P46014 (P2C70_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	581 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein dephosphorylation Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CLV1	Q9SYQ8	6	EBI-1646157,EBI-1646111
CRK6	Q9C5S9	4	EBI-1646157,EBI-2023993
KIK1	O49974	3	EBI-1646157,EBI-2015790	From 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 581

581

Protein phosphatase 2C 70

PRO_0000057780

Regions

Topological domain

1 – 7

7

Extracellular Potential

Transmembrane

8 – 28

21

Helical; Potential

Topological domain

29 – 581

553

Cytoplasmic Potential

Domain

208 – 259

52

FHA

Domain

289 – 581

293

PP2C-like

Sites

Metal binding

346

1

Manganese 1 By similarity

Metal binding

346

1

Manganese 2 By similarity

Metal binding

347

1

Manganese 1; via carbonyl oxygen By similarity

Metal binding

521

1

Manganese 2 By similarity

Metal binding

568

1

Manganese 2 By similarity

Secondary structure

1

.

.

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.

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581

Helix Strand Turn

Details...

Beta strand

180 – 186

7

Beta strand

195 – 198

4

Beta strand

207 – 215

9

Beta strand

217 – 219

3

Beta strand

225 – 235

11

Turn

236 – 239

4

Beta strand

240 – 245

6

Beta strand

257 – 260

4

Turn

264 – 266

3

Beta strand

279 – 282

4

Beta strand

284 – 286

3

Beta strand

288 – 295

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: EE0C2A41E55E100D	FASTA	581	64,911
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.

IPI

IPI00532527.

PIR

A55174.

RefSeq

NP_197429.1. NM_121933.3.

UniGene

At.10199.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MZK	NMR	-	A	180-313	[»]

ProteinModelPortal

P46014.

SMR

P46014. Positions 180-298, 341-577.

ModBase

Search...

Protein-protein interaction databases

IntAct

P46014. 12 interactions.

MINT

MINT-98609.

STRING

3702.AT5G19280.2-P.

Proteomic databases

PaxDb

P46014.

PRIDE

P46014.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G19280.1; AT5G19280.1; AT5G19280.

GeneID

832048.

KEGG

ath:AT5G19280.

Organism-specific databases

TAIR

At5g19280.

Phylogenomic databases

eggNOG

COG0631.

HOGENOM

HOG000240507.

InParanoid

P46014.

KO

K01090.

PhylomeDB

P46014.

ProtClustDB

CLSN2686769.

Gene expression databases

ArrayExpress

P46014.

Genevestigator

P46014.

GermOnline

AT5G19280. Arabidopsis thaliana.

Family and domain databases

Gene3D

2.60.200.20. 1 hit.
3.60.40.10. 1 hit.

InterPro

IPR000253. FHA_dom.
IPR016660. Kinase_assoc_Pase.
IPR001932. PP2C-like.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
IPR008984. SMAD_FHA_domain.
[Graphical view]

PANTHER

PTHR13832. PTHR13832. 1 hit.

Pfam

PF00498. FHA. 1 hit.
PF00481. PP2C. 1 hit.
[Graphical view]

PIRSF

PIRSF016465. Kap_phosphatase. 1 hit.

SMART

SM00240. FHA. 1 hit.
SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]

SUPFAM

SSF81606. PP2C-related. 1 hit.
SSF49879. SMAD_FHA. 1 hit.

PROSITE

PS50006. FHA_DOMAIN. 1 hit.
PS01032. PP2C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P46014.

Entry information

Entry name

P2C70_ARATH

Accession

Primary (citable) accession number: P46014

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program