Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P46014

- P2C70_ARATH

UniProt

P46014 - P2C70_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein phosphatase 2C 70

Gene

KAPP

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi346 – 3461Manganese 1By similarity
Metal bindingi346 – 3461Manganese 2By similarity
Metal bindingi347 – 3471Manganese 1; via carbonyl oxygenBy similarity
Metal bindingi521 – 5211Manganese 2By similarity
Metal bindingi568 – 5681Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein serine/threonine phosphatase activity Source: InterPro

GO - Biological processi

  1. protein dephosphorylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 2C 70 (EC:3.1.3.16)
Short name:
AtPP2C70
Alternative name(s):
Kinase-associated protein phosphatase
Gene namesi
Name:KAPP
Ordered Locus Names:At5g19280
ORF Names:F7K24.30, T24G5.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G19280.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77ExtracellularSequence Analysis
Transmembranei8 – 2821HelicalSequence AnalysisAdd
BLAST
Topological domaini29 – 581553CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 581581Protein phosphatase 2C 70PRO_0000057780Add
BLAST

Proteomic databases

PaxDbiP46014.
PRIDEiP46014.

Expressioni

Tissue specificityi

Expressed in all tissues examined.

Gene expression databases

ExpressionAtlasiP46014. baseline and differential.
GenevestigatoriP46014.

Interactioni

Subunit structurei

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 BRI1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CLV1Q9SYQ86EBI-1646157,EBI-1646111
CRK6Q9C5S94EBI-1646157,EBI-2023993
KIK1O499743EBI-1646157,EBI-2015790From a different organism.

Protein-protein interaction databases

BioGridi17324. 11 interactions.
IntActiP46014. 12 interactions.
MINTiMINT-98609.
STRINGi3702.AT5G19280.2-P.

Structurei

Secondary structure

1
581
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi180 – 1867Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi207 – 2159Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi225 – 23511Combined sources
Turni236 – 2394Combined sources
Beta strandi240 – 2456Combined sources
Beta strandi257 – 2604Combined sources
Turni264 – 2663Combined sources
Beta strandi279 – 2824Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi288 – 2958Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MZKNMR-A180-313[»]
ProteinModelPortaliP46014.
SMRiP46014. Positions 180-298, 335-577.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46014.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini208 – 25952FHAPROSITE-ProRule annotationAdd
BLAST
Domaini289 – 581293PP2C-likeAdd
BLAST

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation
Contains 1 PP2C-like domain.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000240507.
InParanoidiP46014.
KOiK01090.
PhylomeDBiP46014.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.60.40.10. 1 hit.
InterProiIPR000253. 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]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00498. FHA. 1 hit.
PF00481. PP2C. 1 hit.
[Graphical view]
PIRSFiPIRSF016465. Kap_phosphatase. 1 hit.
SMARTiSM00240. FHA. 1 hit.
SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS01032. PP2C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P46014-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAMIGMNIIG LFMVLMLLLI SLIILFACKP WRYFSRFRSS SRFSSTFKVG
60 70 80 90 100
DLQRPLISDD GNLIQGQTSE VTREYDLEGA CYQNDGLLHS SLTEGRFYKQ
110 120 130 140 150
RLPSSSPHFS QGESFVLEVI SEPSDNALVG QTLKLPAEKG SLAEVQTYDW
160 170 180 190 200
QNNRNENLQY NLEKDRLINL SPRLVEDQRS WLFLEVIAGP AIGLQHAVNS
210 220 230 240 250
TSSSKLPVKL GRVSPSDLAL KDSEVSGKHA QITWNSTKFK WELVDMGSLN
260 270 280 290 300
GTLVNSHSIS HPDLGSRKWG NPVELASDDI ITLGTTTKVY VRISSQNEFQ
310 320 330 340 350
IPFKIGVASD PMAMRRGGRK LPMEDVCHYK WPLPGANKFG LFCVCDGHGG
360 370 380 390 400
SGAAQSAIKI IPEVLANILS DSLRKEKVLS KRDASDVLRD MFAKTEARLE
410 420 430 440 450
EHQYEGCTAT VLLVWKDNEE NFFAQCANLG DSACVIHLGG RYIQMTEDHR
460 470 480 490 500
VVSLSERKRF QEAGLALRDG ETRLFGINLA RMLGDKFPKQ QDSRFSAEPY
510 520 530 540 550
ISEPLRIDQS SKDVFAVLAS DGLWDVVSPK KAVQLVLQMR DKERGRESSA
560 570 580
EKIANGLLNE ARAMRTKDNT SIIYLDFDTS L
Length:581
Mass (Da):64,911
Last modified:November 1, 1997 - v2
Checksum:iEE0C2A41E55E100D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA55174.
RefSeqiNP_197429.1. NM_121933.3. [P46014-1]
UniGeneiAt.10199.

Genome annotation databases

EnsemblPlantsiAT5G19280.1; AT5G19280.1; AT5G19280. [P46014-1]
GeneIDi832048.
KEGGiath:AT5G19280.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi A55174.
RefSeqi NP_197429.1. NM_121933.3. [P46014-1 ]
UniGenei At.10199.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MZK NMR - A 180-313 [» ]
ProteinModelPortali P46014.
SMRi P46014. Positions 180-298, 335-577.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 17324. 11 interactions.
IntActi P46014. 12 interactions.
MINTi MINT-98609.
STRINGi 3702.AT5G19280.2-P.

Proteomic databases

PaxDbi P46014.
PRIDEi P46014.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G19280.1 ; AT5G19280.1 ; AT5G19280 . [P46014-1 ]
GeneIDi 832048.
KEGGi ath:AT5G19280.

Organism-specific databases

TAIRi AT5G19280.

Phylogenomic databases

eggNOGi COG0631.
HOGENOMi HOG000240507.
InParanoidi P46014.
KOi K01090.
PhylomeDBi P46014.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTracei P46014.

Gene expression databases

ExpressionAtlasi P46014. baseline and differential.
Genevestigatori P46014.

Family and domain databases

Gene3Di 2.60.200.20. 1 hit.
3.60.40.10. 1 hit.
InterProi IPR000253. 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 ]
PANTHERi PTHR13832. PTHR13832. 1 hit.
Pfami PF00498. FHA. 1 hit.
PF00481. PP2C. 1 hit.
[Graphical view ]
PIRSFi PIRSF016465. Kap_phosphatase. 1 hit.
SMARTi SM00240. FHA. 1 hit.
SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEi PS50006. FHA_DOMAIN. 1 hit.
PS01032. PP2C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiP2C70_ARATH
AccessioniPrimary (citable) accession number: P46014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3