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 27-MAR-2024, entry version 197. 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}; GN OrderedLocusNames=At5g19280; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.P46014; -. DR iPTMnet; P46014; -. DR PaxDb; 3702-AT5G19280-2; -. 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 TAIR; AT5G19280; KAPP. 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 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 CDD; cd22678; FHA_PP2C70-like; 1. DR CDD; cd00143; PP2Cc; 1. DR DisProt; DP01355; -. DR Gene3D; 2.60.200.20; -; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 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-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1. DR PANTHER; PTHR13832:SF643; PROTEIN PHOSPHATASE 2C 70; 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; SSF81606; PP2C-like; 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. DR PROSITE; PS01032; PPM_1; 1. DR PROSITE; PS51746; PPM_2; 1. DR Genevisible; P46014; AT. 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 //