ID Q8LBH8_ARATH Unreviewed; 304 AA.
AC Q8LBH8;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
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 {ECO:0000313|EMBL:AAM64756.1};
RN [1] {ECO:0000313|EMBL:AAM64756.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12093376;
RA Haas B.J., Volfovsky N., Town C.D., Troukhan M., Alexandrov N.,
RA Feldmann K.A., Flavell R.B., White O., Salzberg S.L.;
RT "Full-length messenger RNA sequences greatly improve genome annotation.";
RL Genome Biol. 3:RESEARCH0029-RESEARCH0029(2002).
RN [2] {ECO:0000313|EMBL:AAM64756.1}
RP NUCLEOTIDE SEQUENCE.
RA Brover V., Troukhan M., Alexandrov N., Lu Y.-P., Flavell R., Feldmann K.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAM64756.1}
RP NUCLEOTIDE SEQUENCE.
RA Alexandrov N.A., Troukhan M.E., Brover V.V., Flavell R.B., Feldmann K.A.;
RT "Features of Arabidopsis genes and genome discovered using full-length
RT cDNAs.";
RL Plant Mol. Biol. 60:71-87(2006).
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 Evidence={ECO:0000256|RuleBase:RU004273};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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DR EMBL; AY087200; AAM64756.1; -; mRNA.
DR AlphaFoldDB; Q8LBH8; -.
DR TAIR; AT3G46820; -.
DR ExpressionAtlas; Q8LBH8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07414; MPP_PP1_PPKL; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF459; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1 ISOZYME 2-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|RuleBase:RU004273};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}.
FT DOMAIN 119..124
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
SQ SEQUENCE 304 AA; 34731 MW; F10C204288480676 CRC64;
MDPAVLDDII RRLLDYRNPK AGTKQAMLND SEIRQLCFVS REIFLQQPCL LELAAPVKIC
GDIHGQYSDL LRLFEYGGFP PAANYLFLGD YVDRGKQSLE TICLLLAYKI KYPENFFLLR
GNHECASINR IYGFYDECKR RFNVKLWKVF TDTFNCLPVA AVIDEKILCM HGGLSPELIN
VEQIKNIERP TDVPDAGLLC DLLWSDPSKD VKGWGMNDRG VSYTFGADKV AEFLIKNDMD
LVCRAHQVVE DGYEFFADRQ LVTMFSAPNY CGEFDNAGAL MSVDESLMCS FQILKPVDRR
SRFF
//
