PYL4_ARATH
ID PYL4_ARATH Reviewed; 207 AA.
AC O80920;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Abscisic acid receptor PYL4 {ECO:0000303|PubMed:19407142, ECO:0000303|PubMed:19624469, ECO:0000303|PubMed:19898420, ECO:0000303|PubMed:21658606, ECO:0000303|PubMed:23844015, ECO:0000303|PubMed:24563205};
DE AltName: Full=ABI1-binding protein 2 {ECO:0000303|PubMed:19874541};
DE AltName: Full=PYR1-like protein 4 {ECO:0000303|PubMed:19407142, ECO:0000303|PubMed:19624469, ECO:0000303|PubMed:19898420, ECO:0000303|PubMed:21658606, ECO:0000303|PubMed:23844015, ECO:0000303|PubMed:24563205};
DE AltName: Full=Regulatory components of ABA receptor 10;
GN Name=PYL4 {ECO:0000303|PubMed:19407142, ECO:0000303|PubMed:19624469,
GN ECO:0000303|PubMed:19898420, ECO:0000303|PubMed:21658606,
GN ECO:0000303|PubMed:23844015, ECO:0000303|PubMed:24563205};
GN Synonyms=ABIP2 {ECO:0000303|PubMed:19874541}, RCAR10;
GN OrderedLocusNames=At2g38310 {ECO:0000312|Araport:AT2G38310};
GN ORFNames=T19C21.20 {ECO:0000312|EMBL:AAC28773.1};
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=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 [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.
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 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 INTERACTION WITH HAB1, 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 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 [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 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 [12]
RP INTERACTION WITH DDA1.
RX PubMed=24563205; DOI=10.1105/tpc.113.122234;
RA Irigoyen M.L., Iniesto E., Rodriguez L., Puga M.I., Yanagawa Y., Pick E.,
RA Strickland E., Paz-Ares J., Wei N., De Jaeger G., Rodriguez P.L.,
RA Deng X.W., Rubio V.;
RT "Targeted degradation of abscisic acid receptors is mediated by the
RT ubiquitin ligase substrate adaptor DDA1 in Arabidopsis.";
RL Plant Cell 26:712-728(2014).
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 TOPP1.
RX PubMed=26943172; DOI=10.1371/journal.pgen.1005835;
RA Hou Y.J., Zhu Y., Wang P., Zhao Y., Xie S., Batelli G., Wang B., Duan C.G.,
RA Wang X., Xing L., Lei M., Yan J., Zhu X., Zhu J.K.;
RT "Type one protein phosphatase 1 and its regulatory protein inhibitor 2
RT negatively regulate ABA signaling.";
RL PLoS Genet. 12:E1005835-E1005835(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) when
CC activated by ABA (PubMed:19624469, PubMed:23844015, PubMed:21658606).
CC Can be activated by both (-)-ABA and (+)-ABA (PubMed:23844015).
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 (By similarity). Interacts with HAB1, ABI1 and ABI2, and possibly
CC with other PP2Cs (PubMed:19407142, 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 TOPP1 (PubMed:26943172). Interacts
CC with DDA1 (PubMed:24563205). Interacts with FREE1 (via N-terminus)
CC (PubMed:27495812). Interacts with the E3 ubiquitin-protein ligase RSL1
CC at the plasma membrane (PubMed:25330042).
CC {ECO:0000250|UniProtKB:O49686, ECO:0000269|PubMed:19407142,
CC ECO:0000269|PubMed:19874541, ECO:0000269|PubMed:19898420,
CC ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:24563205,
CC ECO:0000269|PubMed:25330042, ECO:0000269|PubMed:25465408,
CC ECO:0000269|PubMed:26943172, ECO:0000269|PubMed:27495812}.
CC -!- INTERACTION:
CC O80920; P49597: ABI1; NbExp=9; IntAct=EBI-2349683, EBI-782526;
CC O80920; O04719-1: ABI2; NbExp=2; IntAct=EBI-2349683, EBI-15803514;
CC O80920; Q9LNW3: AIP1; NbExp=3; IntAct=EBI-2349683, EBI-1573499;
CC O80920; Q84K72: At1g06510; NbExp=3; IntAct=EBI-2349683, EBI-4429795;
CC O80920; Q9ZW21: At2g29380; NbExp=3; IntAct=EBI-2349683, EBI-4441103;
CC O80920; Q8VZQ4: B''GAMMA; NbExp=3; IntAct=EBI-2349683, EBI-4428781;
CC O80920; Q9CAJ0: HAB1; NbExp=8; IntAct=EBI-2349683, EBI-2309302;
CC O80920; Q94F58: NAC089; NbExp=3; IntAct=EBI-2349683, EBI-2319707;
CC O80920; P49598: PP2CA; NbExp=5; IntAct=EBI-2349683, EBI-1764934;
CC O80920; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2349683, EBI-4426178;
CC O80920; Q9LMA8: TIFY10A; NbExp=3; IntAct=EBI-2349683, EBI-1388539;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. 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 (e.g. CAR1) (PubMed:25465408). Localized
CC transiently in the vacuole when in complex with RSL1 (PubMed:27495812).
CC {ECO:0000269|PubMed:25465408, 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 -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
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DR EMBL; AC004683; AAC28773.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09522.1; -; Genomic_DNA.
DR EMBL; AY039586; AAK62641.1; -; mRNA.
DR EMBL; AY054141; AAL06802.1; -; mRNA.
DR EMBL; AY087146; AAM64704.1; -; mRNA.
DR PIR; T02514; T02514.
DR RefSeq; NP_565887.1; NM_129387.3.
DR AlphaFoldDB; O80920; -.
DR SMR; O80920; -.
DR BioGRID; 3753; 19.
DR DIP; DIP-53474N; -.
DR IntAct; O80920; 16.
DR STRING; 3702.AT2G38310.1; -.
DR iPTMnet; O80920; -.
DR PaxDb; O80920; -.
DR PRIDE; O80920; -.
DR ProteomicsDB; 226011; -.
DR EnsemblPlants; AT2G38310.1; AT2G38310.1; AT2G38310.
DR GeneID; 818411; -.
DR Gramene; AT2G38310.1; AT2G38310.1; AT2G38310.
DR KEGG; ath:AT2G38310; -.
DR Araport; AT2G38310; -.
DR TAIR; locus:2057175; AT2G38310.
DR eggNOG; ENOG502QWFG; Eukaryota.
DR HOGENOM; CLU_077517_0_0_1; -.
DR InParanoid; O80920; -.
DR OMA; TLAVNFH; -.
DR OrthoDB; 1400653at2759; -.
DR PhylomeDB; O80920; -.
DR PRO; PR:O80920; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80920; baseline and differential.
DR Genevisible; O80920; AT.
DR GO; GO:0005737; C:cytoplasm; ISS: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: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; 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: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; Vacuole.
FT CHAIN 1..207
FT /note="Abscisic acid receptor PYL4"
FT /id="PRO_0000391739"
FT REGION 45..195
FT /note="START-like"
FT MOTIF 107..111
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 137..139
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 81
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 111..116
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 138..144
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 160
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 110
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 171
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 179
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT DISULFID 52..176
FT /note="Reversible"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
SQ SEQUENCE 207 AA; 22435 MW; 118160B35D7066BB CRC64;
MLAVHRPSSA VSDGDSVQIP MMIASFQKRF PSLSRDSTAA RFHTHEVGPN QCCSAVIQEI
SAPISTVWSV VRRFDNPQAY KHFLKSCSVI GGDGDNVGSL RQVHVVSGLP AASSTERLDI
LDDERHVISF SVVGGDHRLS NYRSVTTLHP SPISGTVVVE SYVVDVPPGN TKEETCDFVD
VIVRCNLQSL AKIAENTAAE SKKKMSL
