ID P2C13_ARATH Reviewed; 383 AA. AC Q9LNF4; Q67XZ2; Q67ZV7; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 2. DT 27-MAR-2024, entry version 136. DE RecName: Full=Probable protein phosphatase 2C 13; DE Short=AtPP2C13; DE EC=3.1.3.16; GN OrderedLocusNames=At1g48040; ORFNames=F21D18.27, T2J15.5; 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; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-383. RC STRAIN=cv. Columbia; RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.; RT "Arabidopsis ORF clones."; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. 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=AAF79528.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAG51521.1; Type=Erroneous initiation; 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; AC023673; AAF79528.1; ALT_INIT; Genomic_DNA. DR EMBL; AC051631; AAG51521.1; ALT_INIT; Genomic_DNA. DR EMBL; CP002684; AEE32241.1; -; Genomic_DNA. DR EMBL; AK176010; BAD43773.1; -; mRNA. DR EMBL; AK176676; BAD44439.1; -; mRNA. DR EMBL; BT015400; AAU05523.1; -; mRNA. DR RefSeq; NP_175238.2; NM_103700.4. DR AlphaFoldDB; Q9LNF4; -. DR SMR; Q9LNF4; -. DR BioGRID; 26447; 9. DR IntAct; Q9LNF4; 9. DR iPTMnet; Q9LNF4; -. DR PaxDb; 3702-AT1G48040-1; -. DR ProteomicsDB; 248701; -. DR EnsemblPlants; AT1G48040.1; AT1G48040.1; AT1G48040. DR GeneID; 841222; -. DR Gramene; AT1G48040.1; AT1G48040.1; AT1G48040. DR KEGG; ath:AT1G48040; -. DR Araport; AT1G48040; -. DR TAIR; AT1G48040; -. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_013173_21_0_1; -. DR InParanoid; Q9LNF4; -. DR OMA; ICQQSIP; -. DR OrthoDB; 91820at2759; -. DR PhylomeDB; Q9LNF4; -. DR PRO; PR:Q9LNF4; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9LNF4; baseline and differential. 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; IPR000222; PP2C_BS. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1. DR PANTHER; PTHR13832:SF620; PROTEIN PHOSPHATASE 2C 13-RELATED; 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; PS01032; PPM_1; 1. DR PROSITE; PS51746; PPM_2; 1. DR Genevisible; Q9LNF4; AT. PE 2: Evidence at transcript level; KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase; KW Reference proteome. FT CHAIN 1..383 FT /note="Probable protein phosphatase 2C 13" FT /id="PRO_0000367944" FT DOMAIN 78..349 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT BINDING 121 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 121 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 122 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 297 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 340 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT CONFLICT 160 FT /note="E -> G (in Ref. 3; BAD44439)" FT /evidence="ECO:0000305" SQ SEQUENCE 383 AA; 42106 MW; 4304B1895B801ECF CRC64; MILSQTMVAE AEIRVLDVKC HISAPKDQKN FQIDEVRVSE SVRAEISGSA ETPRFGSGMS CVTTTIGESA SDFIPTIRSG SFADIRSRET MEDEHICIDD LSAHLGSYNF SVPSAFYGVF DGHGGPEAAI FMKENLTRLF FQDAVFPEMP SIVDAFFLEE LENSHRKAFA LADLAMADET IVSGSCGTTA LTALIIGRHL LVANAGDCRA VLCRRGVAVD MSFDHRSTYE PERRRIEDLG GYFEDGYLNG VLAVTRAIGD WELKNPFTDS SSPLISDPEI GQIILTEDDE FLILACDGIW DVLSSQNAVS NVRQGLRRHG DPRQCAMELG KEAARLQSSD NMTVIVICFS SVPSSPKQPQ RRRLRFCVSD EARARLQAML AGE //