ID P2C51_ARATH Reviewed; 528 AA. AC Q93YS2; F4J0Z1; F4J0Z2; Q9M1V6; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 2. DT 24-JAN-2024, entry version 126. DE RecName: Full=Probable protein phosphatase 2C 51; DE Short=AtPP2C51; DE EC=3.1.3.16; GN OrderedLocusNames=At3g63340; ORFNames=F16M2.190, MAA21.3; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(2000). RN [2] 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 [3] 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 [4] 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). 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. 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=Q93YS2-1; Sequence=Displayed; CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AEE80468.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At3g63330 and At3g63340.; Evidence={ECO:0000305}; CC Sequence=AEE80469.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At3g63330 and At3g63340.; Evidence={ECO:0000305}; CC Sequence=CAB86435.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At3g63330 and At3g63340.; Evidence={ECO:0000305}; 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; AL138648; CAB86435.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002686; AEE80468.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002686; AEE80469.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002686; ANM64224.1; -; Genomic_DNA. DR EMBL; AY059789; AAL24137.1; -; mRNA. DR PIR; T48123; T48123. DR RefSeq; NP_001326269.1; NM_001340203.1. [Q93YS2-1] DR AlphaFoldDB; Q93YS2; -. DR SMR; Q93YS2; -. DR STRING; 3702.Q93YS2; -. DR PaxDb; 3702-AT3G63340-2; -. DR ProteomicsDB; 248719; -. [Q93YS2-1] DR EnsemblPlants; AT3G63340.12; AT3G63340.12; AT3G63340. [Q93YS2-1] DR GeneID; 825509; -. DR Gramene; AT3G63340.12; AT3G63340.12; AT3G63340. [Q93YS2-1] DR KEGG; ath:AT3G63340; -. DR Araport; AT3G63340; -. DR TAIR; AT3G63340; -. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_012110_0_0_1; -. DR InParanoid; Q93YS2; -. DR PhylomeDB; Q93YS2; -. DR PRO; PR:Q93YS2; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q93YS2; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. 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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR47992:SF26; PROTEIN PHOSPHATASE 2C 50-RELATED; 1. DR Pfam; PF00481; PP2C; 2. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS51746; PPM_2; 1. DR Genevisible; Q93YS2; AT. PE 2: Evidence at transcript level; KW Alternative splicing; Hydrolase; Magnesium; Manganese; Membrane; KW Metal-binding; Protein phosphatase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..528 FT /note="Probable protein phosphatase 2C 51" FT /id="PRO_0000367975" FT TRANSMEM 8..28 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 71..445 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT BINDING 117 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 117 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 118 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 385 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 436 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT CONFLICT 199 FT /note="D -> G (in Ref. 3; AAL24137)" FT /evidence="ECO:0000305" SQ SEQUENCE 528 AA; 58354 MW; 803DF76D1D45ADE5 CRC64; MTSSIKSSLL NLGLLIIFFV FFFLVINCRG ESSTCLAVYK QGGAPAVFQS PKCPRWILQN WGSPTHSGAG RCHTAAIQGR RNYQEDRLLC ALDLRIPFPG KTGTPKDVLV GIAAVFDGHN GAEASDMASK LLLDYFALHI NFLLDATFSA MTRKLIGRFP TKGDHSVILH GVSRDEIMHL YNLDFQMQFR DSLPLHFDDS LPLDIMKEAL LRAIHDIDVT FTKEASNRKL NSGSTATIAL IADGQLMVAS IGDSKALLCS EKFETLEEAR ATLVKLYRER RRNRGSSPSR FSDFKLEHGN GLLRFIAKEL TKDHHPNRED EKIRVEAAGG YVTEWAGVPR VNGQLTVSRA IGDLTYRSYG VISAPEVMDW QPLVANDSFL VVSSDGIFEK LEVQEVCDLL WEVNNQTSSG AGVPSYCSIS LADCLVNTAF EKGSMDNMAA VVVPLKSNLV TQLQRKEQSM NDNKDKIASA LPCSNCTLPL PNDINLGPLQ LKQAQPLGTM FNRLLRLKTE VFAAFICQRT LLGHLKGK //