P2C62_ARATH
ID P2C62_ARATH Reviewed; 724 AA.
AC Q93V88; Q9SZC7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable protein phosphatase 2C 62;
DE Short=AtPP2C62;
DE EC=3.1.3.16;
GN OrderedLocusNames=At4g33500; ORFNames=F17M5.260;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38808.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80067.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035678; CAB38808.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161583; CAB80067.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86236.1; -; Genomic_DNA.
DR EMBL; AY035047; AAK59552.1; -; mRNA.
DR EMBL; AY051052; AAK93729.1; -; mRNA.
DR PIR; T06001; T06001.
DR RefSeq; NP_567923.1; NM_119504.4.
DR AlphaFoldDB; Q93V88; -.
DR SMR; Q93V88; -.
DR BioGRID; 14772; 1.
DR STRING; 3702.AT4G33500.1; -.
DR iPTMnet; Q93V88; -.
DR PaxDb; Q93V88; -.
DR PRIDE; Q93V88; -.
DR ProteomicsDB; 248726; -.
DR EnsemblPlants; AT4G33500.1; AT4G33500.1; AT4G33500.
DR GeneID; 829488; -.
DR Gramene; AT4G33500.1; AT4G33500.1; AT4G33500.
DR KEGG; ath:AT4G33500; -.
DR Araport; AT4G33500; -.
DR TAIR; locus:2119246; AT4G33500.
DR eggNOG; KOG1379; Eukaryota.
DR HOGENOM; CLU_010300_0_0_1; -.
DR InParanoid; Q93V88; -.
DR OMA; WIGIADG; -.
DR OrthoDB; 826926at2759; -.
DR PhylomeDB; Q93V88; -.
DR PRO; PR:Q93V88; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93V88; baseline and differential.
DR Genevisible; Q93V88; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.40.10; -; 2.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PTHR12320; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..724
FT /note="Probable protein phosphatase 2C 62"
FT /id="PRO_0000367984"
FT DOMAIN 482..719
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 357..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 514
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 643
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 710
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 724 AA; 78924 MW; E395C345F5F79D64 CRC64;
MADHLILSLQ APPFLIFPCS LHRSWRFPGG IRYSVPEFRL SSQLQLANSI SPSKSSASSS
SPPENSAPEK FDLVSSTQLK DGSHVFRFGD ASEIEKYLEA EEKARCVEVE TQNAKIAEEA
SEVSRKQKKL VSSIIETSTE KEETAAPSDL SNVIKIKDRK RVRSPTKKKK ETVNVSRSED
KIDAKSASVS NLSSIVSVAE AIPISSTEEE AVVEKEITAK SYNVEPLSSE AMKKVSVNKI
GDCETNGYQE NRMEVQARPS LSTQQEITPV STIEIDDNLD VTEKPIEAEE NLVAEPTATD
DLSPDELLST SEATHRSVDE IAQKPVIDTS EENLLNTFEA EENPVVEPTA TAAVSSDELI
STSEATRHSV DEIAQKPIID TSEKNPMETF VEPEAVHSSV DESTEKLVVV TSDVENDGEN
VASTTEDEIT VRDTITDSGS ISNNDDTKVE DLQLPVPETA SLEPIKAASG REELVSKAFY
LDSGFASLQS PFKALAGRED AYFISHHNWI GIADGVSQWS FEGINKGMYA QELMSNCEKI
ISNETAKISD PVQVLHRSVN ETKSSGSSTA LIAHLDNNEL HIANIGDSGF MVIRDGTVLQ
NSSPMFHHFC FPLHITQGCD VLKLAEVYHV NLEEGDVVIA ATDGLFDNLY EKEIVSIVCG
SLKQSLEPQK IAELVAAKAQ EVGRSKTERT PFADAAKEEG YNGHKGGKLD AVTVIISFVK
IVST
