P2C08_ARATH
ID P2C08_ARATH Reviewed; 351 AA.
AC Q9LMT1; A8MRQ0; Q147S0; Q944K0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable protein phosphatase 2C 8;
DE Short=AtPP2C08;
DE EC=3.1.3.16;
GN OrderedLocusNames=At1g18030; ORFNames=T10F20.4;
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 1).
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clone.";
RL Submitted (JUL-2006) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LMT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LMT1-2; Sequence=VSP_036757, VSP_036758;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97840.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC034107; AAF97840.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE29665.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29666.1; -; Genomic_DNA.
DR EMBL; AF428352; AAL16282.1; -; mRNA.
DR EMBL; BT026023; ABG48379.1; -; mRNA.
DR PIR; G86315; G86315.
DR RefSeq; NP_001077557.1; NM_001084088.2. [Q9LMT1-2]
DR RefSeq; NP_564045.1; NM_101665.3. [Q9LMT1-1]
DR AlphaFoldDB; Q9LMT1; -.
DR SMR; Q9LMT1; -.
DR BioGRID; 23622; 1.
DR IntAct; Q9LMT1; 1.
DR MINT; Q9LMT1; -.
DR STRING; 3702.AT1G18030.1; -.
DR PaxDb; Q9LMT1; -.
DR PRIDE; Q9LMT1; -.
DR ProteomicsDB; 248696; -. [Q9LMT1-1]
DR EnsemblPlants; AT1G18030.1; AT1G18030.1; AT1G18030. [Q9LMT1-1]
DR EnsemblPlants; AT1G18030.2; AT1G18030.2; AT1G18030. [Q9LMT1-2]
DR GeneID; 838383; -.
DR Gramene; AT1G18030.1; AT1G18030.1; AT1G18030. [Q9LMT1-1]
DR Gramene; AT1G18030.2; AT1G18030.2; AT1G18030. [Q9LMT1-2]
DR KEGG; ath:AT1G18030; -.
DR Araport; AT1G18030; -.
DR TAIR; locus:2194035; AT1G18030.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_1_2_1; -.
DR InParanoid; Q9LMT1; -.
DR OMA; IIYCANI; -.
DR PhylomeDB; Q9LMT1; -.
DR PRO; PR:Q9LMT1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMT1; baseline and differential.
DR Genevisible; Q9LMT1; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
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..351
FT /note="Probable protein phosphatase 2C 8"
FT /id="PRO_0000367939"
FT DOMAIN 74..348
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 301..305
FT /note="FGPSD -> SVWTK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036757"
FT VAR_SEQ 306..351
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036758"
FT CONFLICT 56
FT /note="A -> V (in Ref. 3; AAL16282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 38486 MW; 0A6808FD713CCB7E CRC64;
MLEKESDLTA MEKPNNKHAA DSFSSEDLVS PVKKAKKSEE VSGGGEAVAA VGNREAEEDK
PSFVSEEKKE FLVEADVAED KGARHTMEDV WVVLPDASLD FPGTLRCAHF AIYDGHGGRL
AAEFAKKHLH LNVLSAGLPR ELLDVKVAKK AILEGFRKTD ELLLQKSVSG GWQDGATAVC
VWILDQKVFV ANIGDAKAVL ARSSTTNELG NHTEAGNPLK AIVLTREHKA IYPQERSRIQ
KSGGVISSNG RLQGRLEVSR AFGDRHFKKF GVSATPDIHA FELTERENFM ILGCDGLWEV
FGPSDAVGFV QKLLKEGLHV STVSRRLVKE AVKERRCKDN CTAIVIVFKR V
