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P2C05_ARATH
ID   P2C05_ARATH             Reviewed;         428 AA.
AC   O80492; Q8W588;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Probable protein phosphatase 2C 5;
DE            Short=AtPP2C05;
DE            EC=3.1.3.16;
GN   OrderedLocusNames=At1g09160; ORFNames=T12M4.15;
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;
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].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
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=AAL31893.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC003114; AAC24088.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28405.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28406.1; -; Genomic_DNA.
DR   EMBL; AF419561; AAL31893.1; ALT_FRAME; mRNA.
DR   EMBL; BT029756; ABM06026.1; -; mRNA.
DR   EMBL; AK316880; BAH19588.1; -; mRNA.
DR   PIR; A86224; A86224.
DR   RefSeq; NP_172388.1; NM_100786.4.
DR   RefSeq; NP_849621.1; NM_179290.3.
DR   AlphaFoldDB; O80492; -.
DR   SMR; O80492; -.
DR   BioGRID; 22677; 1.
DR   IntAct; O80492; 1.
DR   STRING; 3702.AT1G09160.1; -.
DR   iPTMnet; O80492; -.
DR   PaxDb; O80492; -.
DR   PRIDE; O80492; -.
DR   ProteomicsDB; 248700; -.
DR   EnsemblPlants; AT1G09160.1; AT1G09160.1; AT1G09160.
DR   EnsemblPlants; AT1G09160.2; AT1G09160.2; AT1G09160.
DR   GeneID; 837436; -.
DR   Gramene; AT1G09160.1; AT1G09160.1; AT1G09160.
DR   Gramene; AT1G09160.2; AT1G09160.2; AT1G09160.
DR   KEGG; ath:AT1G09160; -.
DR   Araport; AT1G09160; -.
DR   TAIR; locus:2195331; AT1G09160.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_3_1_1; -.
DR   InParanoid; O80492; -.
DR   OMA; CAKCRNK; -.
DR   OrthoDB; 567418at2759; -.
DR   PhylomeDB; O80492; -.
DR   PRO; PR:O80492; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O80492; baseline and differential.
DR   Genevisible; O80492; AT.
DR   GO; GO:0005886; C:plasma membrane; HDA: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: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; 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..428
FT                   /note="Probable protein phosphatase 2C 5"
FT                   /id="PRO_0000367937"
FT   DOMAIN          25..297
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         73
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   428 AA;  45780 MW;  63E584318E44B831 CRC64;
     MSVSKASRTQ HSLVPLATLI GRELRSEKVE KPFVKYGQAA LAKKGEDYFL IKTDCERVPG
     DPSSAFSVFG IFDGHNGNSA AIYTKEHLLE NVVSAIPQGA SRDEWLQALP RALVAGFVKT
     DIEFQQKGET SGTTVTFVII DGWTITVASV GDSRCILDTQ GGVVSLLTVD HRLEENVEER
     ERITASGGEV GRLNVFGGNE VGPLRCWPGG LCLSRSIGDT DVGEFIVPIP HVKQVKLPDA
     GGRLIIASDG IWDILSSDVA AKACRGLSAD LAAKLVVKEA LRTKGLKDDT TCVVVDIVPS
     GHLSLAPAPM KKQNPFTSFL SRKNHMDTNN KNGNKLSAVG VVEELFEEGS AVLADRLGKD
     LLSNTETGLL KCAVCQIDES PSEDLSSNGG SIISSASKRW EGPFLCTICK KKKDAMEGKR
     PSKGSVTT
 
 
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