PME3_ARATH
ID PME3_ARATH Reviewed; 592 AA.
AC O49006; Q56X61; Q93YZ2; Q9LUL7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Pectinesterase/pectinesterase inhibitor 3;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 3;
DE AltName: Full=Pectin methylesterase inhibitor 3;
DE Includes:
DE RecName: Full=Pectinesterase 3;
DE Short=PE 3;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 27;
DE Short=AtPME27;
DE AltName: Full=Pectin methylesterase 3;
DE Flags: Precursor;
GN Name=PME3; Synonyms=ARATH27; OrderedLocusNames=At3g14310;
GN ORFNames=MLN21.10;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=9767082; DOI=10.1016/s0378-1119(98)00431-4;
RA Micheli F., Holliger C., Goldberg R., Richard L.;
RT "Characterization of the pectin methylesterase-like gene AtPME3: a new
RT member of a gene family comprising at least 12 genes in Arabidopsis
RT thaliana.";
RL Gene 220:13-20(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=15593128; DOI=10.1002/pmic.200400882;
RA Boudart G., Jamet E., Rossignol M., Lafitte C., Borderies G., Jauneau A.,
RA Esquerre-Tugaye M.-T., Pont-Lezica R.;
RT "Cell wall proteins in apoplastic fluids of Arabidopsis thaliana rosettes:
RT identification by mass spectrometry and bioinformatics.";
RL Proteomics 5:212-221(2005).
RN [8]
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).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:15593128}. Secreted, cell wall {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers and siliques.
CC {ECO:0000269|PubMed:16622707, ECO:0000269|PubMed:9767082}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout silique development.
CC {ECO:0000269|PubMed:16622707}.
CC -!- MISCELLANEOUS: The PMEI region may act as an autoinhibitory domain and
CC prevent untimely PME activity during transport.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL24278.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD94011.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF033204; AAC72288.1; -; Genomic_DNA.
DR EMBL; AB022220; BAB01037.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75500.1; -; Genomic_DNA.
DR EMBL; AY037184; AAK59769.1; -; mRNA.
DR EMBL; AY052252; AAK97722.1; -; mRNA.
DR EMBL; AY143950; AAN28889.1; -; mRNA.
DR EMBL; AY058892; AAL24278.1; ALT_FRAME; mRNA.
DR EMBL; AK221816; BAD94011.1; ALT_SEQ; mRNA.
DR RefSeq; NP_188048.1; NM_112289.3.
DR AlphaFoldDB; O49006; -.
DR SMR; O49006; -.
DR BioGRID; 5985; 3.
DR STRING; 3702.AT3G14310.1; -.
DR PaxDb; O49006; -.
DR PRIDE; O49006; -.
DR ProteomicsDB; 226210; -.
DR EnsemblPlants; AT3G14310.1; AT3G14310.1; AT3G14310.
DR GeneID; 820651; -.
DR Gramene; AT3G14310.1; AT3G14310.1; AT3G14310.
DR KEGG; ath:AT3G14310; -.
DR Araport; AT3G14310; -.
DR TAIR; locus:2091000; AT3G14310.
DR eggNOG; ENOG502QSQ4; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; O49006; -.
DR OMA; WLRSTTF; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; O49006; -.
DR BioCyc; ARA:AT3G14310-MON; -.
DR BRENDA; 3.1.1.11; 399.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:O49006; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O49006; baseline and differential.
DR Genevisible; O49006; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0030599; F:pectinesterase activity; IDA:TAIR.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009620; P:response to fungus; IEP:TAIR.
DR GO; GO:0009624; P:response to nematode; IMP:TAIR.
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 Apoplast; Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..592
FT /note="Pectinesterase/pectinesterase inhibitor 3"
FT /id="PRO_0000371662"
FT REGION 53..212
FT /note="Pectinesterase inhibitor 3"
FT REGION 281..578
FT /note="Pectinesterase 3"
FT ACT_SITE 409
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 430
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 356
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 500
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 408
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 423..443
FT /evidence="ECO:0000250"
FT CONFLICT 81..82
FT /note="GV -> AC (in Ref. 1; AAC72288)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="A -> R (in Ref. 1; AAC72288)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 64256 MW; 32AFAF1E6C471B2F CRC64;
MAPSMKEIFS KDNFKKNKKL VLLSAAVALL FVAAVAGISA GASKANEKRT LSPSSHAVLR
SSCSSTRYPE LCISAVVTAG GVELTSQKDV IEASVNLTIT AVEHNYFTVK KLIKKRKGLT
PREKTALHDC LETIDETLDE LHETVEDLHL YPTKKTLREH AGDLKTLISS AITNQETCLD
GFSHDDADKQ VRKALLKGQI HVEHMCSNAL AMIKNMTDTD IANFEQKAKI TSNNRKLKEE
NQETTVAVDI AGAGELDSEG WPTWLSAGDR RLLQGSGVKA DATVAADGSG TFKTVAAAVA
AAPENSNKRY VIHIKAGVYR ENVEVAKKKK NIMFMGDGRT RTIITGSRNV VDGSTTFHSA
TVAAVGERFL ARDITFQNTA GPSKHQAVAL RVGSDFSAFY NCDMLAYQDT LYVHSNRQFF
VKCLIAGTVD FIFGNAAVVL QDCDIHARRP NSGQKNMVTA QGRTDPNQNT GIVIQKCRIG
ATSDLQSVKG SFPTYLGRPW KEYSQTVIMQ SAISDVIRPE GWSEWTGTFA LNTLTYREYS
NTGAGAGTAN RVKWRGFKVI TAAAEAQKYT AGQFIGGGGW LSSTGFPFSL GL
