Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9CAJ0 (P2C16_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase 2C 16

Short name=AtPP2C16
EC=3.1.3.16
Alternative name(s):
AtP2C-HA
Protein HYPERSENSITIVE TO ABA 1
Protein phosphatase 2C HAB1
Short name=PP2C HAB1
Gene names
Name:HAB1
Synonyms:P2C-HA
Ordered Locus Names:At1g72770
ORF Names:F28P22.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7 Ref.9 Ref.11 Ref.13

Catalytic activity

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

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Enzyme regulation

Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner. Ref.17

Subunit structure

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 and PYL4. Ref.13 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location

Cytoplasm. Nucleus. Note: Mainly cytoplasmic. Ref.13

Tissue specificity

Expressed in seeds, roots, stems, leaves and flowers, especially in meristematic tissues, guard cells, embryo and siliques. Ref.1 Ref.7 Ref.10

Induction

Repressed by MYB44. Induced by ABA. Ref.1 Ref.7 Ref.10 Ref.14 Ref.17

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.

Sequence similarities

Belongs to the PP2C family.

Contains 1 PP2C-like domain.

Sequence caution

The sequence BAH56780.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAbscisic acid signaling pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainSignal
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processabscisic acid-activated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

protein dephosphorylation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine phosphatase activity

Inferred from direct assay PubMed 19855047. Source: TAIR

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9CAJ0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9CAJ0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     402-406: DRYLK → KHCFF
     407-511: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 511489Protein phosphatase 2C 16
PRO_0000344524

Regions

Domain135 – 433299PP2C-like

Sites

Metal binding2431Manganese 1 By similarity
Metal binding2431Manganese 2 By similarity
Metal binding2441Manganese 1; via carbonyl oxygen By similarity
Metal binding4321Manganese 2 By similarity
Metal binding4921Manganese 2 By similarity
Site3851Lock

Natural variations

Alternative sequence402 – 4065DRYLK → KHCFF in isoform 2.
VSP_034844
Alternative sequence407 – 511105Missing in isoform 2.
VSP_034845

Experimental info

Mutagenesis2461G → D: Reduced phosphatase activity, impaired affinity for PYR/PYL/RCAR receptors, and insensitivity to ABA. Ref.9 Ref.13 Ref.15
Sequence conflict461Q → P in CAA05875. Ref.1

Secondary structure

................................................ 511
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B001BAF0DD8333E1

FASTA51155,744
        10         20         30         40         50         60 
MEEMTPAVAM TLSLAANTMC ESSPVEITQL KNVTDAADLL SDSENQSFCN GGTECTMEDV 

        70         80         90        100        110        120 
SELEEVGEQD LLKTLSDTRS GSSNVFDEDD VLSVVEDNSA VISEGLLVVD AGSELSLSNT 

       130        140        150        160        170        180 
AMEIDNGRVL ATAIIVGESS IEQVPTAEVL IAGVNQDTNT SEVVIRLPDE NSNHLVKGRS 

       190        200        210        220        230        240 
VYELDCIPLW GTVSIQGNRS EMEDAFAVSP HFLKLPIKML MGDHEGMSPS LTHLTGHFFG 

       250        260        270        280        290        300 
VYDGHGGHKV ADYCRDRLHF ALAEEIERIK DELCKRNTGE GRQVQWDKVF TSCFLTVDGE 

       310        320        330        340        350        360 
IEGKIGRAVV GSSDKVLEAV ASETVGSTAV VALVCSSHIV VSNCGDSRAV LFRGKEAMPL 

       370        380        390        400        410        420 
SVDHKPDRED EYARIENAGG KVIQWQGARV FGVLAMSRSI GDRYLKPYVI PEPEVTFMPR 

       430        440        450        460        470        480 
SREDECLILA SDGLWDVMNN QEVCEIARRR ILMWHKKNGA PPLAERGKGI DPACQAAADY 

       490        500        510 
LSMLALQKGS KDNISIIVID LKAQRKFKTR T 

« Hide

Isoform 2 [UniParc].

Checksum: 489298C9592A9F43
Show »

FASTA40643,866

References

« Hide 'large scale' references
[1]"Molecular cloning in Arabidopsis thaliana of a new protein phosphatase 2C (PP2C) with homology to ABI1 and ABI2."
Rodriguez P.L., Leube M.P., Grill E.
Plant Mol. Biol. 38:879-883(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION BY ABA.
Strain: cv. Landsberg erecta.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Arabidopsis ORF clones."
Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
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. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
[6]"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-511 (ISOFORM 1).
Tissue: Rosette leaf.
[7]"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."
Saez A., Apostolova N., Gonzalez-Guzman M., Gonzalez-Garcia M.P., Nicolas C., Lorenzo O., Rodriguez P.L.
Plant J. 37:354-369(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ABA.
[8]"Plant PP2C phosphatases: emerging functions in stress signaling."
Schweighofer A., Hirt H., Meskiene I.
Trends Plant Sci. 9:236-243(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[9]"A hypermorphic mutation in the protein phosphatase 2C HAB1 strongly affects ABA signaling in Arabidopsis."
Robert N., Merlot S., N'guyen V., Boisson-Dernier A., Schroeder J.I.
FEBS Lett. 580:4691-4696(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-246.
[10]"ABA-hypersensitive germination3 encodes a protein phosphatase 2C (AtPP2CA) that strongly regulates abscisic acid signaling during germination among Arabidopsis protein phosphatase 2Cs."
Yoshida T., Nishimura N., Kitahata N., Kuromori T., Ito T., Asami T., Shinozaki K., Hirayama T.
Plant Physiol. 140:115-126(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY ABA, TISSUE SPECIFICITY.
[11]"Enhancement of abscisic acid sensitivity and reduction of water consumption in Arabidopsis by combined inactivation of the protein phosphatases type 2C ABI1 and HAB1."
Saez A., Robert N., Maktabi M.H., Schroeder J.I., Serrano R., Rodriguez P.L.
Plant Physiol. 141:1389-1399(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Genome-wide and expression analysis of protein phosphatase 2C in rice and Arabidopsis."
Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.
BMC Genomics 9:550-550(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[13]"HAB1-SWI3B interaction reveals a link between abscisic acid signaling and putative SWI/SNF chromatin-remodeling complexes in Arabidopsis."
Saez A., Rodrigues A., Santiago J., Rubio S., Rodriguez P.L.
Plant Cell 20:2972-2988(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SWI3B, MUTAGENESIS OF GLY-246.
[14]"Overexpression of AtMYB44 enhances stomatal closure to confer abiotic stress tolerance in transgenic Arabidopsis."
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.
Plant Physiol. 146:623-635(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY MYB44.
[15]"Modulation of drought resistance by the abscisic acid receptor PYL5 through inhibition of clade A PP2Cs."
Santiago J., Rodrigues A., Saez A., Rubio S., Antoni R., Dupeux F., Park S.-Y., Marquez J.A., Cutler S.R., Rodriguez P.L.
Plant J. 60:575-588(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PYL5; PYL6 AND PYL8, MUTAGENESIS OF GLY-246.
[16]"Regulators of PP2C phosphatase activity function as abscisic acid sensors."
Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A., Grill E.
Science 324:1064-1068(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PYL9/RCAR1.
[17]"Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins."
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. expand/collapse author list , Schroeder J.I., Volkman B.F., Cutler S.R.
Science 324:1068-1071(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PYR1; PYL1; PYL2; PYL3 AND PYL4, ENZYME REGULATION.
[18]"A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors."
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. expand/collapse author list , Cutler S.R., Zhu J.-K., Xu H.E.
Nature 462:602-608(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 186-506 IN COMPLEX WITH ABSCISIC ACID AND PYL2, INTERACTION WITH PYR1; PYL1; PYL2; PYL3; PYL4; PYL5 AND PYL6, LOCK SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ003119 Genomic DNA. Translation: CAA05875.1.
AC010926 Genomic DNA. Translation: AAG51849.1.
CP002684 Genomic DNA. Translation: AEE35370.1.
CP002684 Genomic DNA. Translation: AEE35371.1.
CP002684 Genomic DNA. Translation: AEE35372.1.
BT015409 mRNA. Translation: AAU05532.1.
AK230171 mRNA. Translation: BAF01980.1.
AK318665 mRNA. Translation: BAH56780.1. Different initiation.
PIRF96752.
RefSeqNP_001077815.1. NM_001084346.2.
NP_001185385.1. NM_001198456.1.
NP_177421.1. NM_105936.3.
UniGeneAt.46635.
At.67356.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KB3X-ray1.95B186-506[»]
3NMTX-ray2.56B172-511[»]
3QN1X-ray1.80B178-511[»]
3RT0X-ray2.11A/B172-511[»]
3UJGX-ray2.60B172-511[»]
3ZVUX-ray2.10B178-511[»]
4DS8X-ray2.21B169-511[»]
4LA7X-ray1.98B178-505[»]
4LG5X-ray2.88B172-511[»]
4LGAX-ray2.70B172-511[»]
4LGBX-ray3.15B172-511[»]
ProteinModelPortalQ9CAJ0.
SMRQ9CAJ0. Positions 180-510.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid28828. 17 interactions.
DIPDIP-48988N.
IntActQ9CAJ0. 16 interactions.
MINTMINT-8299472.

Proteomic databases

PRIDEQ9CAJ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G72770.1; AT1G72770.1; AT1G72770. [Q9CAJ0-1]
AT1G72770.3; AT1G72770.3; AT1G72770. [Q9CAJ0-1]
GeneID843609.
KEGGath:AT1G72770.

Organism-specific databases

TAIRAT1G72770.

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000233896.
InParanoidQ9CAJ0.
KOK14497.
OMAYARIENA.
PhylomeDBQ9CAJ0.
ProtClustDBCLSN2679602.

Enzyme and pathway databases

BioCycARA:AT1G72770-MONOMER.
ARA:GQT-2826-MONOMER.
ARA:GQT-408-MONOMER.

Gene expression databases

GenevestigatorQ9CAJ0.

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9CAJ0.

Entry information

Entry nameP2C16_ARATH
AccessionPrimary (citable) accession number: Q9CAJ0
Secondary accession number(s): C0Z251, O81709, Q0WLM7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names