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Reviewed, UniProtKB/Swiss-Prot Q3E8Z8 (PME28_ARATH)

Last modified November 3, 2009. Version 27. 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:
    Putative pectinesterase/pectinesterase inhibitor 28
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 28
        Alternative name(s):
            Pectin methylesterase inhibitor 28
    2- Recommended name:
            Pectinesterase 28
                Short name=PE 28
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 28
              Short name=AtPME28
Gene names
Name: PME28
Synonyms: ARATH28
Ordered Locus Names: At5g27870
ORF Names: F14I23.30
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 length732 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

Membrane; Single-pass membrane protein Potential.

Tissue specificity

Expressed in flower buds. Ref.3

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
   Cellular componentMembrane
   DomainTransmembrane
   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: InterPro

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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

Chain1 – 732732Putative pectinesterase/pectinesterase inhibitor 28
PRO_0000371681

Regions

Transmembrane17 – 3721 Potential
Region51 – 204154Pectinesterase inhibitor 28
Region252 – 548297Pectinesterase 28
Compositional bias595 – 727133Pro-rich

Sites

Active site3801Proton donor; for pectinesterase activity By similarity
Active site4011Nucleophile; for pectinesterase activity By similarity
Binding site3271Substrate; for pectinesterase activity By similarity
Binding site3571Substrate; for pectinesterase activity By similarity
Binding site4691Substrate; for pectinesterase activity By similarity
Binding site4711Substrate; for pectinesterase activity By similarity
Site3791Transition state stabilizer By similarity

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation4131N-linked (GlcNAc...) Potential
Glycosylation5661N-linked (GlcNAc...) Potential
Glycosylation5701N-linked (GlcNAc...) Potential
Glycosylation5811N-linked (GlcNAc...) Potential
Disulfide bond394 ↔ 414 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q3E8Z8-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: DF433495A0BAAA13

FASTA73278,477
        10         20         30         40         50         60 
MSYGYDDEDA KRKKRYVIIS ISSVLLISMV VAVTIGVSVN KSDNAGDEEI TTSVKAIKDV 

        70         80         90        100        110        120 
CAPTDYKETC EDTLRKDAKD TSDPLELVKT AFNATMKQIS DVAKKSQTMI ELQKDPRAKM 

       130        140        150        160        170        180 
ALDQCKELMD YAIGELSKSF EELGKFEFHK VDEALVKLRI WLSATISHEQ TCLDGFQGTQ 

       190        200        210        220        230        240 
GNAGETIKKA LKTAVQLTHN GLAMVTEMSN YLGQMQIPEM NSRRLLSQEF PSWMDARARR 

       250        260        270        280        290        300 
LLNAPMSEVK PDIVVAQDGS GQYKTINEAL NFVPKKKNTT FVVHIKEGIY KEYVQVNRSM 

       310        320        330        340        350        360 
THLVFIGDGP DKTVISGSKS YKDGITTYKT ATVAIVGDHF IAKNIAFENT AGAIKHQAVA 

       370        380        390        400        410        420 
IRVLADESIF YNCKFDGYQD TLYAHSHRQF YRDCTISGTI DFLFGDAAAV FQNCTLLVRK 

       430        440        450        460        470        480 
PLLNQACPIT AHGRKDPRES TGFVLQGCTI VGEPDYLAVK EQSKTYLGRP WKEYSRTIIM 

       490        500        510        520        530        540 
NTFIPDFVPP EGWQPWLGEF GLNTLFYSEV QNTGPGAAIT KRVTWPGIKK LSDEEILKFT 

       550        560        570        580        590        600 
PAQYIQGDAW IPGKGVPYIL GLFSGNGSTN STVTGSSLSS NTTESSDSPS TVVTPSTSPP 

       610        620        630        640        650        660 
AGHLGSPSDT PSSVVSPSTS LPAGQLGAPP ATPSMVVSPS TSPPAGHLGS PSDTPSSLVS 

       670        680        690        700        710        720 
PSTSPPAGHL GSPSDTPSSV VTPSASPSTS PSASPSVSPS AFPSASPSAS PSASPSVSPS 

       730 
ASPSASPQSS IG

« Hide

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed: 11130714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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.
[3]"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

AC007399 Genomic DNA. No translation available.
IPIIPI00528211.
RefSeqNP_198139.1.
UniGeneAt.55044

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEQ3E8Z8.

Genome annotation databases

GeneID832850.
GenomeReviewsGene locus AT5G27870 in contig BA000015_GR.
KEGGath:AT5G27870.
NMPDRfig|3702.1.peg.24990.

Organism-specific databases

TAIRAt5g27870.

Phylogenomic databases

OMACTITGTI.

Gene expression databases

GenevestigatorQ3E8Z8.

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. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePME28_ARATH
AccessionPrimary (citable) accession number: Q3E8Z8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: November 8, 2005
Last modified: November 3, 2009
This is version 27 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