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Protein

Protein phosphatase 2C 56

Gene

ABI1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), drought-induced resistance and rhizogenesis, response to glucose, high light stress, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as the actin reorganization in guard cells in response to ABA. Involved in the resistance to the bacterial pathogen Pseudomonas syringae pv. tomato. Controls negatively fibrillin expression that is involved in mediating ABA-induced photoprotection. May be involved in ABA content regulation. Plays a role in the Pro accumulation in response to reduced water availability (low water potential). Required for the ABA negative regulation of the ethylene-induced hyponastic growth. Involved in acquired thermotolerance of root growth and seedling survival. Activates/represses SRK2E/OST1 in response to ABA-dependent stimuli, especially in stomata closure regulation involving SLAC1.49 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.3 Publications

Cofactori

Mg2+3 Publications, Mn2+3 PublicationsNote: Binds 2 magnesium or manganese ions per subunit.4 Publications

Enzyme regulationi

Phosphatase activity repressed by oxidized GPX3 and phosphatidic acid (PA). PA is produced by PLD alpha 1 in response to ABA. Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner.4 Publications

pH dependencei

Optimum pH is 8.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi177 – 1771Magnesium or manganese 1Combined sources
Metal bindingi177 – 1771Magnesium or manganese 2Combined sources
Metal bindingi178 – 1781Magnesium or manganese 1; via carbonyl oxygenBy similarity
Metal bindingi261 – 2611Magnesium or manganese 1Combined sources
Metal bindingi262 – 2621Magnesium or manganese 1By similarity
Sitei300 – 3001LockBy similarity
Metal bindingi347 – 3471Magnesium or manganese 1; via amide nitrogenCombined sources
Metal bindingi347 – 3471Magnesium or manganese 2Combined sources
Metal bindingi351 – 3511Magnesium or manganese 1By similarity
Metal bindingi413 – 4131Magnesium or manganese 2Combined sources

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphoprotein phosphatase activity Source: CACAO
  • protein kinase binding Source: UniProtKB
  • protein serine/threonine phosphatase activity Source: TAIR

GO - Biological processi

  • abscisic acid-activated signaling pathway Source: UniProtKB-KW
  • negative regulation of abscisic acid-activated signaling pathway Source: UniProtKB
  • protein dephosphorylation Source: CACAO
  • regulation of abscisic acid-activated signaling pathway Source: TAIR
  • regulation of stomatal movement Source: TAIR
  • response to abscisic acid Source: TAIR
  • response to cold Source: TAIR
  • response to heat Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Abscisic acid signaling pathway

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT4G26080-MONOMER.
BRENDAi3.1.3.16. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 2C 56 (EC:3.1.3.16)
Short name:
AtPP2C56
Alternative name(s):
Protein ABSCISIC ACID-INSENSITIVE 1
Protein phosphatase 2C ABI1
Short name:
PP2C ABI1
Gene namesi
Name:ABI1
Ordered Locus Names:At4g26080
ORF Names:F20B18.190
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G26080.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: TAIR
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 682RK → GA: Normal binding with PA, no reduction of phosphatase activity. 1 Publication
Mutagenesisi73 – 731R → A: Loss of binding with PA, no reduction of phosphatase activity. 2 Publications
Mutagenesisi93 – 931D → A: No phenotype. 1 Publication
Mutagenesisi141 – 1433MED → IHG: Reduced inhibition of the ABA signaling pathway and loss of phosphatase activity. 1 Publication
Mutagenesisi142 – 1421E → A: Reduced binding affinity for PYL1, and impaired phosphatase activity. 1 Publication
Mutagenesisi174 – 1741G → D: No inhibition of the ABA signaling pathway and loss of phosphatase activity. 1 Publication
Mutagenesisi177 – 1793DGH → KLN: No inhibition of the ABA signaling pathway and loss of phosphatase activity. 1 Publication
Mutagenesisi177 – 1771D → A: Loss of phosphatase activity, impaired negative regulation of the ABA signaling pathway, reduced interaction with ATHB-6, and reduced negative control on fibrillin expression. 3 Publications
Mutagenesisi180 – 1801G → D in abi1; wilty phenotype, reduced phosphatase activity, ABA-insensitive seed germination and growth, impaired ABA-mediated binding to PYR1, and reduced interaction with ATHB-6. Increased sensitivity to ABA and loss of phosphatase activity; when associated with T-185, or Y-259, or C-304, or D-307, or F-314, or L-328, or N-316. No inhibition of the ABA signaling pathway and loss of phosphatase activity; when associated with D-174. 8 Publications
Mutagenesisi185 – 1851A → T: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
Mutagenesisi239 – 2391T → A: Normal affinity for PYL1. 1 Publication
Mutagenesisi259 – 2591C → Y: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
Mutagenesisi298 – 2981I → A: Loss of affinity for PYL1. 1 Publication
Mutagenesisi300 – 3001W → A: Loss of affinity for PYL1. 1 Publication
Mutagenesisi304 – 3041R → A: Loss of affinity for PYL1. 2 Publications
Mutagenesisi304 – 3041R → C: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 2 Publications
Mutagenesisi306 – 3061F → A: Reduced affinity for PYL1. 1 Publication
Mutagenesisi307 – 3071G → D: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
Mutagenesisi308 – 3081V → A: Reduced affinity for PYL1. 1 Publication
Mutagenesisi314 – 3141S → F: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
Mutagenesisi319 – 3191Y → A: Reduced affinity for PYL1. 1 Publication
Mutagenesisi328 – 3281P → L: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
Mutagenesisi416 – 4161S → N: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
Mutagenesisi425 – 4273RRK → QNN: Cytoplasmic subcellular localization, and loss of negative regulation of the ABA signaling pathway. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Protein phosphatase 2C 56PRO_0000057766Add
BLAST

Proteomic databases

PaxDbiP49597.
PRIDEiP49597.

PTM databases

iPTMnetiP49597.

Expressioni

Tissue specificityi

Expressed in seeds and seedlings. In roots, confined to lateral root caps and columella cells.2 Publications

Inductioni

Repressed by MYB44. Induced by low temperature, drought, high salt, ABA and ethylene.6 Publications

Gene expression databases

GenevisibleiP49597. AT.

Interactioni

Subunit structurei

Interacts with SPK1, ATHB-6, CIPK15/PKS3, GPX3, SRK2E/OST1, SRK2D, SRK2I, SCAR1, SCAR2, SCAR3 and SCARL. Binds to the PA released by the phospholipase D alpha 1 (PLDALPHA1) in response to ABA during the stomatal closure regulation. Interacts with ABA-bounded PYR1, PYL1, PYL2, PYL3, PYL4, PYL5, PYL6, PYL7, PYL8, PYL9, PYL10, and with free PYL2, PYL3, PYL4 and PYL13. Binds to RPL12B, CPK21 and CPK23.18 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PYL4O809203EBI-782526,EBI-2349683
PYL5Q9FLB13EBI-782526,EBI-2363181
PYL9Q84MC74EBI-782526,EBI-2349513
PYR1O496867EBI-782526,EBI-2349590
SRK2DQ391924EBI-782526,EBI-2363308
SRK2EQ940H64EBI-782526,EBI-782514
SRK2IQ391933EBI-782526,EBI-2620383

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi14001. 62 interactions.
DIPiDIP-36706N.
IntActiP49597. 22 interactions.
MINTiMINT-8390807.
STRINGi3702.AT4G26080.1.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi129 – 1346Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi143 – 1486Combined sources
Turni149 – 1524Combined sources
Helixi166 – 1694Combined sources
Beta strandi171 – 18212Combined sources
Helixi183 – 20321Combined sources
Helixi207 – 2104Combined sources
Helixi211 – 23121Combined sources
Helixi232 – 2343Combined sources
Beta strandi244 – 2496Combined sources
Beta strandi251 – 26111Combined sources
Beta strandi263 – 2686Combined sources
Beta strandi271 – 2755Combined sources
Helixi284 – 2929Combined sources
Beta strandi297 – 3059Combined sources
Turni306 – 3083Combined sources
Helixi318 – 3203Combined sources
Turni321 – 3233Combined sources
Beta strandi329 – 3346Combined sources
Beta strandi339 – 3457Combined sources
Helixi347 – 3504Combined sources
Helixi355 – 36915Combined sources
Helixi393 – 40816Combined sources
Beta strandi415 – 4217Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JRQX-ray2.10A125-429[»]
3KDJX-ray1.88B119-434[»]
3NMNX-ray2.15B/D117-434[»]
ProteinModelPortaliP49597.
SMRiP49597. Positions 125-424.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49597.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini128 – 422295PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi423 – 4275Nuclear localization signal1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi417 – 4204Poly-Val

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the PP2C family.Curated
Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0698. Eukaryota.
COG0631. LUCA.
HOGENOMiHOG000233896.
InParanoidiP49597.
KOiK14497.
OMAiCPTHIIV.
OrthoDBiEOG09360DDO.
PhylomeDBiP49597.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 3 hits.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49597-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEVSPAIAG PFRPFSETQM DFTGIRLGKG YCNNQYSNQD SENGDLMVSL
60 70 80 90 100
PETSSCSVSG SHGSESRKVL ISRINSPNLN MKESAAADIV VVDISAGDEI
110 120 130 140 150
NGSDITSEKK MISRTESRSL FEFKSVPLYG FTSICGRRPE MEDAVSTIPR
160 170 180 190 200
FLQSSSGSML DGRFDPQSAA HFFGVYDGHG GSQVANYCRE RMHLALAEEI
210 220 230 240 250
AKEKPMLCDG DTWLEKWKKA LFNSFLRVDS EIESVAPETV GSTSVVAVVF
260 270 280 290 300
PSHIFVANCG DSRAVLCRGK TALPLSVDHK PDREDEAARI EAAGGKVIQW
310 320 330 340 350
NGARVFGVLA MSRSIGDRYL KPSIIPDPEV TAVKRVKEDD CLILASDGVW
360 370 380 390 400
DVMTDEEACE MARKRILLWH KKNAVAGDAS LLADERRKEG KDPAAMSAAE
410 420 430
YLSKLAIQRG SKDNISVVVV DLKPRRKLKS KPLN
Length:434
Mass (Da):47,506
Last modified:June 6, 2002 - v2
Checksum:i4A4C54F04195F572
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241G → R in AAK59578 (PubMed:14593172).Curated
Sequence conflicti105 – 1051I → V in CAA55484 (PubMed:8197457).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12856 mRNA. Translation: AAA50237.1.
X77116 mRNA. Translation: CAA54383.1.
X78886 Genomic DNA. Translation: CAA55484.1.
AL049483 Genomic DNA. Translation: CAB39673.1.
AL161564 Genomic DNA. Translation: CAB79463.1.
CP002687 Genomic DNA. Translation: AEE85155.1.
AY035073 mRNA. Translation: AAK59578.1.
AY142623 mRNA. Translation: AAN13081.1.
AK226529 mRNA. Translation: BAE98668.1.
PIRiT04263.
RefSeqiNP_194338.1. NM_118741.2.
UniGeneiAt.21332.

Genome annotation databases

EnsemblPlantsiAT4G26080.1; AT4G26080.1; AT4G26080.
GeneIDi828714.
GrameneiAT4G26080.1; AT4G26080.1; AT4G26080.
KEGGiath:AT4G26080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12856 mRNA. Translation: AAA50237.1.
X77116 mRNA. Translation: CAA54383.1.
X78886 Genomic DNA. Translation: CAA55484.1.
AL049483 Genomic DNA. Translation: CAB39673.1.
AL161564 Genomic DNA. Translation: CAB79463.1.
CP002687 Genomic DNA. Translation: AEE85155.1.
AY035073 mRNA. Translation: AAK59578.1.
AY142623 mRNA. Translation: AAN13081.1.
AK226529 mRNA. Translation: BAE98668.1.
PIRiT04263.
RefSeqiNP_194338.1. NM_118741.2.
UniGeneiAt.21332.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JRQX-ray2.10A125-429[»]
3KDJX-ray1.88B119-434[»]
3NMNX-ray2.15B/D117-434[»]
ProteinModelPortaliP49597.
SMRiP49597. Positions 125-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14001. 62 interactions.
DIPiDIP-36706N.
IntActiP49597. 22 interactions.
MINTiMINT-8390807.
STRINGi3702.AT4G26080.1.

PTM databases

iPTMnetiP49597.

Proteomic databases

PaxDbiP49597.
PRIDEiP49597.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G26080.1; AT4G26080.1; AT4G26080.
GeneIDi828714.
GrameneiAT4G26080.1; AT4G26080.1; AT4G26080.
KEGGiath:AT4G26080.

Organism-specific databases

TAIRiAT4G26080.

Phylogenomic databases

eggNOGiKOG0698. Eukaryota.
COG0631. LUCA.
HOGENOMiHOG000233896.
InParanoidiP49597.
KOiK14497.
OMAiCPTHIIV.
OrthoDBiEOG09360DDO.
PhylomeDBiP49597.

Enzyme and pathway databases

BioCyciARA:AT4G26080-MONOMER.
BRENDAi3.1.3.16. 399.

Miscellaneous databases

EvolutionaryTraceiP49597.
PROiP49597.

Gene expression databases

GenevisibleiP49597. AT.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 3 hits.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiP2C56_ARATH
AccessioniPrimary (citable) accession number: P49597
Secondary accession number(s): Q0WW30, Q43717, Q94C87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: June 6, 2002
Last modified: September 7, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Enhanced ABA signaling repressor activity by the proteasomal inhibitor MG132 accompanied by a cytoplasmic localization.
Plants insensitive to ABA (abi1-1) are more resistant to P.syringae.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.