PYR1_ARATH
ID PYR1_ARATH Reviewed; 191 AA.
AC O49686;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Abscisic acid receptor PYR1 {ECO:0000303|PubMed:19624469, ECO:0000303|PubMed:19898494};
DE AltName: Full=ABI1-binding protein 6 {ECO:0000303|PubMed:19874541};
DE AltName: Full=Protein PYRABACTIN RESISTANCE 1 {ECO:0000303|PubMed:19624469, ECO:0000303|PubMed:19898494};
DE AltName: Full=Regulatory components of ABA receptor 11 {ECO:0000303|PubMed:19407143};
GN Name=PYR1 {ECO:0000303|PubMed:19624469, ECO:0000303|PubMed:19898494};
GN Synonyms=ABIP6 {ECO:0000303|PubMed:19874541},
GN RCAR11 {ECO:0000303|PubMed:19407143};
GN OrderedLocusNames=At4g17870 {ECO:0000312|Araport:AT4G17870};
GN ORFNames=T6K21.50 {ECO:0000312|EMBL:CAA17130.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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 [5]
RP FUNCTION.
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 [6]
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 [7]
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 [8]
RP FUNCTION, MUTAGENESIS OF PRO-88; SER-152 AND ARG-157, INTERACTION WITH
RP HAB1; AHG3; ABI1 AND ABI2, 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 [9]
RP FUNCTION.
RX PubMed=19769575; DOI=10.1111/j.1365-313x.2009.04025.x;
RA Szostkiewicz I., Richter K., Kepka M., Demmel S., Ma Y., Korte A.,
RA Assaad F.F., Christmann A., Grill E.;
RT "Closely related receptor complexes differ in their ABA selectivity and
RT sensitivity.";
RL Plant J. 61:25-35(2010).
RN [10]
RP FUNCTION, HOMODIMER, 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 INTERACTION WITH AIP1.
RX PubMed=23378449; DOI=10.1093/pcp/pct017;
RA Kim W., Lee Y., Park J., Lee N., Choi G.;
RT "HONSU, a protein phosphatase 2C, regulates seed dormancy by inhibiting ABA
RT signaling in Arabidopsis.";
RL Plant Cell Physiol. 54:555-572(2013).
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 INTERACTION WITH RSL1, SUBCELLULAR LOCATION, AND PTM.
RC STRAIN=cv. Columbia;
RX PubMed=25330042; DOI=10.1111/tpj.12708;
RA Bueso E., Rodriguez L., Lorenzo-Orts L., Gonzalez-Guzman M., Sayas E.,
RA Munoz-Bertomeu J., Ibanez C., Serrano R., Rodriguez P.L.;
RT "The single-subunit RING-type E3 ubiquitin ligase RSL1 targets PYL4 and
RT PYR1 ABA receptors in plasma membrane to modulate abscisic acid
RT signaling.";
RL Plant J. 80:1057-1071(2014).
RN [15]
RP INTERACTION WITH FREE1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27495812; DOI=10.1105/tpc.16.00178;
RA Belda-Palazon B., Rodriguez L., Fernandez M.A., Castillo M.-C.,
RA Anderson E.M., Gao C., Gonzalez-Guzman M., Peirats-Llobet M., Zhao Q.,
RA De Winne N., Gevaert K., De Jaeger G., Jiang L., Leon J., Mullen R.T.,
RA Rodriguez P.L.;
RT "FYVE1/FREE1 interacts with the PYL4 ABA receptor and mediates its delivery
RT to the vacuolar degradation pathway.";
RL Plant Cell 28:2291-2311(2016).
RN [16]
RP INTERACTION WITH CAR4.
RC STRAIN=cv. Columbia;
RX PubMed=26719420; DOI=10.1073/pnas.1512779113;
RA Diaz M., Sanchez-Barrena M.J., Gonzalez-Rubio J.M., Rodriguez L.,
RA Fernandez D., Antoni R., Yunta C., Belda-Palazon B., Gonzalez-Guzman M.,
RA Peirats-Llobet M., Menendez M., Boskovic J., Marquez J.A., Rodriguez P.L.,
RA Albert A.;
RT "Calcium-dependent oligomerization of CAR proteins at cell membrane
RT modulates ABA signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E396-E405(2016).
RN [17]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=29970817; DOI=10.3390/ijms19071945;
RA Ge H., Li X., Chen S., Zhang M., Liu Z., Wang J., Li X., Yang Y.;
RT "The expression of CARK1 or RCAR11 driven by synthetic promoters increases
RT drought tolerance in Arabidopsis thaliana.";
RL Int. J. Mol. Sci. 19:1945-1945(2018).
RN [18]
RP MUTAGENESIS OF THR-78, INTERACTION WITH CARK1, PHOSPHORYLATION AT THR-78,
RP PTM, AND SUBCELLULAR LOCATION.
RX PubMed=29928509; DOI=10.1038/s41421-018-0029-y;
RA Zhang L., Li X., Li D., Sun Y., Li Y., Luo Q., Liu Z., Wang J., Li X.,
RA Zhang H., Lou Z., Yang Y.;
RT "CARK1 mediates ABA signaling by phosphorylation of ABA receptors.";
RL Cell Discov. 4:30-30(2018).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-191 IN COMPLEX WITH ABSCISIC
RP ACID, SUBUNIT, AND DIMERIZATION.
RX PubMed=19898494; DOI=10.1038/nature08591;
RA Santiago J., Dupeux F., Round A., Antoni R., Park S.-Y., Jamin M.,
RA Cutler S.R., Rodriguez P.L., Marquez J.A.;
RT "The abscisic acid receptor PYR1 in complex with abscisic acid.";
RL Nature 462:665-668(2009).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH ABSCISIC ACID,
RP MUTAGENESIS OF LYS-59 AND ARG-116, INTERACTION WITH ABI1, SUBUNIT, AND
RP DIMERIZATION.
RX PubMed=19933100; DOI=10.1126/science.1181829;
RA Nishimura N., Hitomi K., Arvai A.S., Rambo R.P., Hitomi C., Cutler S.R.,
RA Schroeder J.I., Getzoff E.D.;
RT "Structural mechanism of abscisic acid binding and signaling by dimeric
RT PYR1.";
RL Science 326:1373-1379(2009).
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) when
CC activated by ABA (PubMed:19407142, PubMed:19624469, PubMed:19769575,
CC PubMed:23844015, PubMed:21658606). Can be activated by both (-)-ABA and
CC (+)-ABA (PubMed:23844015). Promotes drought tolerance
CC (PubMed:29970817). {ECO:0000269|PubMed:19407142,
CC ECO:0000269|PubMed:19624469, ECO:0000269|PubMed:19769575,
CC ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:23844015,
CC ECO:0000269|PubMed:29970817}.
CC -!- SUBUNIT: Homodimer (PubMed:21658606,PubMed:19898494,PubMed:19933100).
CC Binds ABA on one subunit only. Interacts with HAB1, AHG3, ABI1 and ABI2
CC when complexed to ABA, and possibly with other PP2Cs (PubMed:19407142,
CC PubMed:19874541, PubMed:19898420, PubMed:19898494, PubMed:19933100).
CC Binds to CARs protein in an ABA-independent manner, both at the plasma
CC membrane and in the nucleus (PubMed:26719420). Interacts directly with
CC CAR1 and CAR4 (PubMed:25465408, PubMed:26719420). Interacts with CARK1
CC in the cytosol (PubMed:29928509, PubMed:19407142, PubMed:19874541,
CC PubMed:19898420, PubMed:19898494, PubMed:19933100, PubMed:21658606,
CC PubMed:25465408, PubMed:26719420). Interacts with AIP1 in an abscisic
CC acid-dependent manner (PubMed:29928509). Interacts with FREE1 (via N-
CC terminus) (PubMed:27495812). Interacts with the E3 ubiquitin-protein
CC ligase RSL1 at the plasma membrane (PubMed:25330042).
CC {ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19874541,
CC ECO:0000269|PubMed:19898420, ECO:0000269|PubMed:19898494,
CC ECO:0000269|PubMed:19933100, ECO:0000269|PubMed:21658606,
CC ECO:0000269|PubMed:25330042, ECO:0000269|PubMed:25465408,
CC ECO:0000269|PubMed:26719420, ECO:0000269|PubMed:27495812,
CC ECO:0000269|PubMed:29928509}.
CC -!- INTERACTION:
CC O49686; P49597: ABI1; NbExp=12; IntAct=EBI-2349590, EBI-782526;
CC O49686; O04719: ABI2; NbExp=3; IntAct=EBI-2349590, EBI-537680;
CC O49686; O04719-1: ABI2; NbExp=2; IntAct=EBI-2349590, EBI-15803514;
CC O49686; Q9LNW3: AIP1; NbExp=3; IntAct=EBI-2349590, EBI-1573499;
CC O49686; Q9CAJ0: HAB1; NbExp=17; IntAct=EBI-2349590, EBI-2309302;
CC O49686; O49686: PYR1; NbExp=8; IntAct=EBI-2349590, EBI-2349590;
CC O49686; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2349590, EBI-4426178;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:29928509}. Nucleus
CC {ECO:0000269|PubMed:25465408}. Cell membrane
CC {ECO:0000269|PubMed:25330042, ECO:0000269|PubMed:25465408}. Vacuole
CC {ECO:0000269|PubMed:27495812}. Note=Localizes at the plasma membrane in
CC the presence of a CAR protein (By similarity). Localized transiently in
CC the vacuole when in complex with RSL1 (PubMed:27495812).
CC {ECO:0000250|UniProtKB:O80920, ECO:0000269|PubMed:27495812}.
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 -!- PTM: Ubiquitynated and degraded by the proteasome upon binding to the
CC E3 ubiquitin-protein ligase RSL1 at the plasma membrane.
CC {ECO:0000269|PubMed:25330042}.
CC -!- PTM: Phosphorylated by CARK1 especially in response to abscisic acid
CC (ABA); this phosphorylation promotes its stability and inhibitory
CC ability to ABI1. {ECO:0000269|PubMed:29928509}.
CC -!- MISCELLANEOUS: The synthetic growth inhibitor pyrabactin inhibits ABA-
CC binding and subsequent PP2Cs inhibitor properties.
CC -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
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DR EMBL; AL021889; CAA17130.1; -; Genomic_DNA.
DR EMBL; AL161547; CAB78789.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83959.1; -; Genomic_DNA.
DR EMBL; AY042890; AAK68830.1; -; mRNA.
DR EMBL; AY081526; AAM10088.1; -; mRNA.
DR PIR; T05073; T05073.
DR RefSeq; NP_193521.1; NM_117896.3.
DR PDB; 3K3K; X-ray; 1.70 A; A/B=1-191.
DR PDB; 3K90; X-ray; 2.00 A; A/B/C/D=1-191.
DR PDB; 3NJO; X-ray; 2.47 A; A/B/C=1-191.
DR PDB; 3QN1; X-ray; 1.80 A; A=3-191.
DR PDB; 3WG8; X-ray; 2.30 A; A=1-191.
DR PDB; 3ZVU; X-ray; 2.10 A; A=3-191.
DR PDB; 4WVO; X-ray; 2.25 A; A=1-181.
DR PDB; 5OR2; X-ray; 2.50 A; A=3-191.
DR PDB; 5OR6; X-ray; 2.40 A; A=3-191.
DR PDB; 5UR4; X-ray; 1.52 A; A=1-181.
DR PDB; 5UR5; X-ray; 1.93 A; A=1-181.
DR PDB; 5UR6; X-ray; 1.63 A; A=1-181.
DR PDB; 5YGV; X-ray; 2.50 A; A/B=1-191.
DR PDBsum; 3K3K; -.
DR PDBsum; 3K90; -.
DR PDBsum; 3NJO; -.
DR PDBsum; 3QN1; -.
DR PDBsum; 3WG8; -.
DR PDBsum; 3ZVU; -.
DR PDBsum; 4WVO; -.
DR PDBsum; 5OR2; -.
DR PDBsum; 5OR6; -.
DR PDBsum; 5UR4; -.
DR PDBsum; 5UR5; -.
DR PDBsum; 5UR6; -.
DR PDBsum; 5YGV; -.
DR AlphaFoldDB; O49686; -.
DR SMR; O49686; -.
DR BioGRID; 12803; 14.
DR ComplexPortal; CPX-1620; PYR1 ABA receptor complex.
DR DIP; DIP-53473N; -.
DR IntAct; O49686; 11.
DR MINT; O49686; -.
DR STRING; 3702.AT4G17870.1; -.
DR iPTMnet; O49686; -.
DR PaxDb; O49686; -.
DR PRIDE; O49686; -.
DR ProteomicsDB; 224811; -.
DR EnsemblPlants; AT4G17870.1; AT4G17870.1; AT4G17870.
DR GeneID; 827510; -.
DR Gramene; AT4G17870.1; AT4G17870.1; AT4G17870.
DR KEGG; ath:AT4G17870; -.
DR Araport; AT4G17870; -.
DR TAIR; locus:2141040; AT4G17870.
DR eggNOG; ENOG502QW1M; Eukaryota.
DR HOGENOM; CLU_077517_0_1_1; -.
DR InParanoid; O49686; -.
DR OMA; EREGRIW; -.
DR OrthoDB; 1238726at2759; -.
DR PhylomeDB; O49686; -.
DR EvolutionaryTrace; O49686; -.
DR PRO; PR:O49686; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49686; baseline and differential.
DR Genevisible; O49686; AT.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0062049; C:protein phosphatase inhibitor complex; IPI:ComplexPortal.
DR GO; GO:0010427; F:abscisic acid binding; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; 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:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IDA:TAIR.
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; Phosphoprotein; Protein phosphatase inhibitor; Receptor;
KW Reference proteome; Vacuole.
FT CHAIN 1..191
FT /note="Abscisic acid receptor PYR1"
FT /id="PRO_0000391735"
FT REGION 23..176
FT /note="START-like"
FT MOTIF 85..89
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 115..117
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 59
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:19898494,
FT ECO:0000269|PubMed:19933100"
FT BINDING 89..94
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:19898494,
FT ECO:0000269|PubMed:19933100"
FT BINDING 116..122
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:19898494,
FT ECO:0000269|PubMed:19933100"
FT BINDING 141
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:19898494,
FT ECO:0000269|PubMed:19933100"
FT SITE 88
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000269|PubMed:19407142"
FT SITE 152
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000269|PubMed:19407142"
FT MOD_RES 78
FT /note="Phosphothreonine; by CARK1"
FT /evidence="ECO:0000269|PubMed:29928509"
FT MUTAGEN 59
FT /note="K->Q: Impaired ABA-mediated binding to PP2Cs."
FT /evidence="ECO:0000269|PubMed:19933100"
FT MUTAGEN 78
FT /note="T->A: Reduced CARK1-mediated phosphorylation."
FT /evidence="ECO:0000269|PubMed:29928509"
FT MUTAGEN 88
FT /note="P->S: Insensitivity to pyrabactin and impaired ABA-
FT mediated binding to PP2Cs."
FT /evidence="ECO:0000269|PubMed:19407142"
FT MUTAGEN 116
FT /note="R->G: Impaired ABA-mediated binding to PP2Cs."
FT /evidence="ECO:0000269|PubMed:19933100"
FT MUTAGEN 152
FT /note="S->L: Insensitivity to pyrabactin and impaired ABA-
FT mediated binding to PP2Cs."
FT /evidence="ECO:0000269|PubMed:19407142"
FT MUTAGEN 157
FT /note="R->H: Reduced sensitivity to pyrabactin."
FT /evidence="ECO:0000269|PubMed:19407142"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:3ZVU"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:5UR4"
FT HELIX 14..20
FT /evidence="ECO:0007829|PDB:5UR4"
FT STRAND 29..40
FT /evidence="ECO:0007829|PDB:5UR4"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:5UR4"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5UR4"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:5UR4"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:5UR4"
FT STRAND 87..100
FT /evidence="ECO:0007829|PDB:5UR4"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:5UR4"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:5UR4"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:5UR4"
FT STRAND 134..146
FT /evidence="ECO:0007829|PDB:5UR4"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:3K3K"
FT HELIX 158..179
FT /evidence="ECO:0007829|PDB:5UR4"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:3K3K"
SQ SEQUENCE 191 AA; 21575 MW; AD35DA240E286B55 CRC64;
MPSELTPEER SELKNSIAEF HTYQLDPGSC SSLHAQRIHA PPELVWSIVR RFDKPQTYKH
FIKSCSVEQN FEMRVGCTRD VIVISGLPAN TSTERLDILD DERRVTGFSI IGGEHRLTNY
KSVTTVHRFE KENRIWTVVL ESYVVDMPEG NSEDDTRMFA DTVVKLNLQK LATVAEAMAR
NSGDGSGSQV T
