Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi177Magnesium or manganese 1Combined sources1
Metal bindingi177Magnesium or manganese 2Combined sources1
Metal bindingi178Magnesium or manganese 1; via carbonyl oxygenBy similarity1
Metal bindingi261Magnesium or manganese 1Combined sources1
Metal bindingi262Magnesium or manganese 1By similarity1
Sitei300LockBy similarity1
Metal bindingi347Magnesium or manganese 1; via amide nitrogenCombined sources1
Metal bindingi347Magnesium or manganese 2Combined sources1
Metal bindingi351Magnesium or manganese 1By similarity1
Metal bindingi413Magnesium or manganese 2Combined sources1

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

Keywordsi

Molecular functionHydrolase, Protein phosphatase
Biological processAbscisic acid signaling pathway
LigandMagnesium, Manganese, Metal-binding

Enzyme and pathway databases

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

TAIRilocus:2005488. AT4G26080.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: TAIR
  • plasma membrane Source: UniProtKB-SubCell

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67 – 68RK → GA: Normal binding with PA, no reduction of phosphatase activity. 1 Publication2
Mutagenesisi73R → A: Loss of binding with PA, no reduction of phosphatase activity. 2 Publications1
Mutagenesisi93D → A: No phenotype. 1 Publication1
Mutagenesisi141 – 143MED → IHG: Reduced inhibition of the ABA signaling pathway and loss of phosphatase activity. 1 Publication3
Mutagenesisi142E → A: Reduced binding affinity for PYL1, and impaired phosphatase activity. 1 Publication1
Mutagenesisi174G → D: No inhibition of the ABA signaling pathway and loss of phosphatase activity. 1 Publication1
Mutagenesisi177 – 179DGH → KLN: No inhibition of the ABA signaling pathway and loss of phosphatase activity. 1 Publication3
Mutagenesisi177D → 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 Publications1
Mutagenesisi180G → 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 Publications1
Mutagenesisi185A → T: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication1
Mutagenesisi239T → A: Normal affinity for PYL1. 1 Publication1
Mutagenesisi259C → Y: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication1
Mutagenesisi298I → A: Loss of affinity for PYL1. 1 Publication1
Mutagenesisi300W → A: Loss of affinity for PYL1. 1 Publication1
Mutagenesisi304R → A: Loss of affinity for PYL1. 2 Publications1
Mutagenesisi304R → C: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 2 Publications1
Mutagenesisi306F → A: Reduced affinity for PYL1. 1 Publication1
Mutagenesisi307G → D: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication1
Mutagenesisi308V → A: Reduced affinity for PYL1. 1 Publication1
Mutagenesisi314S → F: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication1
Mutagenesisi319Y → A: Reduced affinity for PYL1. 1 Publication1
Mutagenesisi328P → L: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication1
Mutagenesisi416S → N: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication1
Mutagenesisi425 – 427RRK → QNN: Cytoplasmic subcellular localization, and loss of negative regulation of the ABA signaling pathway. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000577661 – 434Protein phosphatase 2C 56Add BLAST434

Proteomic databases

PaxDbiP49597.

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

Show more details

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

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

Structurei

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi129 – 134Combined sources6
Beta strandi138 – 140Combined sources3
Beta strandi143 – 148Combined sources6
Turni149 – 152Combined sources4
Helixi166 – 169Combined sources4
Beta strandi171 – 182Combined sources12
Helixi183 – 203Combined sources21
Helixi207 – 210Combined sources4
Helixi211 – 231Combined sources21
Helixi232 – 234Combined sources3
Beta strandi244 – 249Combined sources6
Beta strandi251 – 261Combined sources11
Beta strandi263 – 268Combined sources6
Beta strandi271 – 275Combined sources5
Helixi284 – 292Combined sources9
Beta strandi297 – 305Combined sources9
Turni306 – 308Combined sources3
Helixi318 – 320Combined sources3
Turni321 – 323Combined sources3
Beta strandi329 – 334Combined sources6
Beta strandi339 – 345Combined sources7
Helixi347 – 350Combined sources4
Helixi355 – 369Combined sources15
Helixi393 – 408Combined sources16
Beta strandi415 – 421Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP49597.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini128 – 422PPM-type phosphatasePROSITE-ProRule annotationAdd BLAST295

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi423 – 427Nuclear localization signal1 Publication5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi417 – 420Poly-Val4

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

Phylogenomic databases

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

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiView protein in InterPro
IPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiView protein in Pfam
PF00481. PP2C. 1 hit.
SMARTiView protein in SMART
SM00332. PP2Cc. 1 hit.
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiView protein in PROSITE
PS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti24G → R in AAK59578 (PubMed:14593172).Curated1
Sequence conflicti105I → V in CAA55484 (PubMed:8197457).Curated1

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_118741.3.
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_118741.3.
UniGeneiAt.21332.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

iPTMnetiP49597.

Proteomic databases

PaxDbiP49597.

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

AraportiAT4G26080.
TAIRilocus:2005488. AT4G26080.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi3.1.3.16. 399.

Miscellaneous databases

EvolutionaryTraceiP49597.
PROiP49597.

Gene expression databases

GenevisibleiP49597. AT.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiView protein in InterPro
IPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiView protein in Pfam
PF00481. PP2C. 1 hit.
SMARTiView protein in SMART
SM00332. PP2Cc. 1 hit.
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiView protein in PROSITE
PS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiP2C56_ARATH
AccessioniPrimary (citable) accession number: P49597
Secondary accession number(s): Q0WW30, Q43717, Q94C87
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: June 6, 2002
Last modified: February 15, 2017
This is version 167 of the entry and version 2 of the sequence. See 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.