Q9LQN6 (P2C04_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable protein phosphatase 2C 4
Short name=AtPP2C04
EC=3.1.3.16

Alternative name(s):
Protein POLTERGEIST-LIKE 5
Protein phosphatase 2C PLL5
Short name=PP2C PLL5

Gene names

Name:	PLL5
Ordered Locus Names:	At1g07630
ORF Names:	F24B9.25, F24B9.31

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	662 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in leaf development regulation. Ref.5
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Subcellular location	Nucleus Probable.
Tissue specificity	Expressed in seedlings, roots, leaves, stems, young inflorescences, flowers and siliques. Ref.5
Domain	The conserved PP2C phosphatase domain (250-651) is interrupted by an insertion of approximately 100 amino acids.
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors.
Disruption phenotype	Plants show abnormal leaves altered in shape and curling. Ref.5
Sequence similarities	Belongs to the PP2C family. Contains 1 PP2C-like domain.
Sequence caution	The sequence AAK32783.1 differs from that shown. Reason: Frameshift at position 491. The sequence AAM91433.1 differs from that shown. Reason: Frameshift at position 491.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	Magnesium Manganese Metal-binding
Molecular function	Developmental protein Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	leaf development Inferred from mutant phenotype Ref.5. Source: TAIR
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay Ref.6. Source: TAIR
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 662	662	Probable protein phosphatase 2C 4		PRO_0000301263
Regions
	Domain	269 – 629	361	PP2C-like
	Compositional bias	14 – 17	4	Poly-Gly
	Compositional bias	62 – 66	5	Poly-Thr
Sites
	Metal binding	286	1	Manganese 1 By similarity
	Metal binding	286	1	Manganese 2 By similarity
	Metal binding	287	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	581	1	Manganese 2 By similarity
	Metal binding	644	1	Manganese 2 By similarity
Amino acid modifications
	Modified residue	125	1	Phosphoserine Ref.6
	Modified residue	172	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	368	1	S → G in AAM61450. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9LQN6 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B1A3670D06B1B94E	FASTA	662	74,274
	10 20 30 40 50 60 MGNGVTKLSI CFTGGGGERL RPKDISVLLP DPLDEGLGHS FCYVRPDPTL ISSSKVHSEE 70 80 90 100 110 120 DTTTTTFRTI SGASVSANTA TPLSTSLYDP YGHIDRAAAF ESTTSFSSIP LQPIPKSSGP 130 140 150 160 170 180 IVLGSGPIER GFLSGPIERG FMSGPLDRVG LFSGPLDKPN SDHHHQFQRS FSHGLALRVG 190 200 210 220 230 240 SRKRSLVRIL RRAISKTMSR GQNSIVAPIK SVKDSDNWGI RSEKSRNLHN ENLTVNSLNF 250 260 270 280 290 300 SSEVSLDDDV SLENQNLQWA QGKAGEDRVH VVVSEEHGWL FVGIYDGFNG PDAPDYLLSH 310 320 330 340 350 360 LYPVVHRELK GLLWDDSNVE SKSQDLERSN GDESCSNQEK DETCERWWRC EWDRESQDLD 370 380 390 400 410 420 RRLKEQISRR SGSDRLTNHS EVLEALSQAL RKTEEAYLDT ADKMLDENPE LALMGSCVLV 430 440 450 460 470 480 MLMKGEDIYV MNVGDSRAVL GQKSEPDYWL AKIRQDLERI NEETMMNDLE GCEGDQSSLV 490 500 510 520 530 540 PNLSAFQLTV DHSTNIEEEV ERIRNEHPDD VTAVTNERVK GSLKVTRAFG AGFLKQPKWN 550 560 570 580 590 600 NALLEMFQID YVGKSPYINC LPSLYHHRLG SKDRFLILSS DGLYQYFTNE EAVSEVELFI 610 620 630 640 650 660 TLQPEGDPAQ HLVQELLFRA AKKAGMDFHE LLEIPQGERR RYHDDVSIVV ISLEGRMWKS CV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. , 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.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"POL and related phosphatases are dosage-sensitive regulators of meristem and organ development in Arabidopsis." Song S.-K., Clark S.E. Dev. Biol. 285:272-284(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, DISRUPTION PHENOTYPE.
[6]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, MASS SPECTROMETRY. Strain: cv. Columbia.
[7]	"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.
[8]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC007583 Genomic DNA. Translation: AAF75095.1. CP002684 Genomic DNA. Translation: AEE28151.1. AF361615 mRNA. Translation: AAK32783.1. Frameshift. AY133603 mRNA. Translation: AAM91433.1. Frameshift. AY084887 mRNA. Translation: AAM61450.1.
IPI	IPI00532446.
PIR	G86210.
RefSeq	NP_563791.1. NM_100636.2.
UniGene	At.43724. At.72523.
3D structure databases
ProteinModelPortal	Q9LQN6.
SMR	Q9LQN6. Positions 281-656.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G07630.1; AT1G07630.1; AT1G07630.
GeneID	837276.
KEGG	ath:AT1G07630.
Organism-specific databases
TAIR	At1g07630.
Phylogenomic databases
eggNOG	COG0631.
HOGENOM	HOG000239375.
InParanoid	Q9LQN6.
OMA	TTPEGDP.
PhylomeDB	Q9LQN6.
ProtClustDB	CLSN2683691.
Gene expression databases
Genevestigator	Q9LQN6.
Family and domain databases
Gene3D	3.60.40.10. 3 hits.
InterPro	IPR001932. PP2C-like. IPR015655. Protein_Pase_2C. [Graphical view]
PANTHER	PTHR13832. PTHR13832. 1 hit.
Pfam	PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00332. PP2Cc. 1 hit. [Graphical view]
SUPFAM	SSF81606. PP2C-related. 1 hit.
PROSITE	PS01032. PP2C. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P2C04_ARATH

Accession

Primary (citable) accession number: Q9LQN6
Secondary accession number(s): Q8LFF0, Q9ASX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program