PYL10_ARATH
ID PYL10_ARATH Reviewed; 183 AA.
AC Q8H1R0; Q9SUE6;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Abscisic acid receptor PYL10;
DE AltName: Full=ABI1-binding protein 8;
DE AltName: Full=PYR1-like protein 10;
DE AltName: Full=Regulatory components of ABA receptor 4;
GN Name=PYL10; Synonyms=RCAR4; OrderedLocusNames=At4g27920; ORFNames=T13J8.30;
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 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 [5]
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 [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 INTERACTION WITH PYL13.
RX PubMed=24165892; DOI=10.1038/cr.2013.143;
RA Li W., Wang L., Sheng X., Yan C., Zhou R., Hang J., Yin P., Yan N.;
RT "Molecular basis for the selective and ABA-independent inhibition of PP2CA
RT by PYL13.";
RL Cell Res. 23:1369-1379(2013).
RN [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH HAB1, FUNCTION,
RP MONOMER, SUBUNIT, INTERACTION WITH ABI1 AND HAB1, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ABA.
RA Sun D.M., Wu M.H., Wang H.P., Zang J.Y., Tian C.L.;
RT "Crystal structure of abscisic acid-bound PYL10.";
RL Submitted (MAR-2011) to the PDB data bank.
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). {ECO:0000269|PubMed:21658606,
CC ECO:0000269|PubMed:23844015}.
CC -!- SUBUNIT: Monomer (PubMed:21658606). Forms heterodimer with PYL13, thus
CC antagonizing PP2Cs-binding and ABA-independent inhibition of PP2Cs
CC (PubMed:24165892). Homodimer. Binds ABA on one subunit only. Binds to
CC CARs protein in an ABA-independent manner, both at the plasma membrane
CC and in the nucleus (By similarity). Interacts with ABI1 and HAB1, and
CC possibly with other PP2Cs, in an ABA-independent manner
CC (PubMed:19874541, PubMed:21658606). {ECO:0000250|UniProtKB:O49686,
CC ECO:0000269|PubMed:19874541, ECO:0000269|PubMed:21658606,
CC ECO:0000269|PubMed:24165892}.
CC -!- INTERACTION:
CC Q8H1R0; P49597: ABI1; NbExp=7; IntAct=EBI-2363213, EBI-782526;
CC Q8H1R0; O04719: ABI2; NbExp=3; IntAct=EBI-2363213, EBI-537680;
CC Q8H1R0; Q9LNW3: AIP1; NbExp=3; IntAct=EBI-2363213, EBI-1573499;
CC Q8H1R0; Q9ZW21: At2g29380; NbExp=7; IntAct=EBI-2363213, EBI-4441103;
CC Q8H1R0; Q9SUC0: At4g20930; NbExp=3; IntAct=EBI-2363213, EBI-25528816;
CC Q8H1R0; O80507: CKB4; NbExp=5; IntAct=EBI-2363213, EBI-25528847;
CC Q8H1R0; Q9CAJ0: HAB1; NbExp=4; IntAct=EBI-2363213, EBI-2309302;
CC Q8H1R0; Q9LNP9: HAB2; NbExp=3; IntAct=EBI-2363213, EBI-15803614;
CC Q8H1R0; Q9SN12: MYB77; NbExp=3; IntAct=EBI-2363213, EBI-2324225;
CC Q8H1R0; P49598: PP2CA; NbExp=3; IntAct=EBI-2363213, EBI-1764934;
CC Q8H1R0; Q9FIF5: SAG113; NbExp=3; IntAct=EBI-2363213, EBI-2363373;
CC Q8H1R0; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2363213, EBI-4426178;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Nucleus
CC {ECO:0000250|UniProtKB:O49686}. 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36761.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79594.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035524; CAB36761.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161572; CAB79594.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85409.1; -; Genomic_DNA.
DR EMBL; AY142526; AAN13069.1; -; mRNA.
DR PIR; T02893; T02893.
DR RefSeq; NP_194521.2; NM_118930.3.
DR PDB; 3R6P; X-ray; 2.70 A; A=1-183.
DR PDB; 3RT0; X-ray; 2.11 A; C/D=1-183.
DR PDB; 3RT2; X-ray; 1.50 A; A=1-183.
DR PDB; 3UQH; X-ray; 3.00 A; A/B=1-183.
DR PDB; 6NWB; X-ray; 2.00 A; A=25-180.
DR PDB; 6NWC; X-ray; 2.35 A; A=25-179.
DR PDB; 7MLC; X-ray; 1.77 A; A=25-183.
DR PDB; 7MLD; X-ray; 1.80 A; A=25-183.
DR PDBsum; 3R6P; -.
DR PDBsum; 3RT0; -.
DR PDBsum; 3RT2; -.
DR PDBsum; 3UQH; -.
DR PDBsum; 6NWB; -.
DR PDBsum; 6NWC; -.
DR PDBsum; 7MLC; -.
DR PDBsum; 7MLD; -.
DR AlphaFoldDB; Q8H1R0; -.
DR SMR; Q8H1R0; -.
DR BioGRID; 14192; 13.
DR IntAct; Q8H1R0; 12.
DR STRING; 3702.AT4G27920.1; -.
DR PaxDb; Q8H1R0; -.
DR PRIDE; Q8H1R0; -.
DR EnsemblPlants; AT4G27920.1; AT4G27920.1; AT4G27920.
DR GeneID; 828905; -.
DR Gramene; AT4G27920.1; AT4G27920.1; AT4G27920.
DR KEGG; ath:AT4G27920; -.
DR Araport; AT4G27920; -.
DR TAIR; locus:2132917; AT4G27920.
DR eggNOG; ENOG502QPYH; Eukaryota.
DR HOGENOM; CLU_077517_0_1_1; -.
DR InParanoid; Q8H1R0; -.
DR OMA; DYIKMHH; -.
DR OrthoDB; 1261133at2759; -.
DR PhylomeDB; Q8H1R0; -.
DR EvolutionaryTrace; Q8H1R0; -.
DR PRO; PR:Q8H1R0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8H1R0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS: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: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 Disulfide bond; Membrane; Nucleus; Protein phosphatase inhibitor; Receptor;
KW Reference proteome.
FT CHAIN 1..183
FT /note="Abscisic acid receptor PYL10"
FT /id="PRO_0000391745"
FT REGION 20..172
FT /note="START-like"
FT MOTIF 81..85
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 111..113
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 56
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:3R6P"
FT BINDING 85..90
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 112..118
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 137
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 57
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT SITE 84
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 104
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT SITE 148
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 156
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT SITE 159
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT DISULFID 27..153
FT /note="Reversible"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:3RT2"
FT STRAND 26..37
FT /evidence="ECO:0007829|PDB:3RT2"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:3RT2"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3RT2"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:3RT2"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6NWB"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:3RT2"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:6NWC"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:3RT2"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:3RT2"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:3RT2"
FT STRAND 117..127
FT /evidence="ECO:0007829|PDB:3RT2"
FT STRAND 130..142
FT /evidence="ECO:0007829|PDB:3RT2"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6NWB"
FT HELIX 149..177
FT /evidence="ECO:0007829|PDB:3RT2"
SQ SEQUENCE 183 AA; 20642 MW; 896A016CA9D2752F CRC64;
MNGDETKKVE SEYIKKHHRH ELVESQCSST LVKHIKAPLH LVWSIVRRFD EPQKYKPFIS
RCVVQGKKLE VGSVREVDLK SGLPATKSTE VLEILDDNEH ILGIRIVGGD HRLKNYSSTI
SLHSETIDGK TGTLAIESFV VDVPEGNTKE ETCFFVEALI QCNLNSLADV TERLQAESME
KKI
