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Q94CB1 (PME25_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable pectinesterase/pectinesterase inhibitor 25

Including the following 2 domains:

  1. Pectinesterase inhibitor 25
    Alternative name(s):
    Pectin methylesterase inhibitor 25
  2. Pectinesterase 25
    Short name=PE 25
    EC=3.1.1.11
    Alternative name(s):
    Pectin methylesterase 25
    Short name=AtPME25
Gene names
Name:PME25
Synonyms:ARATH25
Ordered Locus Names:At3g10720
ORF Names:T7M13.20
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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 siliques. Ref.7

Developmental stage

Expressed throughout silique development. Ref.7

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.

Sequence caution

The sequence AAF19577.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

cellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

   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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q94CB1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q94CB1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-356: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 619596Probable pectinesterase/pectinesterase inhibitor 25
PRO_0000371680

Regions

Region73 – 231159Pectinesterase inhibitor 25
Region302 – 601300Pectinesterase 25
Compositional bias32 – 8958Pro-rich

Sites

Active site4331Proton donor; for pectinesterase activity By similarity
Active site4541Nucleophile; for pectinesterase activity By similarity
Binding site3801Substrate; for pectinesterase activity By similarity
Binding site4101Substrate; for pectinesterase activity By similarity
Binding site5221Substrate; for pectinesterase activity By similarity
Binding site5241Substrate; for pectinesterase activity By similarity
Site4321Transition state stabilizer By similarity

Amino acid modifications

Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation3121N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation3641N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential
Glycosylation5001N-linked (GlcNAc...) Potential
Glycosylation5501N-linked (GlcNAc...) Potential
Glycosylation5911N-linked (GlcNAc...) Potential
Glycosylation5961N-linked (GlcNAc...) Potential
Disulfide bond447 ↔ 467 By similarity

Natural variations

Alternative sequence1 – 356356Missing in isoform 2.
VSP_037088

Experimental info

Sequence conflict3591M → I in AAM67242. Ref.4
Sequence conflict3641N → K in AAM67242. Ref.4
Sequence conflict5121E → D in AAM67242. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: C37A7FE1B9A2B0C5

FASTA61967,956
        10         20         30         40         50         60 
MKMQTLNFTS SLLFLSFIFL SCALLISSQQ SPSQPHSEPP SQLPFEPPVE SPFFPPSQPP 

        70         80         90        100        110        120 
IFVPPSQPPS LPPSQSQSPS LACKSTPYPK LCRTILNAVK SSPSDPYRYG KFTIKQCLKQ 

       130        140        150        160        170        180 
ASRLSKVITS YARRVESKPG SATAEEIGAV ADCGELSELS VNYLETVTTE LKTAQVMTAA 

       190        200        210        220        230        240 
LVEHVNSLLS GVVTNQQTCL DGLVEAKSGF AAAIGSPMGN LTRLYSISLG LVSHALNRNL 

       250        260        270        280        290        300 
KRFKASKGKI LGGGNSTYRE PLETLIKGLR KTCDNDKDCR KTSRNLGELG ETSGGSILVS 

       310        320        330        340        350        360 
KAVIVGPFKS DNFTTITDAI AAAPNNTRPE DGYFVIYARE GVYEEYIVVP INKKNLMLMG 

       370        380        390        400        410        420 
DGINKTIITG NHNVVDGWTT YNCSSFAVVG ERFMAVDVTF RNTAGPEKHQ AVALRNNAEG 

       430        440        450        460        470        480 
SSFYRCSFEG YQDTLYVHSL RQFYRECDIY GTVDFIFGNA AAIFQNCNIY ARKPMAKQKN 

       490        500        510        520        530        540 
AITAHGRLDP NQNTGISIIN CTIKAAPDLA AEPKSAMTFL GRPWKPYSRT VFMQSYISDI 

       550        560        570        580        590        600 
VQPVGWLEWN GTIGLDTIYY GEYSNFGPGA NTNQRVQWLG YNLLNLAEAM NFTVYNFTMG 

       610 
DTWLPQTDIP FYGGLLSKE

« Hide

Isoform 2 [UniParc].

Checksum: 20129070A273EAD8
Show »

FASTA26329,517

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"Arabidopsis ORF clones."
Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
[6]"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.
[7]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC011708 Genomic DNA. Translation: AAF19577.1. Different initiation.
CP002686 Genomic DNA. Translation: AEE74946.1.
CP002686 Genomic DNA. Translation: AEE74947.1.
AY034996 mRNA. Translation: AAK59501.1.
AY084383 mRNA. Translation: AAM67242.1.
BT029534 mRNA. Translation: ABL66790.1.
IPIIPI00528952.
IPI00534987.
RefSeqNP_187683.2. NM_111908.4.
NP_566379.1. NM_111909.1.
UniGeneAt.19163.

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortalQ94CB1.
SMRQ94CB1. Positions 298-615.
ModBaseSearch...

Proteomic databases

PRIDEQ94CB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G10720.2; AT3G10720.2; AT3G10720.
GeneID820241.
GenomeReviewsGene locus AT3G10720 in contig BA000014_GR.
KEGGath:AT3G10720.

Organism-specific databases

TAIRAt3g10720.

Phylogenomic databases

eggNOGCOG4677.
GeneTreeEPGT00070000027901.
InParanoidQ94CB1.
OMATVYNFTM.
PhylomeDBQ94CB1.
ProtClustDBPLN03043.

Gene expression databases

ArrayExpressQ94CB1.
GenevestigatorQ94CB1.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
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]
SMARTSM00856. PMEI. 1 hit.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
SSF101148. Pectinesterase_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. False negative.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME25_ARATH
AccessionPrimary (citable) accession number: Q94CB1
Secondary accession number(s): Q3EB96, Q8LGA3, Q9SG78
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: December 1, 2001
Last modified: December 14, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents