PME25_ARATH
ID PME25_ARATH Reviewed; 619 AA.
AC Q94CB1; Q3EB96; Q8LGA3; Q9SG78;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 25;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 25;
DE AltName: Full=Pectin methylesterase inhibitor 25;
DE Includes:
DE RecName: Full=Pectinesterase 25;
DE Short=PE 25;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 25;
DE Short=AtPME25;
DE Flags: Precursor;
GN Name=PME25; Synonyms=ARATH25; OrderedLocusNames=At3g10720;
GN ORFNames=T7M13.20;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 1).
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] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) 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 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, cell wall {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94CB1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94CB1-2; Sequence=VSP_037088;
CC -!- TISSUE SPECIFICITY: Expressed in siliques.
CC {ECO:0000269|PubMed:16622707}.
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=AAF19577.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC011708; AAF19577.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE74946.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74947.1; -; Genomic_DNA.
DR EMBL; AY034996; AAK59501.1; -; mRNA.
DR EMBL; AY084383; AAM67242.1; -; mRNA.
DR EMBL; BT029534; ABL66790.1; -; mRNA.
DR RefSeq; NP_187683.2; NM_111908.5. [Q94CB1-1]
DR RefSeq; NP_566379.1; NM_111909.2. [Q94CB1-2]
DR AlphaFoldDB; Q94CB1; -.
DR SMR; Q94CB1; -.
DR STRING; 3702.AT3G10720.2; -.
DR PaxDb; Q94CB1; -.
DR PRIDE; Q94CB1; -.
DR ProteomicsDB; 234933; -. [Q94CB1-1]
DR EnsemblPlants; AT3G10720.1; AT3G10720.1; AT3G10720. [Q94CB1-2]
DR EnsemblPlants; AT3G10720.2; AT3G10720.2; AT3G10720. [Q94CB1-1]
DR GeneID; 820241; -.
DR Gramene; AT3G10720.1; AT3G10720.1; AT3G10720. [Q94CB1-2]
DR Gramene; AT3G10720.2; AT3G10720.2; AT3G10720. [Q94CB1-1]
DR KEGG; ath:AT3G10720; -.
DR Araport; AT3G10720; -.
DR TAIR; locus:2103212; AT3G10720.
DR eggNOG; ENOG502QT2B; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q94CB1; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q94CB1; -.
DR BioCyc; ARA:AT3G10720-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q94CB1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94CB1; baseline and differential.
DR Genevisible; Q94CB1; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0042545; P:cell wall modification; IEA:InterPro.
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 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 PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Aspartyl esterase; Cell wall;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..619
FT /note="Probable pectinesterase/pectinesterase inhibitor 25"
FT /id="PRO_0000371680"
FT REGION 31..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..231
FT /note="Pectinesterase inhibitor 25"
FT REGION 302..601
FT /note="Pectinesterase 25"
FT COMPBIAS 37..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 433
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 454
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 380
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 524
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 432
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 447..467
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..356
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_037088"
FT CONFLICT 359
FT /note="M -> I (in Ref. 4; AAM67242)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="N -> K (in Ref. 4; AAM67242)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="E -> D (in Ref. 4; AAM67242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 67956 MW; C37A7FE1B9A2B0C5 CRC64;
MKMQTLNFTS SLLFLSFIFL SCALLISSQQ SPSQPHSEPP SQLPFEPPVE SPFFPPSQPP
IFVPPSQPPS LPPSQSQSPS LACKSTPYPK LCRTILNAVK SSPSDPYRYG KFTIKQCLKQ
ASRLSKVITS YARRVESKPG SATAEEIGAV ADCGELSELS VNYLETVTTE LKTAQVMTAA
LVEHVNSLLS GVVTNQQTCL DGLVEAKSGF AAAIGSPMGN LTRLYSISLG LVSHALNRNL
KRFKASKGKI LGGGNSTYRE PLETLIKGLR KTCDNDKDCR KTSRNLGELG ETSGGSILVS
KAVIVGPFKS DNFTTITDAI AAAPNNTRPE DGYFVIYARE GVYEEYIVVP INKKNLMLMG
DGINKTIITG NHNVVDGWTT YNCSSFAVVG ERFMAVDVTF RNTAGPEKHQ AVALRNNAEG
SSFYRCSFEG YQDTLYVHSL RQFYRECDIY GTVDFIFGNA AAIFQNCNIY ARKPMAKQKN
AITAHGRLDP NQNTGISIIN CTIKAAPDLA AEPKSAMTFL GRPWKPYSRT VFMQSYISDI
VQPVGWLEWN GTIGLDTIYY GEYSNFGPGA NTNQRVQWLG YNLLNLAEAM NFTVYNFTMG
DTWLPQTDIP FYGGLLSKE
