ID PPP7L_ARATH Reviewed; 1340 AA.
AC Q9LNG5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Serine/threonine-protein phosphatase 7 long form homolog;
DE EC=3.1.3.16;
DE AltName: Full=Protein MAIN-LIKE 3 {ECO:0000303|PubMed:24635680};
GN Name=MAIL3 {ECO:0000303|PubMed:24635680}; OrderedLocusNames=At1g48120;
GN ORFNames=F21D18.16;
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] OF 802-1340.
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=17368080; DOI=10.1016/j.tplants.2007.03.003;
RA Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.;
RT "Arabidopsis PPP family of serine/threonine phosphatases.";
RL Trends Plant Sci. 12:169-176(2007).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24635680; DOI=10.1111/tpj.12455;
RA Uehlken C., Horvath B., Stadler R., Sauer N., Weingartner M.;
RT "MAIN-LIKE1 is a crucial factor for correct cell division and
RT differentiation in Arabidopsis thaliana.";
RL Plant J. 78:107-120(2014).
CC -!- FUNCTION: Maybe required to maintain cell division activity in
CC meristematic cells. {ECO:0000250|UniProtKB:Q9LMT7}.
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24635680}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, the shoot apical meristem
CC (SAM), leaf vasculature, hydathodes and mature flowers.
CC {ECO:0000269|PubMed:24635680}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:24635680}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-7 subfamily.
CC {ECO:0000305}.
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DR EMBL; AC023673; AAF79521.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32251.1; -; Genomic_DNA.
DR EMBL; AY064134; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; D96521; D96521.
DR RefSeq; NP_175246.2; NM_103708.4.
DR AlphaFoldDB; Q9LNG5; -.
DR SMR; Q9LNG5; -.
DR BioGRID; 26455; 1.
DR STRING; 3702.Q9LNG5; -.
DR iPTMnet; Q9LNG5; -.
DR PaxDb; 3702-AT1G48120-1; -.
DR ProteomicsDB; 236588; -.
DR EnsemblPlants; AT1G48120.1; AT1G48120.1; AT1G48120.
DR GeneID; 841230; -.
DR Gramene; AT1G48120.1; AT1G48120.1; AT1G48120.
DR KEGG; ath:AT1G48120; -.
DR Araport; AT1G48120; -.
DR TAIR; AT1G48120; MAIL3.
DR eggNOG; KOG0376; Eukaryota.
DR HOGENOM; CLU_005979_0_0_1; -.
DR InParanoid; Q9LNG5; -.
DR OMA; KCHTRAF; -.
DR OrthoDB; 649032at2759; -.
DR PRO; PR:Q9LNG5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNG5; baseline and differential.
DR Genevisible; Q9LNG5; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07418; MPP_PP7; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR019557; AminoTfrase-like_pln_mobile.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041754; MPP_PP7.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR PANTHER; PTHR45668:SF7; SERINE_THREONINE-PROTEIN PHOSPHATASE 7 LONG FORM HOMOLOG; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF10536; PMD; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Manganese; Metal-binding; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..1340
FT /note="Serine/threonine-protein phosphatase 7 long form
FT homolog"
FT /id="PRO_0000308992"
FT REGION 788..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 722
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 660
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255"
FT BINDING 662
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255"
FT BINDING 773
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1340 AA; 149455 MW; A61C545C56C7901B CRC64;
MEVQSLLNFD LDPGPVDQSI LVWQHEHRSA AIWEDEVPPR ELTCRHKLLG MRDWPLDPLV
CQKLIEFGLY GVYKVAFIQL DYALITALVE RWRPETHTFH LPAGEITVTL QDVNILLGLR
VDGPAVTGST KYNWADLCED LLGHRPGPKD LHGSHVSLAW LRENFRNLPA DPDEVTLKCH
TRAFVLALMS GFLYGDKSKH DVALTFLPLL RDFDEVAKLS WGSATLALLY RELCRASKRT
VSTICGPLVL LQLWAWERLH VGRPGRLKDV GASYMDGIDG PLPDPLGCRW RASLSHKENP
RGGLDFYRDQ FDQQKDEQVI WQPYTPDLLA KIPLICVSGE NIWRTVAPLI CFDVVEWHRP
DRVLRQFGLH QTIPAPCDNE KALHAIDKRG KSEYDWSARH SRHIGLWEAR VSSVVSGEPE
CSPMDYNDPY MEWYRRITRR IISPMNERRP GQFLPTGFAF QVLVQRVAAI HARSRASLEE
ELTVGSARQT LQDIVDMCAG ALQLNAPLGS LSNGSVAQAP TPEPFLMLPQ PTPTIIPQKP
MGGEMVCLPL NDMEIDDGLA AEPLELMPPV QDIGCEQSLS SVSQKPLFWP SGGKLTFSWV
CEVMLVFDWS SKNLPPCEFS SVLPFNVLDE LVLFASKILK KEPNCVRIDS EKAEVVVVGD
LHGQLHDLLY LMQDAGFPDG DRFYVFNGNY VDIGAWGLET FLLLLSWKVL LPARVYLLRG
SHESESCTSM YGFKNEVLTK YGDKGAAVYK KCLECFQLLP LASVIAGKVY TAHGGLFRDV
SSFLSDKQER NRKRKRTQKK QTDNTVLDTE DRSESLPLGS LKDLSKVKRR VIDPPTEGSN
LIPGDILWSD PSKDTGLFLN KERGIGLLWG PDCTAKFLQD NNLKWIIRGK GAPDERAKRD
DLAPMNGGYA EDHEGLITLF SAPDHPQFQD TEERHNNKAA YIILQIPECE ELKFQPLEAV
SPRPKAEAYY DFRRLIHPPS NLVHNITNSV DSPSSVPDDK DNLISSENVE YKSMDLSEQM
EVDEKDDVDS KYSESITDEV AAFGTPASGD RDMVDFSDKT ENGSKEADHS ETAEISKDLS
DTVGKPESCS RTRGTYEAIG TDAKLKSNTP EAINLEPQPG CDLYVPDSGN STESRTEKAA
EEACVGRISI DDCSTTGDAA VELEITYDEK LDRVVTEITG NDAAECMTDG NRDIATDGAE
NLEPSTSKLN YSEPSEDIDD STMKFRHNTS CVADSDLETV NGGVNADCSS SSKCLTSKPV
VAHDKFTNLT KPSHDKGYGE SADKPERVIK LVTYSKRKSS DKKHMIESNE DPQQKVNDSV
DSKNKGSLDK SQSVPGDMDS
//
