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Reviewed, UniProtKB/Swiss-Prot O81301 (PME40_ARATH)

Last modified November 3, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable pectinesterase/pectinesterase inhibitor 40
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 40
        Alternative name(s):
            Pectin methylesterase inhibitor 40
    2- Recommended name:
            Pectinesterase 40
                Short name=PE 40
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 40
              Short name=AtPME40
Gene names
Name: PME40
Synonyms: ARATH40
Ordered Locus Names: At4g02320
ORF Names: T14P8.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Acts in the modification of cell walls via demethylesterification of cell wall pectin By similarity.

Catalytic activity

Pectin + n H2O = n methanol + pectate.

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.

Subcellular location

Secreted › cell wall By similarity.

Tissue specificity

Expressed in flower buds. Ref.4

Miscellaneous

The PMEI region may act as an autoinhibitory domain and prevent untimely PME activity during transport.

Sequence similarities

In the N-terminal section; belongs to the PMEI family.

In the C-terminal section; belongs to the pectinesterase family.

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Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionAspartyl esterase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell wall modification

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionaspartyl esterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme inhibitor activity

Inferred from electronic annotation. Source: InterPro

pectinesterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 518494Probable pectinesterase/pectinesterase inhibitor 40
PRO_0000371690

Regions

Region25 – 167143Pectinesterase inhibitor 40
Region207 – 504298Pectinesterase 40

Sites

Active site3351Proton donor; for pectinesterase activity By similarity
Active site3561Nucleophile; for pectinesterase activity By similarity
Binding site3121Substrate; for pectinesterase activity By similarity
Binding site4241Substrate; for pectinesterase activity By similarity
Binding site4261Substrate; for pectinesterase activity By similarity
Site3341Transition state stabilizer By similarity

Amino acid modifications

Glycosylation461N-linked (GlcNAc...) Potential
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation581N-linked (GlcNAc...) Potential
Glycosylation691N-linked (GlcNAc...) Potential
Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation4731N-linked (GlcNAc...) Potential
Glycosylation5081N-linked (GlcNAc...) Potential
Disulfide bond349 ↔ 369 By similarity

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Sequences

Sequence LengthMass (Da)Tools
O81301-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: BECBA58404C701B7

FASTA51857,894
        10         20         30         40         50         60 
MTTKSKHIIL SLTFLLLFLS TVFSSHVTQR FTSSDDITEL VVTALNQTIS NVNLSSSNFS 

        70         80         90        100        110        120 
DLLQRLGSNL SHRDLCAFDD CLELLDDTVF DLTTAISKLR SHSPELHNVK MLLSAAMTNT 

       130        140        150        160        170        180 
RTCLDGFASS DNDENLNNND NKTYGVAESL KESLFNISSH VSDSLAMLEN IPGHIPGKVK 

       190        200        210        220        230        240 
EDVGFPMWVS GSDRNLLQDP VDETKVNLVV AQNGTGNYTT IGEAISAAPN SSETRFVIYI 

       250        260        270        280        290        300 
KCGEYFENIE IPREKTMIMF IGDGIGRTVI KANRSYADGW TAFHSATVGV RGSGFIAKDL 

       310        320        330        340        350        360 
SFVNYAGPEK HQAVALRSSS DLSAYYRCSF ESYQDTIYVH SHKQFYRECD IYGTVDFIFG 

       370        380        390        400        410        420 
DASVVFQNCS LYARRPNPNQ KIIYTAQGRE NSREPTGISI ISSRILAAPD LIPVQANFKA 

       430        440        450        460        470        480 
YLGRPWQLYS RTVIMKSFID DLVDPAGWLK WKDDFALETL YYGEYMNEGP GSNMTNRVQW 

       490        500        510 
PGFKRIETVE EASQFSVGPF IDGNKWLNST RIPFTLDL

« Hide

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W., Redman J.C., Wu H.C., Utterback T., Town C.D.
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"Pectin methylesterases: sequence-structural features and phylogenetic relationships."
Markovic O., Janecek S.
Carbohydr. Res. 339:2281-2295(2004) [PubMed: 15337457] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[4]"Comprehensive expression profiling of the pectin methylesterase gene family during silique development in Arabidopsis thaliana."
Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F., Guerineau F., Pelloux J.
Planta 224:782-791(2006) [PubMed: 16622707] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF069298 Genomic DNA. Translation: AAC19272.1.
AL161494 Genomic DNA. Translation: CAB80725.1.
DQ056638 mRNA. Translation: AAY78786.1.
IPIIPI00533008.
PIRT01318.
RefSeqNP_192141.1.
UniGeneAt.54097

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBaseSearch...

Proteomic databases

PRIDEO81301.

Genome annotation databases

GeneID828067.
GenomeReviewsGene locus AT4G02320 in contig CT486007_GR.
KEGGath:AT4G02320.
NMPDRfig|3702.1.peg.18042.

Organism-specific databases

GeneFarm323. 8.
TAIRAt4g02320.

Phylogenomic databases

OMAGRIYHVA.

Gene expression databases

ArrayExpressO81301.
GenevestigatorO81301.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
G3DSA:1.20.140.40. Pectinesterase_inhib. 1 hit.
PfamPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. False negative.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePME40_ARATH
AccessionPrimary (citable) accession number: O81301
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: November 1, 1998
Last modified: November 3, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents