IMPL1_ARATH
ID IMPL1_ARATH Reviewed; 371 AA.
AC Q94F00; Q8LF86; Q9SA15;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Phosphatase IMPL1, chloroplastic;
DE EC=3.1.3.25;
DE AltName: Full=Protein MYO-INOSITOL MONOPHOSPHATASE-LIKE 1;
DE Flags: Precursor;
GN Name=IMPL1; OrderedLocusNames=At1g31190; ORFNames=F28K20.15;
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].
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19339506; DOI=10.1104/pp.108.135129;
RA Torabinejad J., Donahue J.L., Gunesekera B.N., Allen-Daniels M.J.,
RA Gillaspy G.E.;
RT "VTC4 is a bifunctional enzyme that affects myoinositol and ascorbate
RT biosynthesis in plants.";
RL Plant Physiol. 150:951-961(2009).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=20960216; DOI=10.1007/s10265-010-0381-y;
RA Sato Y., Yazawa K., Yoshida S., Tamaoki M., Nakajima N., Iwai H., Ishii T.,
RA Satoh S.;
RT "Expression and functions of myo-inositol monophosphatase family genes in
RT seed development of Arabidopsis.";
RL J. Plant Res. 124:385-394(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-61, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-60, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Phosphatase acting preferentially on D-myoinositol 1-
CC phosphate (D-Ins 1-P). {ECO:0000269|PubMed:19339506,
CC ECO:0000269|PubMed:20960216}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000269|PubMed:19339506};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in pistil and seed endosperm.
CC {ECO:0000269|PubMed:20960216}.
CC -!- DEVELOPMENTAL STAGE: Detected in globular to heart stage embryos.
CC {ECO:0000269|PubMed:20960216}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21685.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004793; AAD21685.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31327.1; -; Genomic_DNA.
DR EMBL; AY084989; AAM61548.1; -; mRNA.
DR EMBL; AF387002; AAK62447.1; -; mRNA.
DR EMBL; BT008458; AAP37817.1; -; mRNA.
DR PIR; A86438; A86438.
DR RefSeq; NP_564376.1; NM_102857.2.
DR AlphaFoldDB; Q94F00; -.
DR SMR; Q94F00; -.
DR BioGRID; 25242; 2.
DR IntAct; Q94F00; 1.
DR STRING; 3702.AT1G31190.1; -.
DR iPTMnet; Q94F00; -.
DR PaxDb; Q94F00; -.
DR PRIDE; Q94F00; -.
DR ProteomicsDB; 248451; -.
DR EnsemblPlants; AT1G31190.1; AT1G31190.1; AT1G31190.
DR GeneID; 840007; -.
DR Gramene; AT1G31190.1; AT1G31190.1; AT1G31190.
DR KEGG; ath:AT1G31190; -.
DR Araport; AT1G31190; -.
DR TAIR; locus:2029524; AT1G31190.
DR eggNOG; KOG2951; Eukaryota.
DR HOGENOM; CLU_044118_0_2_1; -.
DR InParanoid; Q94F00; -.
DR OMA; DGGNFCV; -.
DR OrthoDB; 915621at2759; -.
DR BioCyc; ARA:AT1G31190-MON; -.
DR BioCyc; MetaCyc:AT1G31190-MON; -.
DR BRENDA; 3.1.3.25; 399.
DR UniPathway; UPA00823; UER00788.
DR PRO; PR:Q94F00; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94F00; baseline and differential.
DR Genevisible; Q94F00; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:TAIR.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd01639; IMPase; 1.
DR InterPro; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chloroplast; Hydrolase; Magnesium; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 61..371
FT /note="Phosphatase IMPL1, chloroplastic"
FT /id="PRO_0000383677"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167..170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 273..275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 20
FT /note="R -> G (in Ref. 4; AAK62447/AAP37817)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="I -> F (in Ref. 3; AAM61548)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="W -> R (in Ref. 3; AAM61548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 40445 MW; 52B3690BE791F089 CRC64;
MGRSLIFSGN MSLRISHLPR SSLPLQNPIS GRTVNRTFRY RCTRILSNSF KSTTRLQTKA
VLSEVSDQTR YPRIGAKTTG TISPAHLLEV VELAAKTGAE VVMEAVNKPR NITYKGLSDL
VTDTDKASEA AILEVVKKNF SDHLILGEEG GIIGDSSSDY LWCIDPLDGT TNFAHGYPSF
AVSVGVLYRG NPAAASVVEF VGGPMCWNTR TFSATAGGGA LCNGQKIHVS KTDAVERALL
ITGFGYEHDD AWSTNMELFK EFTDVSRGVR RLGAAAVDMC HVALGIAESY WEYRLKPWDM
AAGVLIVEEA GGAVTRMDGG KFSVFDRSVL VSNGVLHPKL LERIAPATEN LKSKGIDFSL
WFKPEDYHTE L
