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P46014 (P2C70_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. 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 70

Short name=AtPP2C70
EC=3.1.3.16
Alternative name(s):
Kinase-associated protein phosphatase
Gene names
Name:KAPP
Ordered Locus Names:At5g19280
ORF Names:F7K24.30, T24G5.3
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dephosphorylates the Ser/Thr receptor-like kinase RLK5. May function as a signaling component in a pathway involving RLK5.

Catalytic activity

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

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Subunit structure

Association of RLK5 with kapp domain is dependent on phosphorylation of RLK5 and can be abolished by dephosphorylation. Interacts with SERK1 and CDC48A. Component of the SERK1 signaling complex, composed of KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1 and BRI1. Ref.6

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in all tissues examined.

Sequence similarities

Contains 1 FHA domain.

Contains 1 PP2C-like domain.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CLV1Q9SYQ86EBI-1646157,EBI-1646111
CRK6Q9C5S94EBI-1646157,EBI-2023993
KIK1O499743EBI-1646157,EBI-2015790From a different organism.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: P46014-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 581581Protein phosphatase 2C 70
PRO_0000057780

Regions

Topological domain1 – 77Extracellular Potential
Transmembrane8 – 2821Helical; Potential
Topological domain29 – 581553Cytoplasmic Potential
Domain208 – 25952FHA
Domain289 – 581293PP2C-like

Sites

Metal binding3461Manganese 1 By similarity
Metal binding3461Manganese 2 By similarity
Metal binding3471Manganese 1; via carbonyl oxygen By similarity
Metal binding5211Manganese 2 By similarity
Metal binding5681Manganese 2 By similarity

Secondary structure

....................... 581
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1997. Version 2.
Checksum: EE0C2A41E55E100D

FASTA58164,911
        10         20         30         40         50         60 
MAMIGMNIIG LFMVLMLLLI SLIILFACKP WRYFSRFRSS SRFSSTFKVG DLQRPLISDD 

        70         80         90        100        110        120 
GNLIQGQTSE VTREYDLEGA CYQNDGLLHS SLTEGRFYKQ RLPSSSPHFS QGESFVLEVI 

       130        140        150        160        170        180 
SEPSDNALVG QTLKLPAEKG SLAEVQTYDW QNNRNENLQY NLEKDRLINL SPRLVEDQRS 

       190        200        210        220        230        240 
WLFLEVIAGP AIGLQHAVNS TSSSKLPVKL GRVSPSDLAL KDSEVSGKHA QITWNSTKFK 

       250        260        270        280        290        300 
WELVDMGSLN GTLVNSHSIS HPDLGSRKWG NPVELASDDI ITLGTTTKVY VRISSQNEFQ 

       310        320        330        340        350        360 
IPFKIGVASD PMAMRRGGRK LPMEDVCHYK WPLPGANKFG LFCVCDGHGG SGAAQSAIKI 

       370        380        390        400        410        420 
IPEVLANILS DSLRKEKVLS KRDASDVLRD MFAKTEARLE EHQYEGCTAT VLLVWKDNEE 

       430        440        450        460        470        480 
NFFAQCANLG DSACVIHLGG RYIQMTEDHR VVSLSERKRF QEAGLALRDG ETRLFGINLA 

       490        500        510        520        530        540 
RMLGDKFPKQ QDSRFSAEPY ISEPLRIDQS SKDVFAVLAS DGLWDVVSPK KAVQLVLQMR 

       550        560        570        580 
DKERGRESSA EKIANGLLNE ARAMRTKDNT SIIYLDFDTS L 

« Hide

References

« Hide 'large scale' references
[1]"Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase."
Stone J.M., Collinge M.A., Smith R.D., Horn M.A., Walker J.C.
Science 266:793-795(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Stone J.M.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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. expand/collapse author list , 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.
[6]"The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP."
Rienties I.M., Vink J., Borst J.W., Russinova E., de Vries S.C.
Planta 221:394-405(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SERK1 AND CDC48A, IDENTIFICATION IN THE SERK1 COMPLEX.
[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]"NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase."
Lee G.I., Ding Z., Walker J.C., Van Doren S.R.
Proc. Natl. Acad. Sci. U.S.A. 100:11261-11266(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 175-313.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09505 mRNA. Translation: AAB38148.1.
AC069326 Genomic DNA. No translation available.
AF296837 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92679.1.
AY045853 mRNA. Translation: AAK76527.1.
AY117152 mRNA. Translation: AAM51227.1.
PIRA55174.
RefSeqNP_197429.1. NM_121933.3.
UniGeneAt.10199.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MZKNMR-A180-313[»]
ProteinModelPortalP46014.
SMRP46014. Positions 180-298, 305-579.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17324. 11 interactions.
IntActP46014. 12 interactions.
MINTMINT-98609.
STRING3702.AT5G19280.2-P.

Proteomic databases

PaxDbP46014.
PRIDEP46014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G19280.1; AT5G19280.1; AT5G19280. [P46014-1]
GeneID832048.
KEGGath:AT5G19280.

Organism-specific databases

TAIRAT5G19280.

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000240507.
InParanoidP46014.
KOK01090.
PhylomeDBP46014.
ProtClustDBCLSN2686769.

Enzyme and pathway databases

BioCycARA:AT5G19280-MONOMER.
ARA:GQT-2080-MONOMER.

Gene expression databases

ArrayExpressP46014.
GenevestigatorP46014.

Family and domain databases

Gene3D2.60.200.20. 1 hit.
3.60.40.10. 1 hit.
InterProIPR000253. FHA_dom.
IPR016660. Kinase_assoc_Pase.
IPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00498. FHA. 1 hit.
PF00481. PP2C. 1 hit.
[Graphical view]
PIRSFPIRSF016465. Kap_phosphatase. 1 hit.
SMARTSM00240. FHA. 1 hit.
SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEPS50006. FHA_DOMAIN. 1 hit.
PS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP46014.

Entry information

Entry nameP2C70_ARATH
AccessionPrimary (citable) accession number: P46014
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 137 of the entry and version 2 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