P2C73_ARATH
ID P2C73_ARATH Reviewed; 373 AA.
AC Q0WRB2; Q0WM64; Q8GX49; Q8LD08; Q8SBC4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable protein phosphatase 2C 73;
DE Short=AtPP2C73;
DE EC=3.1.3.16;
DE AltName: Full=AtPPC6;7;
GN Name=PPC6-7; OrderedLocusNames=At5g27930; ORFNames=F14I23.90, F15F15.3;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-373.
RA Izumi S., Yamada M., Ohsato H., Miyazaki S., Bohnert H.J., Fukuhara T.;
RT "Substrate specificity of type 2C protein phosphatases (PP2C) in
RT Arabidopsis thaliana.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
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}.
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DR EMBL; AC007627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93745.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93746.1; -; Genomic_DNA.
DR EMBL; AK118436; BAC43045.1; -; mRNA.
DR EMBL; AK229967; BAF01792.1; -; mRNA.
DR EMBL; AK228402; BAF00337.1; -; mRNA.
DR EMBL; BT026463; ABH04570.1; -; mRNA.
DR EMBL; AY086281; AAM64353.1; -; mRNA.
DR EMBL; AB079668; BAB84697.1; -; mRNA.
DR RefSeq; NP_568503.1; NM_122675.4.
DR RefSeq; NP_851086.1; NM_180755.2.
DR AlphaFoldDB; Q0WRB2; -.
DR SMR; Q0WRB2; -.
DR STRING; 3702.AT5G27930.2; -.
DR PaxDb; Q0WRB2; -.
DR PRIDE; Q0WRB2; -.
DR ProteomicsDB; 250916; -.
DR EnsemblPlants; AT5G27930.1; AT5G27930.1; AT5G27930.
DR EnsemblPlants; AT5G27930.2; AT5G27930.2; AT5G27930.
DR GeneID; 832860; -.
DR Gramene; AT5G27930.1; AT5G27930.1; AT5G27930.
DR Gramene; AT5G27930.2; AT5G27930.2; AT5G27930.
DR KEGG; ath:AT5G27930; -.
DR Araport; AT5G27930; -.
DR TAIR; locus:2143325; AT5G27930.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_6_0_1; -.
DR InParanoid; Q0WRB2; -.
DR OMA; LCHWQEA; -.
DR OrthoDB; 1344250at2759; -.
DR PhylomeDB; Q0WRB2; -.
DR PRO; PR:Q0WRB2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q0WRB2; baseline and differential.
DR Genevisible; Q0WRB2; AT.
DR GO; GO:0005886; C:plasma membrane; 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 GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0009819; P:drought recovery; IMP:TAIR.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR GO; GO:0045926; P:negative regulation of growth; IMP:TAIR.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:TAIR.
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 Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..373
FT /note="Probable protein phosphatase 2C 73"
FT /id="PRO_0000367993"
FT DOMAIN 61..354
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 56
FT /note="Q -> H (in Ref. 3; BAC43045)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="I -> V (in Ref. 3; BAC43045)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="D -> N (in Ref. 7; BAB84697)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="V -> L (in Ref. 6; AAM64353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 41583 MW; A062E30C4169A9F8 CRC64;
MGHFSSMFNG LARSFSIKKV KNNNGNCDAK EAADEMASEA KKKELILKSS GYVNVQGSNN
LASLFSKRGE KGVNQDCALV WEGFGCQEDM IFCGIFDGHG PWGHYVAKQV RNSMPLSLLC
NWQKILAQAT LEPELDLEGS NKKISRFDIW KQSYLKTCAT VDQELEHHRK IDSYYSGTTA
LTIVRQGEVI YVANVGDSRA VLAMESDEGS LVAVQLTLDF KPNLPQEKER IIGCKGRVFC
LDDEPGVHRV WQPDAETPGL AMSRAFGDYC IKEYGLVSVP EVTQRHISTK DHFIILASDG
IWDVISNQEA IEIVSSTAER PKAAKRLVEQ AVRAWKKKRR GYSMDDMSVV CLFLHSSSSS
SLSQHHHAMT ILK
