SLP1_ARATH
ID SLP1_ARATH Reviewed; 389 AA.
AC Q8L774; Q8RY10; Q9LMJ5;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Shewanella-like protein phosphatase 1 {ECO:0000303|PubMed:21976480};
DE Short=AtSLP1 {ECO:0000303|PubMed:21976480};
DE EC=3.1.-.- {ECO:0000305};
DE Flags: Precursor;
GN Name=SLP1 {ECO:0000303|PubMed:21976480};
GN OrderedLocusNames=At1g07010 {ECO:0000312|Araport:AT1G07010};
GN ORFNames=F10K1.27 {ECO:0000312|EMBL:AAF82218.1};
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 FUNCTION, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION,
RP AND 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 [5]
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: Plastid, chloroplast
CC {ECO:0000269|PubMed:21976480}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q8L774-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in rosettes leaves, shoots and flowers
CC (at protein level). {ECO:0000269|PubMed:21976480}.
CC -!- INDUCTION: Circadian-regulated, with a peak in expression at 8 hours
CC light time on a 12 hours light/dark cycle (at protein level)
CC (PubMed:21976480). Induced by heat shock. Down-regulated by infection
CC with the bacterial pathogen P.syringae (Probable).
CC {ECO:0000269|PubMed:21976480, 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=AAF82218.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC067971; AAF82218.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28065.1; -; Genomic_DNA.
DR EMBL; AY079027; AAL84981.1; -; mRNA.
DR EMBL; AY136428; AAM97094.1; -; mRNA.
DR EMBL; BT008476; AAP37835.1; -; mRNA.
DR PIR; H86204; H86204.
DR RefSeq; NP_172182.2; NM_100574.5. [Q8L774-1]
DR AlphaFoldDB; Q8L774; -.
DR SMR; Q8L774; -.
DR IntAct; Q8L774; 1.
DR STRING; 3702.AT1G07010.3; -.
DR PaxDb; Q8L774; -.
DR ProteomicsDB; 228441; -. [Q8L774-1]
DR EnsemblPlants; AT1G07010.1; AT1G07010.1; AT1G07010. [Q8L774-1]
DR GeneID; 837211; -.
DR Gramene; AT1G07010.1; AT1G07010.1; AT1G07010. [Q8L774-1]
DR KEGG; ath:AT1G07010; -.
DR Araport; AT1G07010; -.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_042543_1_0_1; -.
DR OMA; GAFDECA; -.
DR PhylomeDB; Q8L774; -.
DR PRO; PR:Q8L774; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L774; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
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 Alternative splicing; Chloroplast; Hydrolase; Manganese; Metal-binding;
KW Plastid; Protein phosphatase; Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..389
FT /note="Shewanella-like protein phosphatase 1"
FT /id="PRO_0000435683"
FT ACT_SITE 138
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 314
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT CONFLICT 109
FT /note="D -> E (in Ref. 3; AAL84981)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="G -> E (in Ref. 3; AAL84981)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 43732 MW; C0F4E4E00ABE94D0 CRC64;
MASLYLNSLL PLPPSHPQKL LEPSSSSLLS TSNGNELALK PIVINGDPPT FVSAPARRIV
AVGDLHGDLG KARDALQLAG VLSSDGRDQW VGQDTVLVQV GDILDRGDDE IAILSLLRSL
DDQAKANGGA VFQVNGNHET MNVEGDFRYV DARAFDECTD FLDYLEDYAQ DWDKAFRNWI
FESRQWKEDR RSSQTYWDQW NVVKRQKGVI ARSVLLRPGG RLACELSRHG VILRVNNWLF
CHGGLLPHHV AYGIERINRE VSTWMRSPTN YEDSPQMPFI ATRGYDSVVW SRLYSRETSE
LEDYQIEQVN KILHDTLEAV GAKAMVVGHT PQLSGVNCEY GCGIWRVDVG MSSGVLDSRP
EVLEIRGDKA RVIRSNRDRL HELQVADYI
