PYL12_ARATH
ID PYL12_ARATH Reviewed; 159 AA.
AC Q9FJ49;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Abscisic acid receptor PYL12;
DE AltName: Full=PYR1-like protein 12;
DE AltName: Full=Regulatory components of ABA receptor 6;
GN Name=PYL12; Synonyms=RCAR6; OrderedLocusNames=At5g45870; ORFNames=K15I22.7;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 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 [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).
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. {ECO:0000250|UniProtKB:O49686}.
CC -!- SUBUNIT: Homodimer. Binds ABA on one subunit only. Binds to CARs
CC protein in an ABA-independent manner, both at the plasma membrane and
CC in the nucleus (By similarity). Interacts with HAB1, and possibly with
CC other PP2Cs (PubMed:19407142). {ECO:0000250|UniProtKB:O49686,
CC ECO:0000269|PubMed:19407142}.
CC -!- INTERACTION:
CC Q9FJ49; P49597: ABI1; NbExp=3; IntAct=EBI-2363244, EBI-782526;
CC Q9FJ49; Q9LNW3: AIP1; NbExp=3; IntAct=EBI-2363244, EBI-1573499;
CC Q9FJ49; Q9ZW21: At2g29380; NbExp=3; IntAct=EBI-2363244, EBI-4441103;
CC Q9FJ49; Q9SAD4: ESR1; NbExp=3; IntAct=EBI-2363244, EBI-1536756;
CC Q9FJ49; Q9CAJ0: HAB1; NbExp=4; IntAct=EBI-2363244, EBI-2309302;
CC Q9FJ49; Q9LS24: NAC096; NbExp=3; IntAct=EBI-2363244, EBI-1238916;
CC Q9FJ49; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-2363244, EBI-4424877;
CC Q9FJ49; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2363244, 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB016870; BAB09315.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95309.1; -; Genomic_DNA.
DR RefSeq; NP_199399.1; NM_123955.2.
DR AlphaFoldDB; Q9FJ49; -.
DR SMR; Q9FJ49; -.
DR BioGRID; 19876; 10.
DR IntAct; Q9FJ49; 9.
DR STRING; 3702.AT5G45870.1; -.
DR PaxDb; Q9FJ49; -.
DR PRIDE; Q9FJ49; -.
DR ProteomicsDB; 226138; -.
DR EnsemblPlants; AT5G45870.1; AT5G45870.1; AT5G45870.
DR GeneID; 834627; -.
DR Gramene; AT5G45870.1; AT5G45870.1; AT5G45870.
DR KEGG; ath:AT5G45870; -.
DR Araport; AT5G45870; -.
DR TAIR; locus:2152430; AT5G45870.
DR eggNOG; ENOG502RY2P; Eukaryota.
DR HOGENOM; CLU_077517_2_0_1; -.
DR InParanoid; Q9FJ49; -.
DR OMA; QHVCGST; -.
DR OrthoDB; 1432499at2759; -.
DR PhylomeDB; Q9FJ49; -.
DR PRO; PR:Q9FJ49; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ49; 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 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Cell membrane; Cytoplasm; Membrane;
KW Nucleus; Protein phosphatase inhibitor; Receptor; Reference proteome.
FT CHAIN 1..159
FT /note="Abscisic acid receptor PYL12"
FT /id="PRO_0000391747"
FT REGION 3..153
FT /note="START-like"
FT MOTIF 64..68
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 94..96
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 39
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 68..73
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 95..101
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 118
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 67
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 87
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT SITE 129
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
SQ SEQUENCE 159 AA; 17633 MW; BEFDC3CDF077ABD0 CRC64;
MKTSQEQHVC GSTVVQTINA PLPLVWSILR RFDNPKTFKH FVKTCKLRSG DGGEGSVREV
TVVSDLPASF SLERLDELDD ESHVMVISII GGDHRLVNYQ SKTTVFVAAE EEKTVVVESY
VVDVPEGNTE EETTLFADTI VGCNLRSLAK LSEKMMELT
