PME18_ARATH
ID PME18_ARATH Reviewed; 557 AA.
AC Q1JPL7; O49007; Q94AF4; Q94C39; Q9LPX8; Q9LPX9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Pectinesterase/pectinesterase inhibitor 18;
DE AltName: Full=AtPMEpcrA;
DE Contains:
DE RecName: Full=Pectinesterase inhibitor 18;
DE AltName: Full=Pectin methylesterase inhibitor 18;
DE Contains:
DE RecName: Full=Bifunctional pectinesterase 18/rRNA N-glycosylase;
DE Short=PE 18;
DE EC=3.1.1.11;
DE EC=3.2.2.22;
DE AltName: Full=Pectin methylesterase 18;
DE AltName: Full=Pectin methylesterase 4;
DE Short=AtPME4;
DE AltName: Full=Ribosome-inactivating protein;
DE Flags: Precursor;
GN Name=PME18; Synonyms=ARATH4; OrderedLocusNames=At1g11580;
GN ORFNames=T23J18.23, T23J18.24, T23J18.33;
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].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-469, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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 [6]
RP PROTEIN SEQUENCE OF 243-251; 257-274; 282-292; 296-382; 387-413; 429-441;
RP 444-454 AND 530-557, AND FUNCTION.
RX PubMed=18222123; DOI=10.1016/j.bbagen.2007.12.013;
RA De-la-Pena C., Badri D.V., Vivanco J.M.;
RT "Novel role for pectin methylesterase in Arabidopsis: a new function
RT showing ribosome-inactivating protein (RIP) activity.";
RL Biochim. Biophys. Acta 1780:773-783(2008).
RN [7]
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 [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. Inhibits the elongation
CC phase of protein synthesis. {ECO:0000269|PubMed:18222123}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of the N-glycosidic bond at one specific
CC adenosine on the 28S rRNA.; EC=3.2.2.22;
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques, flowers, floral stems,
CC rosette leaves and roots. {ECO:0000269|PubMed:16622707,
CC ECO:0000269|PubMed:9767082}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early seed development and late
CC developmental phases of siliques. {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=AAF16636.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF16637.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011661; AAF16636.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011661; AAF16637.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28755.1; -; Genomic_DNA.
DR EMBL; AY037175; AAK59760.1; -; mRNA.
DR EMBL; AY048217; AAK82480.1; -; mRNA.
DR EMBL; BT025336; ABF57292.1; -; mRNA.
DR EMBL; AF033205; AAC02973.1; -; Genomic_DNA.
DR PIR; A86249; A86249.
DR RefSeq; NP_172624.1; NM_101031.3.
DR AlphaFoldDB; Q1JPL7; -.
DR SMR; Q1JPL7; -.
DR BioGRID; 22941; 2.
DR STRING; 3702.AT1G11580.1; -.
DR iPTMnet; Q1JPL7; -.
DR MetOSite; Q1JPL7; -.
DR SwissPalm; Q1JPL7; -.
DR PaxDb; Q1JPL7; -.
DR PRIDE; Q1JPL7; -.
DR ProteomicsDB; 234737; -.
DR EnsemblPlants; AT1G11580.1; AT1G11580.1; AT1G11580.
DR GeneID; 837701; -.
DR Gramene; AT1G11580.1; AT1G11580.1; AT1G11580.
DR KEGG; ath:AT1G11580; -.
DR Araport; AT1G11580; -.
DR TAIR; locus:2200076; AT1G11580.
DR eggNOG; ENOG502QUQ5; Eukaryota.
DR HOGENOM; CLU_012243_9_2_1; -.
DR InParanoid; Q1JPL7; -.
DR OMA; RTIMEPR; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q1JPL7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q1JPL7; baseline and differential.
DR Genevisible; Q1JPL7; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016020; C:membrane; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009617; P:response to bacterium; IEP: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 Antimicrobial; Aspartyl esterase; Cell wall;
KW Cell wall biogenesis/degradation; Direct protein sequencing; Fungicide;
KW Hydrolase; Plant defense; Protein synthesis inhibitor; Reference proteome;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..557
FT /note="Pectinesterase/pectinesterase inhibitor 18"
FT /id="PRO_0000370182"
FT CHAIN 35..242
FT /note="Pectinesterase inhibitor 18"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370183"
FT CHAIN 243..557
FT /note="Bifunctional pectinesterase 18/rRNA N-glycosylase"
FT /id="PRO_0000370184"
FT REGION 47..203
FT /note="Pectinesterase inhibitor 18"
FT REGION 246..543
FT /note="Pectinesterase 18"
FT ACT_SITE 374
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 395
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 321
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 465
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 373
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="S -> Y (in Ref. 3; AAK59760)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="F -> Y (in Ref. 5; AAC02973)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="L -> E (in Ref. 5; AAC02973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 61687 MW; B1A3C1620DCC127B CRC64;
MSNSNQPLLS KPKSLKHKNL CLVLSFVAIL GSVAFFTAQL ISVNTNNNDD SLLTTSQICH
GAHDQDSCQA LLSEFTTLSL SKLNRLDLLH VFLKNSVWRL ESTMTMVSEA RIRSNGVRDK
AGFADCEEMM DVSKDRMMSS MEELRGGNYN LESYSNVHTW LSSVLTNYMT CLESISDVSV
NSKQIVKPQL EDLVSRARVA LAIFVSVLPA RDDLKMIISN RFPSWLTALD RKLLESSPKT
LKVTANVVVA KDGTGKFKTV NEAVAAAPEN SNTRYVIYVK KGVYKETIDI GKKKKNLMLV
GDGKDATIIT GSLNVIDGST TFRSATVAAN GDGFMAQDIW FQNTAGPAKH QAVALRVSAD
QTVINRCRID AYQDTLYTHT LRQFYRDSYI TGTVDFIFGN SAVVFQNCDI VARNPGAGQK
NMLTAQGRED QNQNTAISIQ KCKITASSDL APVKGSVKTF LGRPWKLYSR TVIMQSFIDN
HIDPAGWFPW DGEFALSTLY YGEYANTGPG ADTSKRVNWK GFKVIKDSKE AEQFTVAKLI
QGGLWLKPTG VTFQEWL
