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PYL9_ORYSJ
ID   PYL9_ORYSJ              Reviewed;         207 AA.
AC   Q5Z8S0;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Abscisic acid receptor PYL9 {ECO:0000305};
DE   AltName: Full=PYR1-like protein 2 {ECO:0000303|PubMed:24743650};
DE            Short=OsPYL2 {ECO:0000303|PubMed:24743650};
DE   AltName: Full=PYR1-like protein 9 {ECO:0000303|PubMed:26362328};
DE            Short=OsPYL9 {ECO:0000303|PubMed:26362328};
DE   AltName: Full=Regulatory components of ABA receptor 9 {ECO:0000305};
GN   Name=PYL9 {ECO:0000303|PubMed:26362328};
GN   Synonyms=PYL2 {ECO:0000303|PubMed:24743650},
GN   RCAR9 {ECO:0000303|PubMed:26362328};
GN   OrderedLocusNames=Os06g0562200 {ECO:0000312|EMBL:BAF19788.1},
GN   LOC_Os06g36670 {ECO:0000305};
GN   ORFNames=P0456F09.29 {ECO:0000312|EMBL:BAD53834.1},
GN   P0656E03.2 {ECO:0000312|EMBL:BAD53743.1};
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=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   [2]
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   [3]
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   [4]
RP   FUNCTION, INTERACTION WITH PP2C30 AND PP2C53, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
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   [5]
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).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ABSCISIC ACID,
RP   FUNCTION, INTERACTION WITH PP2C06, AND HOMODIMERIZATION.
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).
CC   -!- FUNCTION: Involved in abscisic acid (ABA) signaling during seed
CC       germination and abiotic stress response. Acts as positive regulator of
CC       ABA-mediated inhibition of seed germination, and tolerance to drought
CC       and cold stresses (PubMed:26362328). Inhibits the activity of the
CC       protein phosphatases PP2C06 and PP2C09 when activated by abscisic acid
CC       (ABA) (PubMed:24743650). {ECO:0000269|PubMed:24743650,
CC       ECO:0000269|PubMed:26362328}.
CC   -!- SUBUNIT: Homodimer. Interacts with PP2C06 (PubMed:24743650). Interacts
CC       with PP2C50. Binding to PP2C50 is dependent on the presence of abscisic
CC       acid (ABA) (PubMed:28827170). Interacts with PP2C30 and PP2C53. Binding
CC       to PP2C30 and PP2C53 is dependent on the presence of ABA
CC       (PubMed:26362328). {ECO:0000269|PubMed:24743650,
CC       ECO:0000269|PubMed:26362328, ECO:0000269|PubMed:28827170}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26362328}.
CC       Nucleus {ECO:0000269|PubMed:26362328}.
CC   -!- INDUCTION: Repressed by abscisic acid (ABA).
CC       {ECO:0000269|PubMed:26362328}.
CC   -!- MISCELLANEOUS: Plants overexpressing PYL9 exhibit abscisic acid (ABA)
CC       hypersensitive phenotype during seed germination. Plants overexpressing
CC       PYL9 exhibit tolerance to cold and drought stresses.
CC       {ECO:0000269|PubMed:26362328}.
CC   -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC       receptor family. {ECO:0000305}.
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DR   EMBL; AP003714; BAD53743.1; -; Genomic_DNA.
DR   EMBL; AP003762; BAD53834.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF19788.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS98256.1; -; Genomic_DNA.
DR   RefSeq; XP_015641755.1; XM_015786269.1.
DR   PDB; 4OIC; X-ray; 2.00 A; A=1-207.
DR   PDBsum; 4OIC; -.
DR   AlphaFoldDB; Q5Z8S0; -.
DR   SMR; Q5Z8S0; -.
DR   STRING; 4530.OS06T0562200-01; -.
DR   PaxDb; Q5Z8S0; -.
DR   PRIDE; Q5Z8S0; -.
DR   EnsemblPlants; Os06t0562200-01; Os06t0562200-01; Os06g0562200.
DR   GeneID; 4341308; -.
DR   Gramene; Os06t0562200-01; Os06t0562200-01; Os06g0562200.
DR   KEGG; osa:4341308; -.
DR   eggNOG; ENOG502QU62; Eukaryota.
DR   HOGENOM; CLU_077517_0_1_1; -.
DR   InParanoid; Q5Z8S0; -.
DR   OMA; ESTINTH; -.
DR   OrthoDB; 1267148at2759; -.
DR   PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
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; IDA:UniProtKB.
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; IMP: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   GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR   GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR   GO; GO:0009845; P:seed germination; IMP:UniProtKB.
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; Cytoplasm; Nucleus;
KW   Protein phosphatase inhibitor; Receptor; Reference proteome;
KW   Stress response.
FT   CHAIN           1..207
FT                   /note="Abscisic acid receptor PYL9"
FT                   /id="PRO_0000444341"
FT   REGION          31..197
FT                   /note="START-like"
FT                   /evidence="ECO:0000250|UniProtKB:Q8H1R0"
FT   MOTIF           100..104
FT                   /note="Gate loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT   MOTIF           130..132
FT                   /note="Latch loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT   BINDING         74
FT                   /ligand="abscisate"
FT                   /ligand_id="ChEBI:CHEBI:62432"
FT                   /evidence="ECO:0000269|PubMed:24743650,
FT                   ECO:0007744|PDB:4OIC"
FT   BINDING         104..109
FT                   /ligand="abscisate"
FT                   /ligand_id="ChEBI:CHEBI:62432"
FT                   /evidence="ECO:0000250|UniProtKB:O49686"
FT   BINDING         131..137
FT                   /ligand="abscisate"
FT                   /ligand_id="ChEBI:CHEBI:62432"
FT                   /evidence="ECO:0000250|UniProtKB:O49686"
FT   BINDING         162
FT                   /ligand="abscisate"
FT                   /ligand_id="ChEBI:CHEBI:62432"
FT                   /evidence="ECO:0000250|UniProtKB:O49686"
FT   SITE            103
FT                   /note="Involved in interactions with PP2Cs"
FT                   /evidence="ECO:0000250|UniProtKB:O49686"
FT   SITE            173
FT                   /note="Involved in interactions with PP2Cs"
FT                   /evidence="ECO:0000250|UniProtKB:O49686"
FT   HELIX           5..11
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   HELIX           15..20
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   HELIX           22..28
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   STRAND          44..55
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   HELIX           57..65
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   STRAND          77..85
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   STRAND          93..98
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   STRAND          105..115
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   TURN            116..119
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   STRAND          120..127
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   STRAND          129..131
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   STRAND          136..144
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   STRAND          157..167
FT                   /evidence="ECO:0007829|PDB:4OIC"
FT   HELIX           174..198
FT                   /evidence="ECO:0007829|PDB:4OIC"
SQ   SEQUENCE   207 AA;  22333 MW;  31E357633F50CD76 CRC64;
     MEAHVERALR EGLTEEERAA LEPAVMAHHT FPPSTTTATT AAATCTSLVT QRVAAPVRAV
     WPIVRSFGNP QRYKHFVRTC ALAAGDGASV GSVREVTVVS GLPASTSTER LEMLDDDRHI
     ISFRVVGGQH RLRNYRSVTS VTEFQPPAAG PGPAPPYCVV VESYVVDVPD GNTAEDTRMF
     TDTVVKLNLQ MLAAVAEDSS SASRRRD
 
 
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