PYL13_ARATH
ID PYL13_ARATH Reviewed; 164 AA.
AC Q9SN51;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Abscisic acid receptor PYL13;
DE AltName: Full=PYR1-like protein 13;
DE AltName: Full=Regulatory components of ABA receptor 7;
GN Name=PYL13; Synonyms=RCAR7; OrderedLocusNames=At4g18620;
GN ORFNames=F28A21.30;
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 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 [4]
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 [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH PP2CA, FUNCTION,
RP INTERACTION WITH PYL10; PP2CA; ABI1; HAB1 AND HAB2, AND MUTAGENESIS OF
RP GLN-38 AND PHE-71.
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).
CC -!- FUNCTION: Receptor for abscisic acid (ABA) required for ABA-mediated
CC responses such as stomatal closure and germination inhibition (By
CC similarity). Inhibits the activity of group-A protein phosphatases type
CC 2C (PP2Cs), selectively PP2CA, in an ABA-independent manner
CC (PubMed:24165892). {ECO:0000250|UniProtKB:O49686,
CC ECO:0000269|PubMed:24165892}.
CC -!- SUBUNIT: Forms heterodimer with PYL10, thus antagonizing PP2Cs-binding
CC and ABA-independent inhibition of PP2Cs (PubMed:24165892). Homodimer.
CC Binds ABA on one subunit only. Binds to CARs protein in an ABA-
CC independent manner, both at the plasma membrane and in the nucleus (By
CC similarity). Interacts with PP2Cs such as PP2CA, ABI1, HAB1 AND HAB2
CC (PubMed:24165892). {ECO:0000250|UniProtKB:O49686,
CC ECO:0000269|PubMed:24165892}.
CC -!- INTERACTION:
CC Q9SN51; P49597: ABI1; NbExp=3; IntAct=EBI-25515027, EBI-782526;
CC Q9SN51; Q9LNW3: AIP1; NbExp=7; IntAct=EBI-25515027, EBI-1573499;
CC Q9SN51; Q9ZW21: At2g29380; NbExp=3; IntAct=EBI-25515027, EBI-4441103;
CC Q9SN51; Q9LT89: TCP19; NbExp=3; IntAct=EBI-25515027, 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}.
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DR EMBL; AL035526; CAB37447.1; -; Genomic_DNA.
DR EMBL; AL161549; CAB78864.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84069.1; -; Genomic_DNA.
DR PIR; T04854; T04854.
DR RefSeq; NP_193597.1; NM_117978.1.
DR PDB; 4N0G; X-ray; 2.38 A; C/D=1-164.
DR PDBsum; 4N0G; -.
DR AlphaFoldDB; Q9SN51; -.
DR SMR; Q9SN51; -.
DR BioGRID; 12889; 24.
DR IntAct; Q9SN51; 4.
DR STRING; 3702.AT4G18620.1; -.
DR PaxDb; Q9SN51; -.
DR PRIDE; Q9SN51; -.
DR EnsemblPlants; AT4G18620.1; AT4G18620.1; AT4G18620.
DR GeneID; 827596; -.
DR Gramene; AT4G18620.1; AT4G18620.1; AT4G18620.
DR KEGG; ath:AT4G18620; -.
DR Araport; AT4G18620; -.
DR TAIR; locus:2124077; AT4G18620.
DR eggNOG; ENOG502RY2P; Eukaryota.
DR HOGENOM; CLU_077517_2_0_1; -.
DR InParanoid; Q9SN51; -.
DR OMA; TDNILRW; -.
DR OrthoDB; 1432499at2759; -.
DR PhylomeDB; Q9SN51; -.
DR PRO; PR:Q9SN51; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SN51; 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; 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 2: Evidence at transcript level;
KW 3D-structure; Abscisic acid signaling pathway; Cell membrane; Cytoplasm;
KW Membrane; Nucleus; Protein phosphatase inhibitor; Receptor;
KW Reference proteome.
FT CHAIN 1..164
FT /note="Abscisic acid receptor PYL13"
FT /id="PRO_0000391748"
FT REGION 3..160
FT /note="START-like"
FT MOTIF 69..73
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 99..101
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 73..78
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 100..106
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 125
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 72
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 136
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 144
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT MUTAGEN 38
FT /note="Q->K: Becomes an ABA-dependent inhibitor of PP2Cs,
FT including PP2CA, ABI1, HAB1, and HAB2; when associated with
FT L-71."
FT /evidence="ECO:0000269|PubMed:24165892"
FT MUTAGEN 71
FT /note="F->L: Becomes an ABA-dependent inhibitor of PP2Cs,
FT including PP2CA, ABI1, HAB1, and HAB2; when associated with
FT K-38."
FT /evidence="ECO:0000269|PubMed:24165892"
FT STRAND 8..19
FT /evidence="ECO:0007829|PDB:4N0G"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:4N0G"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 74..84
FT /evidence="ECO:0007829|PDB:4N0G"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 89..100
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:4N0G"
FT HELIX 137..162
FT /evidence="ECO:0007829|PDB:4N0G"
SQ SEQUENCE 164 AA; 18127 MW; 542A3563899E9E28 CRC64;
MESSKQKRCR SSVVETIEAP LPLVWSILRS FDKPQAYQRF VKSCTMRSGG GGGKGGEGKG
SVRDVTLVSG FPADFSTERL EELDDESHVM VVSIIGGNHR LVNYKSKTKV VASPEDMAKK
TVVVESYVVD VPEGTSEEDT IFFVDNIIRY NLTSLAKLTK KMMK
