PYL10_ORYSJ
ID PYL10_ORYSJ Reviewed; 212 AA.
AC Q7XBY6; Q9AYL5;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Abscisic acid receptor PYL10 {ECO:0000305};
DE AltName: Full=PYR1-like protein 1 {ECO:0000303|PubMed:24743650};
DE Short=OsPYL1 {ECO:0000303|PubMed:24743650};
DE AltName: Full=PYR1-like protein 10 {ECO:0000303|PubMed:26362328};
DE Short=OsPYL10 {ECO:0000303|PubMed:26362328};
DE AltName: Full=Regulatory components of ABA receptor 10 {ECO:0000305};
GN Name=PYL10 {ECO:0000303|PubMed:26362328};
GN Synonyms=PYL1 {ECO:0000303|PubMed:24743650},
GN RCAR10 {ECO:0000303|PubMed:26362328};
GN OrderedLocusNames=Os10g0573400 {ECO:0000312|EMBL:BAF27307.1},
GN LOC_Os10g42280 {ECO:0000312|EMBL:AAP55122.1};
GN ORFNames=OsJ_32555 {ECO:0000312|EMBL:EAZ17061.1},
GN OSJNBa0003O19.2 {ECO:0000312|EMBL:AAK00445.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=24743650; DOI=10.1371/journal.pone.0095246;
RA He Y., Hao Q., Li W., Yan C., Yan N., Yin P.;
RT "Identification and characterization of ABA receptors in Oryza sativa.";
RL PLoS ONE 9:E95246-E95246(2014).
RN [7]
RP FUNCTION, INTERACTION WITH PP2C53, AND SUBCELLULAR LOCATION.
RX PubMed=26491145; DOI=10.1093/pcp/pcv154;
RA Li C., Shen H., Wang T., Wang X.;
RT "ABA regulates subcellular redistribution of OsABI-LIKE2, a negative
RT regulator in ABA signaling, to control root architecture and drought
RT resistance in Oryza sativa.";
RL Plant Cell Physiol. 56:2396-2408(2015).
RN [8]
RP INTERACTION WITH PP2C53, AND SUBCELLULAR LOCATION.
RX PubMed=26362328; DOI=10.1186/s12284-015-0061-6;
RA Tian X., Wang Z., Li X., Lv T., Liu H., Wang L., Niu H., Bu Q.;
RT "Characterization and functional analysis of pyrabactin resistance-like
RT abscisic acid receptor family in rice.";
RL Rice 8:28-28(2015).
RN [9]
RP INTERACTION WITH PP2C50.
RX PubMed=28827170; DOI=10.1016/j.molp.2017.08.003;
RA Han S., Min M.K., Lee S.Y., Lim C.W., Bhatnagar N., Lee Y., Shin D.,
RA Chung K.Y., Lee S.C., Kim B.G., Lee S.;
RT "Modulation of ABA signaling by altering VxGL motif of PP2Cs in Oryza
RT sativa.";
RL Mol. Plant 10:1190-1205(2017).
CC -!- FUNCTION: Inhibits the protein phosphatases PP2C06 and PP2C09 when
CC activated by abscisic acid (ABA) (PubMed:24743650). Together with
CC PP2C53, SAPK8 and SAPK10, may form an ABA signaling module involved in
CC stress response (PubMed:26491145). {ECO:0000269|PubMed:24743650,
CC ECO:0000269|PubMed:26491145}.
CC -!- SUBUNIT: Homodimer (PubMed:24743650). Interacts with PP2C53. Binding to
CC PP2C53 is dependent on the presence of abscisic acid (ABA)
CC (PubMed:26491145, PubMed:26362328). Interacts with PP2C50. Binding to
CC PP2C50 is dependent on the presence of ABA (PubMed:28827170).
CC {ECO:0000269|PubMed:24743650, ECO:0000269|PubMed:26362328,
CC ECO:0000269|PubMed:26491145, ECO:0000269|PubMed:28827170}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26362328,
CC ECO:0000269|PubMed:26491145}. Nucleus {ECO:0000269|PubMed:26362328,
CC ECO:0000269|PubMed:26491145}.
CC -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
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DR EMBL; AC060755; AAK00445.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP55122.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF27307.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT12177.1; -; Genomic_DNA.
DR EMBL; CM000147; EAZ17061.1; -; Genomic_DNA.
DR RefSeq; XP_015612857.1; XM_015757371.1.
DR AlphaFoldDB; Q7XBY6; -.
DR SMR; Q7XBY6; -.
DR STRING; 4530.OS10T0573400-01; -.
DR PaxDb; Q7XBY6; -.
DR PRIDE; Q7XBY6; -.
DR EnsemblPlants; Os10t0573400-01; Os10t0573400-01; Os10g0573400.
DR GeneID; 4349472; -.
DR Gramene; Os10t0573400-01; Os10t0573400-01; Os10g0573400.
DR KEGG; osa:4349472; -.
DR eggNOG; ENOG502QW1M; Eukaryota.
DR HOGENOM; CLU_077517_0_1_1; -.
DR InParanoid; Q7XBY6; -.
DR OMA; FHSYRIN; -.
DR OrthoDB; 1238726at2759; -.
DR PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0010427; F:abscisic acid binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; 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; Cytoplasm; Nucleus;
KW Protein phosphatase inhibitor; Receptor; Reference proteome;
KW Stress response.
FT CHAIN 1..212
FT /note="Abscisic acid receptor PYL10"
FT /id="PRO_0000444342"
FT REGION 34..191
FT /note="START-like"
FT /evidence="ECO:0000250|UniProtKB:Q8H1R0"
FT MOTIF 103..107
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 133..135
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 70
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:Q8H1R0"
FT BINDING 107..112
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 134..140
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 156
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 106
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 167
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
SQ SEQUENCE 212 AA; 23084 MW; BBA1D03553465083 CRC64;
MEQQEEVPPP PAGLGLTAEE YAQVRATVEA HHRYAVGPGQ CSSLLAQRIH APPAAVWAVV
RRFDCPQVYK HFIRSCVLRP DPHHDDNGND LRPGRLREVS VISGLPASTS TERLDLLDDA
HRVFGFTITG GEHRLRNYRS VTTVSQLDEI CTLVLESYIV DVPDGNTEDD TRLFADTVIR
LNLQKLKSVS EANANAAAAA AAPPPPPPAA AE
