P2C18_ARATH
ID P2C18_ARATH Reviewed; 504 AA.
AC Q8RXZ4; Q2V4C0; Q3ECA6; Q9MA12;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable protein phosphatase 2C 18;
DE Short=AtPP2C18;
DE EC=3.1.3.16;
GN OrderedLocusNames=At1g79630; ORFNames=F20B17.6;
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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RXZ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RXZ4-3; Sequence=VSP_036761;
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF68125.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX814900; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC010793; AAF68125.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36275.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36276.2; -; Genomic_DNA.
DR EMBL; CP002684; ANM57733.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57736.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57737.1; -; Genomic_DNA.
DR EMBL; AY080600; AAL85011.1; -; mRNA.
DR EMBL; AY114037; AAM45085.1; -; mRNA.
DR EMBL; BX814900; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; E96827; E96827.
DR RefSeq; NP_001319418.1; NM_001334901.1. [Q8RXZ4-3]
DR RefSeq; NP_001320218.1; NM_001334903.1. [Q8RXZ4-3]
DR RefSeq; NP_001320221.1; NM_001334902.1. [Q8RXZ4-3]
DR RefSeq; NP_001320222.1; NM_001334904.1. [Q8RXZ4-3]
DR RefSeq; NP_178081.2; NM_106612.4. [Q8RXZ4-1]
DR AlphaFoldDB; Q8RXZ4; -.
DR SMR; Q8RXZ4; -.
DR BioGRID; 29520; 2.
DR IntAct; Q8RXZ4; 2.
DR MINT; Q8RXZ4; -.
DR STRING; 3702.AT1G79630.1; -.
DR PaxDb; Q8RXZ4; -.
DR PRIDE; Q8RXZ4; -.
DR ProteomicsDB; 248702; -. [Q8RXZ4-1]
DR EnsemblPlants; AT1G79630.1; AT1G79630.1; AT1G79630. [Q8RXZ4-1]
DR EnsemblPlants; AT1G79630.3; AT1G79630.3; AT1G79630. [Q8RXZ4-3]
DR EnsemblPlants; AT1G79630.4; AT1G79630.4; AT1G79630. [Q8RXZ4-3]
DR EnsemblPlants; AT1G79630.5; AT1G79630.5; AT1G79630. [Q8RXZ4-3]
DR EnsemblPlants; AT1G79630.6; AT1G79630.6; AT1G79630. [Q8RXZ4-3]
DR GeneID; 844302; -.
DR Gramene; AT1G79630.1; AT1G79630.1; AT1G79630. [Q8RXZ4-1]
DR Gramene; AT1G79630.3; AT1G79630.3; AT1G79630. [Q8RXZ4-3]
DR Gramene; AT1G79630.4; AT1G79630.4; AT1G79630. [Q8RXZ4-3]
DR Gramene; AT1G79630.5; AT1G79630.5; AT1G79630. [Q8RXZ4-3]
DR Gramene; AT1G79630.6; AT1G79630.6; AT1G79630. [Q8RXZ4-3]
DR KEGG; ath:AT1G79630; -.
DR Araport; AT1G79630; -.
DR TAIR; locus:2019868; AT1G79630.
DR eggNOG; KOG0698; Eukaryota.
DR InParanoid; Q8RXZ4; -.
DR OrthoDB; 1344250at2759; -.
DR PhylomeDB; Q8RXZ4; -.
DR PRO; PR:Q8RXZ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RXZ4; baseline and differential.
DR Genevisible; Q8RXZ4; AT.
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 GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..504
FT /note="Probable protein phosphatase 2C 18"
FT /id="PRO_0000367948"
FT DOMAIN 67..399
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..110
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036761"
SQ SEQUENCE 504 AA; 55604 MW; 71B511B182D7B86E CRC64;
MGLCYSVDRT TGKEPGEASS TATTAETVEE RSGSGRWRRP RDLKGGGDIE GIPQVLGRLV
SNGSSKIACL YTQQGKKGTN QDAMLVFENF CSRDDTVFCG VFDGHGPFGH MVAKKVRDTL
PFTLLTQLKM TSESDQSSLV GANGFQIKCT EEEEVQTTES EQVQKTESVT TMDEQWCELN
PNVNNDELPE MYLPLKHAML KSCQQIDKEL KMHPTIDCFC SGTTSVTLIK QGEDLVVGNI
GDSRAVLATR DEDNALLAVQ LTIDLKPDLP GESARIQKCK GRVFALQDEP EVARVWLPNS
DSPGLAMARA FGDFCLKDYG LISVPDINYR RLTERDQFII LASDGVWDVL SNKEAVDIVA
SAPSRSTAAR ALVDTAVRSW RIKYPTSKND DCTVVCLFLQ DSSVAMEVST NVKKDSPKEE
SIESVTNSTS KEEDEIVPVK DEKIPESCGI ESKMMTMTLA ECISVAQDDE EWSALEGLTR
VNSLLSIPRF LSGELRSTSW RKWL
