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PYL9_ARATH
ID   PYL9_ARATH              Reviewed;         187 AA.
AC   Q84MC7; Q8LA91; Q9LNI7;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Abscisic acid receptor PYL9;
DE   AltName: Full=ABI1-binding protein 4;
DE   AltName: Full=PYR1-like protein 9;
DE   AltName: Full=Regulatory components of ABA receptor 1;
GN   Name=PYL9; Synonyms=RCAR1; OrderedLocusNames=At1g01360; ORFNames=F6F3.16;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ABI1; ABI2 AND HAB1, AND
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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) IN COMPLEX WITH ABA, FUNCTION,
RP   MUTAGENESIS OF CYS-29; CYS-34; ILE-112; CYS-159 AND LEU-165, DISULFIDE
RP   BOND, INTERACTION WITH ABA, 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   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ABA, MUTAGENESIS OF
RP   CYS-29; CYS-34 AND CYS-159, AND HOMODIMER.
RX   PubMed=24645846; DOI=10.1111/gtc.12140;
RA   Nakagawa M., Kagiyama M., Shibata N., Hirano Y., Hakoshima T.;
RT   "Mechanism of high-affinity abscisic acid binding to PYL9/RCAR1.";
RL   Genes Cells 19:386-404(2014).
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) in an ABA-
CC       independent manner but more efficiently when activated by ABA. Confers
CC       enhanced sensitivity to ABA (PubMed:19407143, PubMed:23844015,
CC       PubMed:21658606). Can be activated only by (+)-ABA but not by (-)-ABA
CC       (PubMed:23844015). {ECO:0000269|PubMed:19407143,
CC       ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:23844015}.
CC   -!- SUBUNIT: Homodimer (PubMed:24645846). Monomer (PubMed:21658606). Binds
CC       ABA on one subunit only. Binds to CARs protein in an ABA-independent
CC       manner, both at the plasma membrane and in the nucleus (By similarity).
CC       Binds specifically (+)-ABA but not (-)-ABA (PubMed:23844015,
CC       PubMed:24645846). Interacts with HAB1, ABI1 and ABI2, and possibly with
CC       other PP2Cs (PubMed:19407142, PubMed:19407143, PubMed:19874541).
CC       Interacts with TOPP1 (PubMed:26943172). Interacts with DDA1
CC       (PubMed:24563205). {ECO:0000250|UniProtKB:O49686,
CC       ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19407143,
CC       ECO:0000269|PubMed:19874541, ECO:0000269|PubMed:21658606,
CC       ECO:0000269|PubMed:23844015, ECO:0000269|PubMed:24563205,
CC       ECO:0000269|PubMed:24645846, ECO:0000269|PubMed:26943172}.
CC   -!- INTERACTION:
CC       Q84MC7; P49597: ABI1; NbExp=14; IntAct=EBI-2349513, EBI-782526;
CC       Q84MC7; O04719: ABI2; NbExp=7; IntAct=EBI-2349513, EBI-537680;
CC       Q84MC7; Q9SFD5: ADA2A; NbExp=3; IntAct=EBI-2349513, EBI-979206;
CC       Q84MC7; Q9LNW3: AIP1; NbExp=9; IntAct=EBI-2349513, EBI-1573499;
CC       Q84MC7; A0A178WMH3: At1g23220; NbExp=3; IntAct=EBI-2349513, EBI-25519119;
CC       Q84MC7; A0A1P8AVS2: At1g72340; NbExp=3; IntAct=EBI-2349513, EBI-25528474;
CC       Q84MC7; Q9ZW21: At2g29380; NbExp=8; IntAct=EBI-2349513, EBI-4441103;
CC       Q84MC7; A0A384LEC9: At3g29270; NbExp=3; IntAct=EBI-2349513, EBI-25528354;
CC       Q84MC7; Q8GXD8: At4g22250/T10I14_80; NbExp=3; IntAct=EBI-2349513, EBI-4427572;
CC       Q84MC7; O82754: At4g23050; NbExp=3; IntAct=EBI-2349513, EBI-1238561;
CC       Q84MC7; A0A384L3Q5: AXX17_At3g52590; NbExp=3; IntAct=EBI-2349513, EBI-25528525;
CC       Q84MC7; Q9C7T4: BHLH96; NbExp=3; IntAct=EBI-2349513, EBI-15192637;
CC       Q84MC7; Q9SAD4: ESR1; NbExp=3; IntAct=EBI-2349513, EBI-1536756;
CC       Q84MC7; Q9LZL7: Fes1C; NbExp=3; IntAct=EBI-2349513, EBI-4431436;
CC       Q84MC7; Q9CAJ0: HAB1; NbExp=5; IntAct=EBI-2349513, EBI-2309302;
CC       Q84MC7; Q9LNP9: HAB2; NbExp=3; IntAct=EBI-2349513, EBI-15803614;
CC       Q84MC7; O81027: HMGCL; NbExp=3; IntAct=EBI-2349513, EBI-4434127;
CC       Q84MC7; Q9FGM9: HSP23.5; NbExp=3; IntAct=EBI-2349513, EBI-4428388;
CC       Q84MC7; Q9C9X7: IDD14; NbExp=3; IntAct=EBI-2349513, EBI-15191579;
CC       Q84MC7; Q9SCK1: LSU1; NbExp=3; IntAct=EBI-2349513, EBI-4424157;
CC       Q84MC7; Q9FJ07: MYB111; NbExp=3; IntAct=EBI-2349513, EBI-25528560;
CC       Q84MC7; O23160: MYB73; NbExp=7; IntAct=EBI-2349513, EBI-25506855;
CC       Q84MC7; Q9SN12: MYB77; NbExp=8; IntAct=EBI-2349513, EBI-2324225;
CC       Q84MC7; Q94F58: NAC089; NbExp=3; IntAct=EBI-2349513, EBI-2319707;
CC       Q84MC7; Q9ZVL3: NFYC3; NbExp=3; IntAct=EBI-2349513, EBI-2125961;
CC       Q84MC7; Q38845: PP2AA1; NbExp=3; IntAct=EBI-2349513, EBI-1645478;
CC       Q84MC7; Q9XI19: PTAC6; NbExp=3; IntAct=EBI-2349513, EBI-7890412;
CC       Q84MC7; O82277: TCP10; NbExp=3; IntAct=EBI-2349513, EBI-3133327;
CC       Q84MC7; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-2349513, EBI-4424877;
CC       Q84MC7; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-2349513, EBI-4426144;
CC       Q84MC7; A1YKT1: TCP18; NbExp=3; IntAct=EBI-2349513, EBI-15192731;
CC       Q84MC7; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2349513, EBI-4426178;
CC       Q84MC7; Q9FTA2: TCP21; NbExp=3; IntAct=EBI-2349513, EBI-4426168;
CC       Q84MC7; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-2349513, EBI-25522447;
CC       Q84MC7; O64647: TCP9; NbExp=3; IntAct=EBI-2349513, EBI-9838721;
CC       Q84MC7; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-2349513, EBI-4426557;
CC       Q84MC7; Q9LVG2: TOE2; NbExp=3; IntAct=EBI-2349513, EBI-4424568;
CC       Q84MC7; Q8W4L5: VAL1; NbExp=3; IntAct=EBI-2349513, EBI-2616403;
CC       Q84MC7; Q8GXA4: WIP1; NbExp=3; IntAct=EBI-2349513, EBI-1779367;
CC       Q84MC7; Q9SCU5: WNK5; NbExp=3; IntAct=EBI-2349513, EBI-1807651;
CC       Q84MC7; Q93WT0: WRKY31; NbExp=3; IntAct=EBI-2349513, EBI-15208488;
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   -!- TISSUE SPECIFICITY: Expressed in root tips, vascular tissues, stomata,
CC       flowers, pollen tubes and developing seeds.
CC       {ECO:0000269|PubMed:19407143}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAF97339.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAM65514.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC023628; AAF97339.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE27277.1; -; Genomic_DNA.
DR   EMBL; BT006399; AAP21207.1; -; mRNA.
DR   EMBL; AK227623; BAE99614.1; -; mRNA.
DR   EMBL; AY087967; AAM65514.1; ALT_INIT; mRNA.
DR   RefSeq; NP_563626.1; NM_100018.5.
DR   PDB; 3OQU; X-ray; 2.68 A; A/B=1-187.
DR   PDB; 3W9R; X-ray; 1.90 A; A=1-187.
DR   PDBsum; 3OQU; -.
DR   PDBsum; 3W9R; -.
DR   AlphaFoldDB; Q84MC7; -.
DR   SMR; Q84MC7; -.
DR   BioGRID; 23691; 45.
DR   DIP; DIP-53480N; -.
DR   IntAct; Q84MC7; 44.
DR   STRING; 3702.AT1G01360.1; -.
DR   PaxDb; Q84MC7; -.
DR   PRIDE; Q84MC7; -.
DR   ProteomicsDB; 226014; -.
DR   EnsemblPlants; AT1G01360.1; AT1G01360.1; AT1G01360.
DR   GeneID; 838452; -.
DR   Gramene; AT1G01360.1; AT1G01360.1; AT1G01360.
DR   KEGG; ath:AT1G01360; -.
DR   Araport; AT1G01360; -.
DR   TAIR; locus:2035227; AT1G01360.
DR   eggNOG; ENOG502QPYH; Eukaryota.
DR   HOGENOM; CLU_077517_0_0_1; -.
DR   InParanoid; Q84MC7; -.
DR   OMA; HIKAPLR; -.
DR   OrthoDB; 1261133at2759; -.
DR   PhylomeDB; Q84MC7; -.
DR   PRO; PR:Q84MC7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q84MC7; baseline and differential.
DR   Genevisible; Q84MC7; AT.
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; IDA: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: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   DisProt; DP02995; -.
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; Cell membrane; Cytoplasm;
KW   Disulfide bond; Membrane; Nucleus; Protein phosphatase inhibitor; Receptor;
KW   Reference proteome.
FT   CHAIN           1..187
FT                   /note="Abscisic acid receptor PYL9"
FT                   /id="PRO_0000391744"
FT   REGION          27..178
FT                   /note="START-like"
FT   MOTIF           87..91
FT                   /note="Gate loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT   MOTIF           117..119
FT                   /note="Latch loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT   BINDING         63
FT                   /ligand="abscisate"
FT                   /ligand_id="ChEBI:CHEBI:62432"
FT                   /evidence="ECO:0000269|PubMed:23844015,
FT                   ECO:0000269|PubMed:24645846, ECO:0007744|PDB:3OQU,
FT                   ECO:0007744|PDB:3W9R"
FT   BINDING         91..96
FT                   /ligand="abscisate"
FT                   /ligand_id="ChEBI:CHEBI:62432"
FT                   /evidence="ECO:0000250|UniProtKB:O49686"
FT   BINDING         118..124
FT                   /ligand="abscisate"
FT                   /ligand_id="ChEBI:CHEBI:62432"
FT                   /evidence="ECO:0000250|UniProtKB:O49686"
FT   BINDING         143
FT                   /ligand="abscisate"
FT                   /ligand_id="ChEBI:CHEBI:62432"
FT                   /evidence="ECO:0000250|UniProtKB:O49686"
FT   SITE            64
FT                   /note="Involved in ABA binding"
FT                   /evidence="ECO:0000269|PubMed:24645846"
FT   SITE            90
FT                   /note="Involved in interactions with PP2Cs"
FT                   /evidence="ECO:0000250|UniProtKB:O49686"
FT   SITE            110
FT                   /note="Involved in ABA binding"
FT                   /evidence="ECO:0000269|PubMed:24645846"
FT   SITE            154
FT                   /note="Involved in interactions with PP2Cs"
FT                   /evidence="ECO:0000250|UniProtKB:O49686"
FT   SITE            162
FT                   /note="Involved in ABA binding"
FT                   /evidence="ECO:0000269|PubMed:24645846"
FT   SITE            165
FT                   /note="Involved in ABA binding"
FT                   /evidence="ECO:0000269|PubMed:24645846"
FT   DISULFID        29..159
FT                   /note="Reversible"
FT                   /evidence="ECO:0000269|PubMed:23844015"
FT   DISULFID        34..159
FT                   /note="Reversible"
FT                   /evidence="ECO:0000269|PubMed:23844015"
FT   MUTAGEN         29
FT                   /note="C->S: Stable homogeneity in reducing condition."
FT                   /evidence="ECO:0000269|PubMed:23844015,
FT                   ECO:0000269|PubMed:24645846"
FT   MUTAGEN         34
FT                   /note="C->S: Stable homogeneity in reducing condition."
FT                   /evidence="ECO:0000269|PubMed:23844015,
FT                   ECO:0000269|PubMed:24645846"
FT   MUTAGEN         112
FT                   /note="I->V: Increased HAB1 inhibitory ability."
FT                   /evidence="ECO:0000269|PubMed:23844015"
FT   MUTAGEN         159
FT                   /note="C->S: Abnormal stable homogeneity in reducing
FT                   condition."
FT                   /evidence="ECO:0000269|PubMed:23844015,
FT                   ECO:0000269|PubMed:24645846"
FT   MUTAGEN         165
FT                   /note="L->V: Slight potentiation of (-)-ABA-binding."
FT                   /evidence="ECO:0000269|PubMed:23844015"
FT   CONFLICT        7
FT                   /note="G -> D (in Ref. 1; AAM65514)"
FT                   /evidence="ECO:0000305"
FT   HELIX           14..28
FT                   /evidence="ECO:0007829|PDB:3W9R"
FT   STRAND          33..44
FT                   /evidence="ECO:0007829|PDB:3W9R"
FT   HELIX           46..53
FT                   /evidence="ECO:0007829|PDB:3W9R"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:3W9R"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:3W9R"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:3W9R"
FT   STRAND          92..102
FT                   /evidence="ECO:0007829|PDB:3W9R"
FT   TURN            103..106
FT                   /evidence="ECO:0007829|PDB:3W9R"
FT   STRAND          107..118
FT                   /evidence="ECO:0007829|PDB:3W9R"
FT   STRAND          123..133
FT                   /evidence="ECO:0007829|PDB:3W9R"
FT   STRAND          136..148
FT                   /evidence="ECO:0007829|PDB:3W9R"
FT   HELIX           155..181
FT                   /evidence="ECO:0007829|PDB:3W9R"
SQ   SEQUENCE   187 AA;  20901 MW;  070D485311163568 CRC64;
     MMDGVEGGTA MYGGLETVQY VRTHHQHLCR ENQCTSALVK HIKAPLHLVW SLVRRFDQPQ
     KYKPFVSRCT VIGDPEIGSL REVNVKSGLP ATTSTERLEL LDDEEHILGI KIIGGDHRLK
     NYSSILTVHP EIIEGRAGTM VIESFVVDVP QGNTKDETCY FVEALIRCNL KSLADVSERL
     ASQDITQ
 
 
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