SLP2_ARATH
ID SLP2_ARATH Reviewed; 391 AA.
AC Q944L7; Q8LG84; Q9LPR3;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Shewanella-like protein phosphatase 2 {ECO:0000303|PubMed:21976480};
DE Short=AtSLP2 {ECO:0000303|PubMed:21976480};
DE EC=3.1.-.- {ECO:0000305};
GN Name=SLP2 {ECO:0000303|PubMed:21976480}; OrderedLocusNames=At1g18480;
GN ORFNames=F15H18.29, F15H18.4;
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].
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 [5]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=21976480; DOI=10.1104/pp.111.182493;
RA Uhrig R.G., Moorhead G.B.;
RT "Two ancient bacterial-like PPP family phosphatases from Arabidopsis are
RT highly conserved plant proteins that possess unique properties.";
RL Plant Physiol. 157:1778-1792(2011).
RN [6]
RP INDUCTION.
RX PubMed=21960277; DOI=10.1007/s10142-011-0254-z;
RA Kutuzov M.A., Andreeva A.V.;
RT "Prediction of biological functions of Shewanella-like protein phosphatases
RT (Shelphs) across different domains of life.";
RL Funct. Integr. Genomics 12:11-23(2012).
CC -!- FUNCTION: Shows phosphatase activity, hydrolyzing the artificial
CC substrate para-nitrophenylphosphate (pNPP) in vitro.
CC {ECO:0000269|PubMed:21976480}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21976480};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P36873};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21976480}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and siliques (at protein level).
CC {ECO:0000269|PubMed:21976480}.
CC -!- INDUCTION: By infection with the bacterial pathogen P.syringae.
CC {ECO:0000305|PubMed:21960277}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:21976480}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. SLP
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26001.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g18480 and At1g18485.; Evidence={ECO:0000305};
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DR EMBL; AC013354; AAF26001.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29719.1; -; Genomic_DNA.
DR EMBL; AF428293; AAL16125.1; -; mRNA.
DR EMBL; BT000488; AAN18057.1; -; mRNA.
DR EMBL; AY084413; AAM60987.1; -; mRNA.
DR PIR; E86318; E86318.
DR RefSeq; NP_564053.1; NM_101705.2.
DR AlphaFoldDB; Q944L7; -.
DR SMR; Q944L7; -.
DR STRING; 3702.AT1G18480.1; -.
DR iPTMnet; Q944L7; -.
DR SwissPalm; Q944L7; -.
DR PaxDb; Q944L7; -.
DR PRIDE; Q944L7; -.
DR ProteomicsDB; 232660; -.
DR EnsemblPlants; AT1G18480.1; AT1G18480.1; AT1G18480.
DR GeneID; 838428; -.
DR Gramene; AT1G18480.1; AT1G18480.1; AT1G18480.
DR KEGG; ath:AT1G18480; -.
DR Araport; AT1G18480; -.
DR TAIR; locus:2014079; AT1G18480.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_042543_1_1_1; -.
DR OMA; NEVLWFM; -.
DR OrthoDB; 763057at2759; -.
DR PhylomeDB; Q944L7; -.
DR PRO; PR:Q944L7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q944L7; baseline and differential.
DR Genevisible; Q944L7; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd07425; MPP_Shelphs; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041787; MPP_Shelphs.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..391
FT /note="Shewanella-like protein phosphatase 2"
FT /id="PRO_0000342697"
FT ACT_SITE 133
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 295
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT CONFLICT 20
FT /note="S -> Y (in Ref. 4; AAM60987)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="L -> P (in Ref. 4; AAM60987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 43282 MW; 08A7835ADF2EFE00 CRC64;
MSSRENPSGI CKSIPKLISS FVDTFVDYSV SGIFLPQDPS SQNEILQTRF EKPERLVAIG
DLHGDLEKSR EAFKIAGLID SSDRWTGGST MVVQVGDVLD RGGEELKILY FLEKLKREAE
RAGGKILTMN GNHEIMNIEG DFRYVTKKGL EEFQIWADWY CLGNKMKTLC SGLDKPKDPY
EGIPMSFPRM RADCFEGIRA RIAALRPDGP IAKRFLTKNQ TVAVVGDSVF VHGGLLAEHI
EYGLERINEE VRGWINGFKG GRYAPAYCRG GNSVVWLRKF SEEMAHKCDC AALEHALSTI
PGVKRMIMGH TIQDAGINGV CNDKAIRIDV GMSKGCADGL PEVLEIRRDS GVRIVTSNPL
YKENLYSHVA PDSKTGLGLL VPVPKQVEVK A
