P2C70_ARATH
ID P2C70_ARATH Reviewed; 581 AA.
AC P46014;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Protein phosphatase 2C 70;
DE Short=AtPP2C70;
DE EC=3.1.3.16;
DE AltName: Full=Kinase-associated protein phosphatase {ECO:0000303|PubMed:7973632};
DE AltName: Full=Protein ROOT ATTENUATED GROWTH 1 {ECO:0000303|PubMed:18162596};
GN Name=KAPP {ECO:0000303|PubMed:7973632};
GN Synonyms=RAG1 {ECO:0000303|PubMed:18162596}; OrderedLocusNames=At5g19280;
GN ORFNames=F7K24.30, T24G5.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7973632; DOI=10.1126/science.7973632;
RA Stone J.M., Collinge M.A., Smith R.D., Horn M.A., Walker J.C.;
RT "Interaction of a protein phosphatase with an Arabidopsis serine-threonine
RT receptor kinase.";
RL Science 266:793-795(1994).
RN [2]
RP SEQUENCE REVISION.
RA Stone J.M.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, AND INTERACTION WITH CVL1.
RX PubMed=9294234; DOI=10.1073/pnas.94.19.10467;
RA Williams R.W., Wilson J.M., Meyerowitz E.M.;
RT "A possible role for kinase-associated protein phosphatase in the
RT Arabidopsis CLAVATA1 signaling pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:10467-10472(1997).
RN [7]
RP FUNCTION, AND INTERACTION WITH CVL1.
RX PubMed=9701578; DOI=10.1104/pp.117.4.1217;
RA Stone J.M., Trotochaud A.E., Walker J.C., Clark S.E.;
RT "Control of meristem development by CLAVATA1 receptor kinase and kinase-
RT associated protein phosphatase interactions.";
RL Plant Physiol. 117:1217-1225(1998).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12101128; DOI=10.1101/gad.220402;
RA Shah K., Russinova E., Gadella T.W. Jr., Willemse J., de Vries S.C.;
RT "The Arabidopsis kinase-associated protein phosphatase controls
RT internalization of the somatic embryogenesis receptor kinase 1.";
RL Genes Dev. 16:1707-1720(2002).
RN [9]
RP FUNCTION, INTERACTION WITH SERK1 AND CDC48A, AND IDENTIFICATION IN THE
RP SERK1 COMPLEX.
RX PubMed=15592873; DOI=10.1007/s00425-004-1447-7;
RA Rienties I.M., Vink J., Borst J.W., Russinova E., de Vries S.C.;
RT "The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the
RT 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP.";
RL Planta 221:394-405(2005).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT Arabidopsis.";
RL BMC Genomics 9:550-550(2008).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18162596; DOI=10.1104/pp.107.109009;
RA Manabe Y., Bressan R.A., Wang T., Li F., Koiwa H., Sokolchik I., Li X.,
RA Maggio A.;
RT "The Arabidopsis kinase-associated protein phosphatase regulates adaptation
RT to Na+ stress.";
RL Plant Physiol. 146:612-622(2008).
RN [12]
RP STRUCTURE BY NMR OF 175-313.
RX PubMed=14500786; DOI=10.1073/pnas.2031918100;
RA Lee G.I., Ding Z., Walker J.C., Van Doren S.R.;
RT "NMR structure of the forkhead-associated domain from the Arabidopsis
RT receptor kinase-associated protein phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11261-11266(2003).
CC -!- FUNCTION: Dephosphorylates the Ser/Thr receptor-like kinase RLK5. May
CC function as a signaling component in a pathway involving RLK5
CC (PubMed:15592873). Binds and dephosphorylates CLAVATA1 (CLV1).
CC Functions as a negative regulator of the CLV1 signaling in plant
CC development (PubMed:9294234, PubMed:9701578). Dephosphorylates SERK1
CC receptor kinase on threonine residues in the A-loop. Dephosphorylation
CC of SERK1 controls SERK1 internalization (PubMed:12101128). Component of
CC a signaling pathway which mediates adaptation to NaCl stress. Is not a
CC component of the SALT OVERLY SENSITIVE (SOS) pathway (PubMed:18162596).
CC {ECO:0000269|PubMed:12101128, ECO:0000269|PubMed:15592873,
CC ECO:0000269|PubMed:18162596, ECO:0000269|PubMed:9294234,
CC ECO:0000269|PubMed:9701578}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Association of RLK5 with kapp domain is dependent on
CC phosphorylation of RLK5 and can be abolished by dephosphorylation.
CC Interacts with SERK1 and CDC48A. Component of the SERK1 signaling
CC complex, composed of KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2,
CC SERK3/BAK1 and BRI1 (PubMed:15592873). Interacts with CLV1
CC (PubMed:9294234, PubMed:9701578). {ECO:0000269|PubMed:15592873,
CC ECO:0000269|PubMed:9294234, ECO:0000269|PubMed:9701578}.
CC -!- INTERACTION:
CC P46014; Q9SYQ8: CLV1; NbExp=6; IntAct=EBI-1646157, EBI-1646111;
CC P46014; Q9C5S9: CRK6; NbExp=2; IntAct=EBI-1646157, EBI-2023993;
CC P46014; O49974: KIK1; Xeno; NbExp=3; IntAct=EBI-1646157, EBI-2015790;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12101128};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P46014-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedlings show increased sensitivity of roots to
CC salt stress. {ECO:0000269|PubMed:18162596}.
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DR EMBL; U09505; AAB38148.1; -; mRNA.
DR EMBL; AC069326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF296837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92679.1; -; Genomic_DNA.
DR EMBL; AY045853; AAK76527.1; -; mRNA.
DR EMBL; AY117152; AAM51227.1; -; mRNA.
DR PIR; A55174; A55174.
DR RefSeq; NP_197429.1; NM_121933.4. [P46014-1]
DR PDB; 1MZK; NMR; -; A=180-313.
DR PDBsum; 1MZK; -.
DR AlphaFoldDB; P46014; -.
DR BMRB; P46014; -.
DR SMR; P46014; -.
DR BioGRID; 17324; 13.
DR IntAct; P46014; 15.
DR STRING; 3702.AT5G19280.2; -.
DR iPTMnet; P46014; -.
DR PaxDb; P46014; -.
DR PRIDE; P46014; -.
DR ProteomicsDB; 250913; -. [P46014-1]
DR EnsemblPlants; AT5G19280.1; AT5G19280.1; AT5G19280. [P46014-1]
DR GeneID; 832048; -.
DR Gramene; AT5G19280.1; AT5G19280.1; AT5G19280. [P46014-1]
DR KEGG; ath:AT5G19280; -.
DR Araport; AT5G19280; -.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_033671_0_0_1; -.
DR InParanoid; P46014; -.
DR OMA; WDVISVK; -.
DR PhylomeDB; P46014; -.
DR EvolutionaryTrace; P46014; -.
DR PRO; PR:P46014; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P46014; baseline and differential.
DR Genevisible; P46014; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0050408; F:[pyruvate kinase]-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00060; FHA; 1.
DR CDD; cd00143; PP2Cc; 1.
DR DisProt; DP01355; -.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR016660; Kinase_assoc_Pase.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00481; PP2C; 1.
DR PIRSF; PIRSF016465; Kap_phosphatase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Hydrolase; Magnesium;
KW Manganese; Membrane; Metal-binding; Protein phosphatase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..581
FT /note="Protein phosphatase 2C 70"
FT /id="PRO_0000057780"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 208..259
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 304..577
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 346
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 521
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 568
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:1MZK"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1MZK"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:1MZK"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1MZK"
FT STRAND 225..235
FT /evidence="ECO:0007829|PDB:1MZK"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:1MZK"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:1MZK"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:1MZK"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:1MZK"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1MZK"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1MZK"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:1MZK"
SQ SEQUENCE 581 AA; 64911 MW; EE0C2A41E55E100D CRC64;
MAMIGMNIIG LFMVLMLLLI SLIILFACKP WRYFSRFRSS SRFSSTFKVG DLQRPLISDD
GNLIQGQTSE VTREYDLEGA CYQNDGLLHS SLTEGRFYKQ RLPSSSPHFS QGESFVLEVI
SEPSDNALVG QTLKLPAEKG SLAEVQTYDW QNNRNENLQY NLEKDRLINL SPRLVEDQRS
WLFLEVIAGP AIGLQHAVNS TSSSKLPVKL GRVSPSDLAL KDSEVSGKHA QITWNSTKFK
WELVDMGSLN GTLVNSHSIS HPDLGSRKWG NPVELASDDI ITLGTTTKVY VRISSQNEFQ
IPFKIGVASD PMAMRRGGRK LPMEDVCHYK WPLPGANKFG LFCVCDGHGG SGAAQSAIKI
IPEVLANILS DSLRKEKVLS KRDASDVLRD MFAKTEARLE EHQYEGCTAT VLLVWKDNEE
NFFAQCANLG DSACVIHLGG RYIQMTEDHR VVSLSERKRF QEAGLALRDG ETRLFGINLA
RMLGDKFPKQ QDSRFSAEPY ISEPLRIDQS SKDVFAVLAS DGLWDVVSPK KAVQLVLQMR
DKERGRESSA EKIANGLLNE ARAMRTKDNT SIIYLDFDTS L
