ID P2C17_ARATH Reviewed; 283 AA. AC Q8L7I4; Q94AE3; Q9C9R2; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=Probable protein phosphatase 2C 17; DE Short=AtPP2C17; DE EC=3.1.3.16; GN OrderedLocusNames=At1g78200; ORFNames=T11I11.14; 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=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=19423640; DOI=10.1093/dnares/dsp009; RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., RA Shinozaki K.; RT "Analysis of multiple occurrences of alternative splicing events in RT Arabidopsis thaliana using novel sequenced full-length cDNAs."; RL DNA Res. 16:155-164(2009). RN [5] 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 -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG52101.1; Type=Erroneous gene model prediction; 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; AC012680; AAG52101.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002684; AEE36080.1; -; Genomic_DNA. DR EMBL; CP002684; AEE36081.1; -; Genomic_DNA. DR EMBL; CP002684; ANM60992.1; -; Genomic_DNA. DR EMBL; AY048244; AAK82506.1; -; mRNA. DR EMBL; AY133563; AAM91393.1; -; mRNA. DR EMBL; AK317294; BAH19970.1; -; mRNA. DR PIR; D96811; D96811. DR RefSeq; NP_001323236.1; NM_001334823.1. DR RefSeq; NP_001323237.1; NM_001334822.1. DR RefSeq; NP_001323238.1; NM_001334821.1. DR RefSeq; NP_565172.1; NM_106470.3. DR RefSeq; NP_974168.1; NM_202439.3. DR AlphaFoldDB; Q8L7I4; -. DR SMR; Q8L7I4; -. DR iPTMnet; Q8L7I4; -. DR PaxDb; 3702-AT1G78200-2; -. DR ProteomicsDB; 248873; -. DR EnsemblPlants; AT1G78200.1; AT1G78200.1; AT1G78200. DR EnsemblPlants; AT1G78200.2; AT1G78200.2; AT1G78200. DR EnsemblPlants; AT1G78200.3; AT1G78200.3; AT1G78200. DR GeneID; 844156; -. DR Gramene; AT1G78200.1; AT1G78200.1; AT1G78200. DR Gramene; AT1G78200.2; AT1G78200.2; AT1G78200. DR Gramene; AT1G78200.3; AT1G78200.3; AT1G78200. DR KEGG; ath:AT1G78200; -. DR Araport; AT1G78200; -. DR TAIR; AT1G78200; -. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_013173_0_1_1; -. DR InParanoid; Q8L7I4; -. DR OMA; MPKICCS; -. DR OrthoDB; 11028at2759; -. DR PhylomeDB; Q8L7I4; -. DR PRO; PR:Q8L7I4; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q8L7I4; baseline and differential. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. 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:SF36; PPM-TYPE PHOSPHATASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS51746; PPM_2; 1. DR Genevisible; Q8L7I4; AT. PE 2: Evidence at transcript level; KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase; KW Reference proteome. FT CHAIN 1..283 FT /note="Probable protein phosphatase 2C 17" FT /id="PRO_0000367947" FT DOMAIN 32..282 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT BINDING 69 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 70 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 234 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 273 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT CONFLICT 198..200 FT /note="VSR -> ISS (in Ref. 3; AAK82506)" FT /evidence="ECO:0000305" FT CONFLICT 229..231 FT /note="LIL -> IIM (in Ref. 3; AAK82506)" FT /evidence="ECO:0000305" SQ SEQUENCE 283 AA; 30854 MW; 576000E070123F3E CRC64; MPKICCSRSA TQVVVAQKSN SGKGRNGEGG IKYGFSLIKG KSNHSMEDYH VAKFTNFNGN ELGLFAIFDG HKGDHVAAYL QKHLFSNILK DGEFLVDPRR AIAKAYENTD QKILADNRTD LESGGSTAVT AILINGKALW IANVGDSRAI VSSRGKAKQM SVDHDPDDDT ERSMIESKGG FVTNRPGDVP RVNGLLAVSR VFGDKNLKAY LNSEPEIKDV TIDSHTDFLI LASDGISKVM SNQEAVDVAK KLKDPKEAAR QVVAEALKRN SKDDISCIVV RFR //