PME1_ARATH
ID PME1_ARATH Reviewed; 586 AA.
AC Q43867;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Pectinesterase 1;
DE Short=PE 1;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 1;
DE Short=AtPME1;
DE Flags: Precursor;
GN Name=PME1; Synonyms=ARATH65; OrderedLocusNames=At1g53840;
GN ORFNames=T18A20.7;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Shoot;
RX PubMed=7982486; DOI=10.1016/0014-5793(94)01187-7;
RA Richard L., Qin L.X., Gadal P., Goldberg R.;
RT "Molecular cloning and characterisation of a putative pectin methylesterase
RT cDNA in Arabidopsis thaliana (L.).";
RL FEBS Lett. 355:135-139(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8666246; DOI=10.1016/0378-1119(95)00766-0;
RA Richard L., Qin L.X., Goldberg R.;
RT "Clustered genes within the genome of Arabidopsis thaliana encoding pectin
RT methylesterase-like enzymes.";
RL Gene 170:207-211(1996).
RN [3]
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 [4]
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 [5]
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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15337457; DOI=10.1016/j.carres.2004.06.023;
RA Markovic O., Janecek S.;
RT "Pectin methylesterases: sequence-structural features and phylogenetic
RT relationships.";
RL Carbohydr. Res. 339:2281-2295(2004).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16622707; DOI=10.1007/s00425-006-0261-9;
RA Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F.,
RA Guerineau F., Pelloux J.;
RT "Comprehensive expression profiling of the pectin methylesterase gene
RT family during silique development in Arabidopsis thaliana.";
RL Planta 224:782-791(2006).
RN [8]
RP INTERACTION WITH SBT6.1, SUBCELLULAR LOCATION, DOMAIN, AND CLEAVAGE BY
RP SBT6.1.
RX PubMed=19144003; DOI=10.1111/j.1365-313x.2009.03784.x;
RA Wolf S., Rausch T., Greiner S.;
RT "The N-terminal pro region mediates retention of unprocessed type-I PME in
RT the Golgi apparatus.";
RL Plant J. 58:361-375(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28741704; DOI=10.1111/pce.13038;
RA Creighton M.T., Kolton A., Kataya A.R.A., Maple-Groedem J., Averkina I.O.,
RA Heidari B., Lillo C.;
RT "Methylation of protein phosphatase 2A-influence of regulators and
RT environmental stress factors.";
RL Plant Cell Environ. 40:2347-2358(2017).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin (By similarity).
CC Demethylates protein phosphatase 2A (PP2A) that have been reversibly
CC carboxymethylated by LCMT1. Acts as negative regulators of genes
CC involved in salt stress response (PubMed:28741704).
CC {ECO:0000250|UniProtKB:Q5MFV8, ECO:0000269|PubMed:28741704}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBUNIT: Interacts with SBT6.1. {ECO:0000269|PubMed:19144003}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:19144003}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:19144003}. Note=Cleaved in the Golgi apparatus by
CC SBT6.1 (S1P) after the Arg-Arg-Leu-Met (RRLM) and Arg-Arg-Leu-Leu
CC (RRLL) motifs. This processing is required for extracellular targeting.
CC {ECO:0000269|PubMed:19144003}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques.
CC {ECO:0000269|PubMed:16622707}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout silique development.
CC {ECO:0000269|PubMed:16622707}.
CC -!- DOMAIN: The PMEI region may act as an autoinhibitory domain and prevent
CC untimely PME activity during transport. The PMEI region is cleaved by
CC SBT6.1 (S1P) in the Golgi apparatus prior to cell wall targeting.
CC {ECO:0000305|PubMed:19144003}.
CC -!- DISRUPTION PHENOTYPE: Reduced number of leaves at flowering time in
CC long day conditions. {ECO:0000269|PubMed:28741704}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC family. {ECO:0000305}.
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DR EMBL; X81585; CAA57275.1; -; mRNA.
DR EMBL; U25649; AAC50024.1; -; Genomic_DNA.
DR EMBL; AC009324; AAF02857.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33008.1; -; Genomic_DNA.
DR EMBL; AY054197; AAL06858.1; -; mRNA.
DR PIR; JC4778; JC4778.
DR RefSeq; NP_175787.1; NM_104261.3.
DR AlphaFoldDB; Q43867; -.
DR SMR; Q43867; -.
DR STRING; 3702.AT1G53840.1; -.
DR PaxDb; Q43867; -.
DR PRIDE; Q43867; -.
DR ProteomicsDB; 234975; -.
DR EnsemblPlants; AT1G53840.1; AT1G53840.1; AT1G53840.
DR GeneID; 841821; -.
DR Gramene; AT1G53840.1; AT1G53840.1; AT1G53840.
DR KEGG; ath:AT1G53840; -.
DR Araport; AT1G53840; -.
DR TAIR; locus:2197061; AT1G53840.
DR eggNOG; ENOG502RA2Q; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q43867; -.
DR OMA; DKHKWNV; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q43867; -.
DR BioCyc; ARA:AT1G53840-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q43867; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q43867; baseline and differential.
DR Genevisible; Q43867; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; ISS:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; ISS:TAIR.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:0051722; F:protein C-terminal methylesterase activity; IDA:UniProtKB.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.140.40; -; 1.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 1: Evidence at protein level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
KW Reference proteome; Secreted; Signal; Stress response.
FT SIGNAL 1..49
FT /evidence="ECO:0000255"
FT CHAIN 50..586
FT /note="Pectinesterase 1"
FT /id="PRO_0000023474"
FT MOTIF 250..253
FT /note="RRLM cleavage motif"
FT /evidence="ECO:0000305|PubMed:19144003"
FT MOTIF 269..272
FT /note="RRLL cleavage motif"
FT /evidence="ECO:0000305|PubMed:19144003"
FT ACT_SITE 408
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 429
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 494
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 407
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 422..442
FT /evidence="ECO:0000250"
SQ SEQUENCE 586 AA; 64149 MW; EF2752BCC535BE99 CRC64;
MDSVNSFKGY GKVDEAQDLA LKKKTRKRLL LLSISVVVLI AVIIAAVVAT VVHKNKNEST
PSPPPELTPS TSLKAICSVT RFPESCISSI SKLPSSNTTD PETLFKLSLK VIIDELDSIS
DLPEKLSKET EDERIKSALR VCGDLIEDAL DRLNDTVSAI DDEEKKKTLS SSKIEDLKTW
LSATVTDHET CFDSLDELKQ NKTEYANSTI TQNLKSAMSR STEFTSNSLA IVSKILSALS
DLGIPIHRRR RLMSHHHQQS VDFEKWARRR LLQTAGLKPD VTVAGDGTGD VLTVNEAVAK
VPKKSLKMFV IYVKSGTYVE NVVMDKSKWN VMIYGDGKGK TIISGSKNFV DGTPTYETAT
FAIQGKGFIM KDIGIINTAG AAKHQAVAFR SGSDFSVYYQ CSFDGFQDTL YPHSNRQFYR
DCDVTGTIDF IFGSAAVVFQ GCKIMPRQPL SNQFNTITAQ GKKDPNQSSG MSIQRCTISA
NGNVIAPTYL GRPWKEFSTT VIMETVIGAV VRPSGWMSWV SGVDPPASIV YGEYKNTGPG
SDVTQRVKWA GYKPVMSDAE AAKFTVATLL HGADWIPATG VINQLS
