-2363192, EBI-25522447;
CC Q8S8E3; O64647: TCP9; NbExp=3; IntAct=EBI-2363192, EBI-9838721;
CC Q8S8E3; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-2363192, EBI-4426557;
CC Q8S8E3; Q9LVG2: TOE2; NbExp=3; IntAct=EBI-2363192, EBI-4424568;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Nucleus
CC {ECO:0000269|PubMed:25465408}. Cell membrane
CC {ECO:0000269|PubMed:25465408}. Nucleus {ECO:0000269|PubMed:27357749}.
CC Note=Localizes at the plasma membrane in the presence of a CAR protein
CC (e.g. CAR1 and CAR4). {ECO:0000269|PubMed:25465408}.
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 -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedlings exhibit increased sensitivity to
CC abscisic acid-induced inhibition of cotyledon expansion. The inhibition
CC effect is more severe with the combination of abscisic acid and
CC jasmonate. {ECO:0000269|PubMed:27357749}.
CC -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25950.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF085279; AAD25950.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC007020; AAD25668.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09815.1; -; Genomic_DNA.
DR EMBL; BT004281; AAO42281.1; -; mRNA.
DR EMBL; BT005608; AAO64028.1; -; mRNA.
DR EMBL; AY088453; AAM65989.1; -; mRNA.
DR RefSeq; NP_565928.1; NM_129593.3.
DR AlphaFoldDB; Q8S8E3; -.
DR SMR; Q8S8E3; -.
DR BioGRID; 3964; 30.
DR DIP; DIP-53482N; -.
DR IntAct; Q8S8E3; 27.
DR MINT; Q8S8E3; -.
DR STRING; 3702.AT2G40330.1; -.
DR PaxDb; Q8S8E3; -.
DR PRIDE; Q8S8E3; -.
DR ProteomicsDB; 226012; -.
DR EnsemblPlants; AT2G40330.1; AT2G40330.1; AT2G40330.
DR GeneID; 818626; -.
DR Gramene; AT2G40330.1; AT2G40330.1; AT2G40330.
DR KEGG; ath:AT2G40330; -.
DR Araport; AT2G40330; -.
DR TAIR; locus:2063063; AT2G40330.
DR eggNOG; ENOG502QWFG; Eukaryota.
DR HOGENOM; CLU_077517_0_0_1; -.
DR OMA; ARYHTHE; -.
DR OrthoDB; 1400653at2759; -.
DR PhylomeDB; Q8S8E3; -.
DR PRO; PR:Q8S8E3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8E3; baseline and differential.
DR Genevisible; Q8S8E3; AT.
DR GO; GO:0005737; C:cytoplasm; ISS: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; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP: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 Abscisic acid signaling pathway; Cell membrane; Cytoplasm; Disulfide bond;
KW Membrane; Nucleus; Protein phosphatase inhibitor; Receptor;
KW Reference proteome.
FT CHAIN 1..215
FT /note="Abscisic acid receptor PYL6"
FT /id="PRO_0000391741"
FT REGION 54..209
FT /note="START-like"
FT MOTIF 116..120
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 146..148
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 90
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 120..125
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 147..153
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 174
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 119
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT DISULFID 61..190
FT /note="Reversible"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
SQ SEQUENCE 215 AA; 23843 MW; 8B9D3F7BD9E2860D CRC64;
MPTSIQFQRS STAAEAANAT VRNYPHHHQK QVQKVSLTRG MADVPEHVEL SHTHVVGPSQ
CFSVVVQDVE APVSTVWSIL SRFEHPQAYK HFVKSCHVVI GDGREVGSVR EVRVVSGLPA
AFSLERLEIM DDDRHVISFS VVGGDHRLMN YKSVTTVHES EEDSDGKKRT RVVESYVVDV
PAGNDKEETC SFADTIVRCN LQSLAKLAEN TSKFS
