Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein phosphatase 2C 16 (AtPP2C16) (EC 3.1.3.16) (AtP2C-HA) (Protein HYPERSENSITIVE TO ABA 1) (Protein phosphatase 2C HAB1) (PP2C HAB1)

 P2C16_ARATH             Reviewed;         511 AA.
Q9CAJ0; C0Z251; O81709; Q0WLM7;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 123.
RecName: Full=Protein phosphatase 2C 16;
Short=AtPP2C16;
EC=3.1.3.16;
AltName: Full=AtP2C-HA;
AltName: Full=Protein HYPERSENSITIVE TO ABA 1;
AltName: Full=Protein phosphatase 2C HAB1;
Short=PP2C HAB1;
Flags: Precursor;
Name=HAB1; Synonyms=P2C-HA; OrderedLocusNames=At1g72770;
ORFNames=F28P22.4;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
INDUCTION BY ABA.
STRAIN=cv. Landsberg erecta;
PubMed=9862504; DOI=10.1023/A:1006012218704;
Rodriguez P.L., Leube M.P., Grill E.;
"Molecular cloning in Arabidopsis thaliana of a new protein
phosphatase 2C (PP2C) with homology to ABI1 and ABI2.";
Plant Mol. Biol. 38:879-883(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-511 (ISOFORM 1).
TISSUE=Rosette leaf;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[7]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY ABA.
PubMed=14731256; DOI=10.1046/j.1365-313X.2003.01966.x;
Saez A., Apostolova N., Gonzalez-Guzman M., Gonzalez-Garcia M.P.,
Nicolas C., Lorenzo O., Rodriguez P.L.;
"Gain-of-function and loss-of-function phenotypes of the protein
phosphatase 2C HAB1 reveal its role as a negative regulator of
abscisic acid signalling.";
Plant J. 37:354-369(2004).
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15130549; DOI=10.1016/j.tplants.2004.03.007;
Schweighofer A., Hirt H., Meskiene I.;
"Plant PP2C phosphatases: emerging functions in stress signaling.";
Trends Plant Sci. 9:236-243(2004).
[9]
FUNCTION, AND MUTAGENESIS OF GLY-246.
PubMed=16876791; DOI=10.1016/j.febslet.2006.07.047;
Robert N., Merlot S., N'guyen V., Boisson-Dernier A., Schroeder J.I.;
"A hypermorphic mutation in the protein phosphatase 2C HAB1 strongly
affects ABA signaling in Arabidopsis.";
FEBS Lett. 580:4691-4696(2006).
[10]
INDUCTION BY ABA, AND TISSUE SPECIFICITY.
PubMed=16339800; DOI=10.1104/pp.105.070128;
Yoshida T., Nishimura N., Kitahata N., Kuromori T., Ito T., Asami T.,
Shinozaki K., Hirayama T.;
"ABA-hypersensitive germination3 encodes a protein phosphatase 2C
(AtPP2CA) that strongly regulates abscisic acid signaling during
germination among Arabidopsis protein phosphatase 2Cs.";
Plant Physiol. 140:115-126(2006).
[11]
FUNCTION.
PubMed=16798945; DOI=10.1104/pp.106.081018;
Saez A., Robert N., Maktabi M.H., Schroeder J.I., Serrano R.,
Rodriguez P.L.;
"Enhancement of abscisic acid sensitivity and reduction of water
consumption in Arabidopsis by combined inactivation of the protein
phosphatases type 2C ABI1 and HAB1.";
Plant Physiol. 141:1389-1399(2006).
[12]
GENE FAMILY, AND NOMENCLATURE.
PubMed=19021904; DOI=10.1186/1471-2164-9-550;
Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C.,
Zhong Y.;
"Genome-wide and expression analysis of protein phosphatase 2C in rice
and Arabidopsis.";
BMC Genomics 9:550-550(2008).
[13]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SWI3B, AND
MUTAGENESIS OF GLY-246.
PubMed=19033529; DOI=10.1105/tpc.107.056705;
Saez A., Rodrigues A., Santiago J., Rubio S., Rodriguez P.L.;
"HAB1-SWI3B interaction reveals a link between abscisic acid signaling
and putative SWI/SNF chromatin-remodeling complexes in Arabidopsis.";
Plant Cell 20:2972-2988(2008).
[14]
INDUCTION BY MYB44.
PubMed=18162593; DOI=10.1104/pp.107.110981;
Jung C., Seo J.S., Han S.W., Koo Y.J., Kim C.H., Song S.I., Nahm B.H.,
Choi Y.D., Cheong J.-J.;
"Overexpression of AtMYB44 enhances stomatal closure to confer abiotic
stress tolerance in transgenic Arabidopsis.";
Plant Physiol. 146:623-635(2008).
[15]
INTERACTION WITH PYL5; PYL6 AND PYL8, AND MUTAGENESIS OF GLY-246.
PubMed=19624469; DOI=10.1111/j.1365-313X.2009.03981.x;
Santiago J., Rodrigues A., Saez A., Rubio S., Antoni R., Dupeux F.,
Park S.-Y., Marquez J.A., Cutler S.R., Rodriguez P.L.;
"Modulation of drought resistance by the abscisic acid receptor PYL5
through inhibition of clade A PP2Cs.";
Plant J. 60:575-588(2009).
[16]
INTERACTION WITH PYL9/RCAR1.
PubMed=19407143; DOI=10.1126/science.1172408;
Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A.,
Grill E.;
"Regulators of PP2C phosphatase activity function as abscisic acid
sensors.";
Science 324:1064-1068(2009).
[17]
INTERACTION WITH PYR1; PYL1; PYL2; PYL3 AND PYL4, AND ENZYME
REGULATION.
PubMed=19407142; DOI=10.1126/science.1173041;
Park S.-Y., Fung P., Nishimura N., Jensen D.R., Fujii H., Zhao Y.,
Lumba S., Santiago J., Rodrigues A., Chow T.F., Alfred S.E.,
Bonetta D., Finkelstein R., Provart N.J., Desveaux D., Rodriguez P.L.,
McCourt P., Zhu J.-K., Schroeder J.I., Volkman B.F., Cutler S.R.;
"Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL
family of START proteins.";
Science 324:1068-1071(2009).
[18]
INTERACTION WITH PYL13.
PubMed=24165892; DOI=10.1038/cr.2013.143;
Li W., Wang L., Sheng X., Yan C., Zhou R., Hang J., Yin P., Yan N.;
"Molecular basis for the selective and ABA-independent inhibition of
PP2CA by PYL13.";
Cell Res. 23:1369-1379(2013).
[19]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 186-506 IN COMPLEX WITH
MAGNESIUM; ABSCISIC ACID AND PYL2, INTERACTION WITH PYR1; PYL1; PYL2;
PYL3; PYL4; PYL5 AND PYL6, AND LOCK SITE.
PubMed=19898420; DOI=10.1038/nature08613;
Melcher K., Ng L.-M., Zhou X.E., Soon F.-F., Xu Y., Suino-Powell K.M.,
Park S.-Y., Weiner J.J., Fujii H., Chinnusamy V., Kovach A., Li J.,
Wang Y., Li J., Peterson F.C., Jensen D.R., Yong E.-L., Volkman B.F.,
Cutler S.R., Zhu J.-K., Xu H.E.;
"A gate-latch-lock mechanism for hormone signalling by abscisic acid
receptors.";
Nature 462:602-608(2009).
[20]
X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 172-511 IN COMPLEX WITH
MAGNESIUM, AND INTERACTION WITH PYL10.
PubMed=21658606; DOI=10.1016/j.molcel.2011.05.011;
Hao Q., Yin P., Li W., Wang L., Yan C., Lin Z., Wu J.Z., Wang J.,
Yan S.F., Yan N.;
"The molecular basis of ABA-independent inhibition of PP2Cs by a
subclass of PYL proteins.";
Mol. Cell 42:662-672(2011).
-!- FUNCTION: Key component and repressor of the abscisic acid (ABA)
signaling pathway that regulates numerous ABA responses, such as
stomatal closure, seed germination and inhibition of vegetative
growth. Confers enhanced sensitivity to drought.
{ECO:0000269|PubMed:14731256, ECO:0000269|PubMed:16798945,
ECO:0000269|PubMed:16876791, ECO:0000269|PubMed:19033529}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:19898420,
ECO:0000269|PubMed:21658606};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000250};
-!- ENZYME REGULATION: Repressed by PYR/PYL/RCAR ABA receptors in an
ABA-dependent manner. {ECO:0000269|PubMed:19407142}.
-!- SUBUNIT: Interacts with SWI3B (via N-terminus). Interacts with
ABA-bounded PYR1, PYL1, PYL2, PYL3, PYL4, PYL5, PYL6, PYL8 and
PYL9, and with free PYL2, PYL3, PYL4, PYL10 and PYL13.
{ECO:0000269|PubMed:19033529, ECO:0000269|PubMed:19407142,
ECO:0000269|PubMed:19407143, ECO:0000269|PubMed:19624469,
ECO:0000269|PubMed:19898420, ECO:0000269|PubMed:21658606,
ECO:0000269|PubMed:24165892}.
-!- INTERACTION:
Q8VZS8:PYL1; NbExp=4; IntAct=EBI-2309302, EBI-2363104;
O80992:PYL2; NbExp=7; IntAct=EBI-2309302, EBI-2363125;
Q9SSM7:PYL3; NbExp=7; IntAct=EBI-2309302, EBI-2363144;
O80920:PYL4; NbExp=5; IntAct=EBI-2309302, EBI-2349683;
Q9FLB1:PYL5; NbExp=8; IntAct=EBI-2309302, EBI-2363181;
Q8S8E3:PYL6; NbExp=6; IntAct=EBI-2309302, EBI-2363192;
Q9FGM1:PYL8; NbExp=3; IntAct=EBI-2309302, EBI-2429535;
O49686:PYR1; NbExp=14; IntAct=EBI-2309302, EBI-2349590;
Q39192:SRK2D; NbExp=2; IntAct=EBI-2309302, EBI-2363308;
Q940H6:SRK2E; NbExp=5; IntAct=EBI-2309302, EBI-782514;
Q39193:SRK2I; NbExp=2; IntAct=EBI-2309302, EBI-2620383;
Q84JG2:SWI3B; NbExp=4; IntAct=EBI-2309302, EBI-1102271;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19033529}.
Nucleus {ECO:0000269|PubMed:19033529}. Note=Mainly cytoplasmic.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9CAJ0-1; Sequence=Displayed;
Name=2;
IsoId=Q9CAJ0-2; Sequence=VSP_034844, VSP_034845;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in seeds, roots, stems, leaves and
flowers, especially in meristematic tissues, guard cells, embryo
and siliques. {ECO:0000269|PubMed:14731256,
ECO:0000269|PubMed:16339800, ECO:0000269|PubMed:9862504}.
-!- INDUCTION: Repressed by MYB44. Induced by ABA.
{ECO:0000269|PubMed:14731256, ECO:0000269|PubMed:16339800,
ECO:0000269|PubMed:18162593, ECO:0000269|PubMed:9862504}.
-!- DOMAIN: The 'lock' site stabilizes the complex made of PP2C, ABA
and PYR/PYL/RCAR receptor by keeping receptor 'gate' and 'latch'
loops in closed positions.
-!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAH56780.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ003119; CAA05875.1; -; Genomic_DNA.
EMBL; AC010926; AAG51849.1; -; Genomic_DNA.
EMBL; CP002684; AEE35370.1; -; Genomic_DNA.
EMBL; CP002684; AEE35371.1; -; Genomic_DNA.
EMBL; CP002684; AEE35372.1; -; Genomic_DNA.
EMBL; CP002684; ANM58361.1; -; Genomic_DNA.
EMBL; CP002684; ANM58362.1; -; Genomic_DNA.
EMBL; BT015409; AAU05532.1; -; mRNA.
EMBL; AK230171; BAF01980.1; -; mRNA.
EMBL; AK318665; BAH56780.1; ALT_INIT; mRNA.
PIR; F96752; F96752.
RefSeq; NP_001077815.1; NM_001084346.3. [Q9CAJ0-2]
RefSeq; NP_001185385.1; NM_001198456.1. [Q9CAJ0-1]
RefSeq; NP_001320804.1; NM_001334550.1. [Q9CAJ0-1]
RefSeq; NP_001320805.1; NM_001334551.1. [Q9CAJ0-2]
RefSeq; NP_177421.1; NM_105936.4. [Q9CAJ0-1]
UniGene; At.46635; -.
UniGene; At.67356; -.
PDB; 3KB3; X-ray; 1.95 A; B=186-506.
PDB; 3NMT; X-ray; 2.56 A; B=172-511.
PDB; 3QN1; X-ray; 1.80 A; B=178-511.
PDB; 3RT0; X-ray; 2.11 A; A/B=172-511.
PDB; 3UJG; X-ray; 2.60 A; B=172-511.
PDB; 3ZVU; X-ray; 2.10 A; B=178-511.
PDB; 4DS8; X-ray; 2.21 A; B=169-511.
PDB; 4LA7; X-ray; 1.98 A; B=178-505.
PDB; 4LG5; X-ray; 2.88 A; B=172-511.
PDB; 4LGA; X-ray; 2.70 A; B=172-511.
PDB; 4LGB; X-ray; 3.15 A; B=172-511.
PDB; 4WVO; X-ray; 2.25 A; B=178-505.
PDB; 5JO1; X-ray; 2.30 A; B=172-506.
PDB; 5JO2; X-ray; 2.42 A; B=172-506.
PDB; 5MN0; X-ray; 2.00 A; B=179-511.
PDBsum; 3KB3; -.
PDBsum; 3NMT; -.
PDBsum; 3QN1; -.
PDBsum; 3RT0; -.
PDBsum; 3UJG; -.
PDBsum; 3ZVU; -.
PDBsum; 4DS8; -.
PDBsum; 4LA7; -.
PDBsum; 4LG5; -.
PDBsum; 4LGA; -.
PDBsum; 4LGB; -.
PDBsum; 4WVO; -.
PDBsum; 5JO1; -.
PDBsum; 5JO2; -.
PDBsum; 5MN0; -.
ProteinModelPortal; Q9CAJ0; -.
SMR; Q9CAJ0; -.
BioGrid; 28828; 25.
DIP; DIP-48988N; -.
IntAct; Q9CAJ0; 21.
MINT; MINT-8299472; -.
STRING; 3702.AT1G72770.1; -.
PaxDb; Q9CAJ0; -.
EnsemblPlants; AT1G72770.1; AT1G72770.1; AT1G72770. [Q9CAJ0-1]
EnsemblPlants; AT1G72770.2; AT1G72770.2; AT1G72770. [Q9CAJ0-2]
EnsemblPlants; AT1G72770.3; AT1G72770.3; AT1G72770. [Q9CAJ0-1]
EnsemblPlants; AT1G72770.4; AT1G72770.4; AT1G72770. [Q9CAJ0-1]
EnsemblPlants; AT1G72770.5; AT1G72770.5; AT1G72770. [Q9CAJ0-2]
GeneID; 843609; -.
Gramene; AT1G72770.1; AT1G72770.1; AT1G72770.
Gramene; AT1G72770.2; AT1G72770.2; AT1G72770.
Gramene; AT1G72770.3; AT1G72770.3; AT1G72770.
Gramene; AT1G72770.4; AT1G72770.4; AT1G72770.
Gramene; AT1G72770.5; AT1G72770.5; AT1G72770.
KEGG; ath:AT1G72770; -.
Araport; AT1G72770; -.
TAIR; locus:2030230; AT1G72770.
eggNOG; KOG0698; Eukaryota.
eggNOG; COG0631; LUCA.
HOGENOM; HOG000233896; -.
InParanoid; Q9CAJ0; -.
KO; K14497; -.
OMA; CFLTVDG; -.
OrthoDB; EOG09360DDO; -.
PhylomeDB; Q9CAJ0; -.
EvolutionaryTrace; Q9CAJ0; -.
PRO; PR:Q9CAJ0; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; Q9CAJ0; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:TAIR.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
CDD; cd00143; PP2Cc; 1.
Gene3D; 3.60.40.10; -; 1.
InterPro; IPR015655; PP2C.
InterPro; IPR000222; PP2C_BS.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR001932; PPM-type_phosphatase_dom.
PANTHER; PTHR13832; PTHR13832; 1.
Pfam; PF00481; PP2C; 1.
SMART; SM00332; PP2Cc; 1.
SUPFAM; SSF81606; SSF81606; 1.
PROSITE; PS01032; PPM_1; 1.
PROSITE; PS51746; PPM_2; 1.
1: Evidence at protein level;
3D-structure; Abscisic acid signaling pathway; Alternative splicing;
Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese;
Metal-binding; Nucleus; Protein phosphatase; Reference proteome;
Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 511 Protein phosphatase 2C 16.
/FTId=PRO_0000344524.
DOMAIN 189 501 PPM-type phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU01082}.
METAL 243 243 Manganese 1. {ECO:0000244|PDB:3KB3,
ECO:0000269|PubMed:19898420}.
METAL 243 243 Manganese 2. {ECO:0000244|PDB:3NMT,
ECO:0000244|PDB:3QN1,
ECO:0000244|PDB:3RT0,
ECO:0000244|PDB:3UJG,
ECO:0000244|PDB:3ZVU,
ECO:0000244|PDB:4LA7,
ECO:0000244|PDB:4LG5,
ECO:0000244|PDB:4LGA,
ECO:0000244|PDB:4WVO,
ECO:0000269|PubMed:21658606}.
METAL 244 244 Manganese 1; via carbonyl oxygen.
{ECO:0000244|PDB:3KB3,
ECO:0000269|PubMed:19898420}.
METAL 432 432 Manganese 2. {ECO:0000244|PDB:3NMT,
ECO:0000244|PDB:3QN1,
ECO:0000244|PDB:3RT0,
ECO:0000244|PDB:3UJG,
ECO:0000244|PDB:3ZVU,
ECO:0000244|PDB:4LA7,
ECO:0000244|PDB:4LG5,
ECO:0000244|PDB:4LGA,
ECO:0000244|PDB:4WVO,
ECO:0000269|PubMed:21658606}.
METAL 492 492 Manganese 2. {ECO:0000244|PDB:3NMT,
ECO:0000244|PDB:3QN1,
ECO:0000244|PDB:3RT0,
ECO:0000244|PDB:3UJG,
ECO:0000244|PDB:3ZVU,
ECO:0000244|PDB:4LA7,
ECO:0000244|PDB:4LG5,
ECO:0000244|PDB:4LGA,
ECO:0000244|PDB:4WVO,
ECO:0000269|PubMed:21658606}.
SITE 385 385 Lock.
VAR_SEQ 402 406 DRYLK -> KHCFF (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_034844.
VAR_SEQ 407 511 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_034845.
MUTAGEN 246 246 G->D: Reduced phosphatase activity,
impaired affinity for PYR/PYL/RCAR
receptors, and insensitivity to ABA.
{ECO:0000269|PubMed:16876791,
ECO:0000269|PubMed:19033529,
ECO:0000269|PubMed:19624469}.
CONFLICT 46 46 Q -> P (in Ref. 1; CAA05875).
{ECO:0000305}.
HELIX 181 183 {ECO:0000244|PDB:3RT0}.
STRAND 190 195 {ECO:0000244|PDB:3QN1}.
STRAND 199 201 {ECO:0000244|PDB:3QN1}.
STRAND 204 216 {ECO:0000244|PDB:3QN1}.
HELIX 217 219 {ECO:0000244|PDB:3QN1}.
STRAND 233 248 {ECO:0000244|PDB:3QN1}.
HELIX 249 268 {ECO:0000244|PDB:3QN1}.
TURN 269 271 {ECO:0000244|PDB:4LA7}.
HELIX 284 302 {ECO:0000244|PDB:3QN1}.
STRAND 319 321 {ECO:0000244|PDB:4LG5}.
STRAND 329 334 {ECO:0000244|PDB:3QN1}.
STRAND 336 346 {ECO:0000244|PDB:3QN1}.
STRAND 348 353 {ECO:0000244|PDB:3QN1}.
STRAND 356 360 {ECO:0000244|PDB:3QN1}.
HELIX 369 377 {ECO:0000244|PDB:3QN1}.
STRAND 382 390 {ECO:0000244|PDB:3QN1}.
TURN 391 393 {ECO:0000244|PDB:3QN1}.
HELIX 403 405 {ECO:0000244|PDB:3QN1}.
TURN 406 408 {ECO:0000244|PDB:3QN1}.
STRAND 414 419 {ECO:0000244|PDB:3QN1}.
STRAND 424 430 {ECO:0000244|PDB:3QN1}.
HELIX 432 435 {ECO:0000244|PDB:3QN1}.
HELIX 440 458 {ECO:0000244|PDB:3QN1}.
TURN 463 468 {ECO:0000244|PDB:3KB3}.
HELIX 472 487 {ECO:0000244|PDB:3QN1}.
STRAND 494 500 {ECO:0000244|PDB:3QN1}.
SEQUENCE 511 AA; 55744 MW; B001BAF0DD8333E1 CRC64;
MEEMTPAVAM TLSLAANTMC ESSPVEITQL KNVTDAADLL SDSENQSFCN GGTECTMEDV
SELEEVGEQD LLKTLSDTRS GSSNVFDEDD VLSVVEDNSA VISEGLLVVD AGSELSLSNT
AMEIDNGRVL ATAIIVGESS IEQVPTAEVL IAGVNQDTNT SEVVIRLPDE NSNHLVKGRS
VYELDCIPLW GTVSIQGNRS EMEDAFAVSP HFLKLPIKML MGDHEGMSPS LTHLTGHFFG
VYDGHGGHKV ADYCRDRLHF ALAEEIERIK DELCKRNTGE GRQVQWDKVF TSCFLTVDGE
IEGKIGRAVV GSSDKVLEAV ASETVGSTAV VALVCSSHIV VSNCGDSRAV LFRGKEAMPL
SVDHKPDRED EYARIENAGG KVIQWQGARV FGVLAMSRSI GDRYLKPYVI PEPEVTFMPR
SREDECLILA SDGLWDVMNN QEVCEIARRR ILMWHKKNGA PPLAERGKGI DPACQAAADY
LSMLALQKGS KDNISIIVID LKAQRKFKTR T


Related products :

Catalog number Product name Quantity
EIAAB32079 Homo sapiens,Human,PP2C domain-containing protein phosphatase 1K,PP2C-kappa,PP2C-like mitochondrial protein,PP2CM,PP2C-type mitochondrial phosphoprotein phosphatase,PPM1K,Protein phosphatase 1K, mitoc
EIAAB32071 Bos taurus,Bovine,Magnesium-dependent calcium inhibitable phosphatase,MCPP,PP2C-gamma,PPM1C,PPM1G,Protein phosphatase 1B,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphatase
EIAAB32061 Homo sapiens,Human,p53-induced protein phosphatase 1,PP2C-delta,PPM1D,Protein phosphatase 1D,Protein phosphatase 2C isoform delta,Protein phosphatase magnesium-dependent 1 delta,WIP1
EIAAB32069 Homo sapiens,Human,PP2C-gamma,PPM1C,PPM1G,Protein phosphatase 1C,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphatase magnesium-dependent 1 gamma
EIAAB32062 Mouse,Mus musculus,p53-induced protein phosphatase 1,PP2C-delta,Ppm1d,Protein phosphatase 1D,Protein phosphatase 2C isoform delta,Protein phosphatase magnesium-dependent 1 delta,Wip1
PP-PPM1G-050 PPM1G, Protein Phosphatase 1G, PP2CG, PPP2CG, MGC1675, MGC2870, PP2C GAMMA, EC 3.1.3.16, Protein phosphatase 2C isoform gamma, PP2C-gamma, Protein phosphatase magnesium-dependent 1 gamma, Protein phos 50
EIAAB32070 Fibroblast growth factor-inducible protein 13,FIN13,Fin13,Mouse,Mus musculus,PP2C-gamma,Ppm1c,Ppm1g,Protein phosphatase 1C,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphata
EIAAB32055 Homo sapiens,Human,PP2C-alpha,PPM1A,PPPM1A,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA
EIAAB32056 Oryctolagus cuniculus,PP2C-alpha,PPM1A,PPPM1A,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA,Rabbit
EIAAB32081 Homo sapiens,Human,PP2CE,PP2C-epsilon,PPM1L,Protein phosphatase 1L,Protein phosphatase 1-like,Protein phosphatase 2C isoform epsilon
EIAAB32054 Pp2c1,PP2C-alpha,Ppm1a,Pppm1a,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA,Rat,Rattus norvegicus
EIAAB32083 Bos taurus,Bovine,PP2CE,PP2C-epsilon,PPM1L,Protein phosphatase 1L,Protein phosphatase 1-like,Protein phosphatase 2C isoform epsilon
EIAAB32082 Kiaa4175,Mouse,Mus musculus,PP2C-epsilon,Ppm1l,Protein phosphatase 1L,Protein phosphatase 1-like,Protein phosphatase 2C isoform epsilon
EIAAB32053 Mouse,Mus musculus,PP2C-alpha,Ppm1a,Pppm1a,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA
EIAAB32139 Homo sapiens,Human,PPTC7,Protein phosphatase PTC7 homolog,TAPP2C,TA-PP2C,T-cell activation protein phosphatase 2C,T-cell activation protein phosphatase 2C-like
EIAAB32084 Homo sapiens,Human,PP2CE,PP2C-eta,PPM1E,PPM1M,Protein phosphatase 1M,Protein phosphatase 2C isoform eta
EIAAB32138 Mouse,Mus musculus,Pptc7,Protein phosphatase PTC7 homolog,Tapp2c,TA-PP2C,T-cell activation protein phosphatase 2C
EIAAB32085 Mouse,Mus musculus,PP2CE,PP2C-eta,Ppm1e,Ppm1m,Protein phosphatase 1M,Protein phosphatase 2C isoform eta
EIAAB32058 Mouse,Mus musculus,Pp2c2,PP2C-beta,Ppm1b,Pppm1b,Protein phosphatase 1B,Protein phosphatase 2C isoform beta
EIAAB32080 Mouse,Mus musculus,PP2C-kappa,Pp2cm,Ppm1k,Protein phosphatase 1K, mitochondrial,Protein phosphatase 2C isoform kappa
EIAAB32057 Pp2c2,PP2C-beta,Ppm1b,Pppm1b,Protein phosphatase 1B,Protein phosphatase 2C isoform beta,Rat,Rattus norvegicus
EIAAB32060 Homo sapiens,Human,PP2CB,PP2C-beta,PPM1B,Protein phosphatase 1B,Protein phosphatase 2C isoform beta
EIAAB32076 Homo sapiens,Human,PP2C-zeta,PPM1J,PPP2CZ,Protein phosphatase 1J,Protein phosphatase 2C isoform zeta
EIAAB32075 Mouse,Mus musculus,PP2C-zeta,Ppm1j,Ppp2cz,Protein phosphatase 1J,Protein phosphatase 2C isoform zeta
EIAAB32077 PP2C-zeta,Ppm1j,Ppp2cz,Protein phosphatase 1J,Protein phosphatase 2C isoform zeta,Rat,Rattus norvegicus


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur