Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9ZQA3 (PME15_ARATH)

Last modified November 3, 2009. Version 47. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Probable pectinesterase 15
      Short name=PE 15
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase 15
      Short name=AtPME15
Gene names
Name: PME15
Synonyms: ARATH15
Ordered Locus Names: At2g36710
ORF Names: F13K3.11
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

Hide | Top

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

Hide | Top

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.4

Developmental stage

Expressed throughout silique development. Ref.4

Sequence similarities

Belongs to the pectinesterase family.

Hide | Top

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionAspartyl esterase
Hydrolase
   PTMGlycoprotein
   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

pectinesterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 407385Probable pectinesterase 15
PRO_0000371672

Regions

Compositional bias50 – 6819His-rich

Sites

Active site2231Proton donor By similarity
Active site2441Nucleophile By similarity
Binding site1651Substrate By similarity
Binding site2001Substrate By similarity
Binding site3051Substrate By similarity
Site2221Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation2661N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2441D → G in AAO22722. Ref.2

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q9ZQA3-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: DBAB7B8E166D0B42

FASTA40744,973
        10         20         30         40         50         60 
MPIKPVLTTL IALLSIILAL YTIQLPSSRS LSSIATTIGA LAKYSTFFGH KHHHHHHHHH 

        70         80         90        100        110        120 
HHHHYHHHEP IKCCEKWTSR LRHQYKTSLV LTVDLHGCGN FSNVQSAIDV VPDLSSSKTL 

       130        140        150        160        170        180 
IIVNSGSYRE KVTVNENKTN LVIQGRGYQN TSIEWNDTAK SAGNTADSFS FVVFAANFTA 

       190        200        210        220        230        240 
YNISFKNNAP EPDPGEADAQ AVALRIEGDQ AAFYGCGFYG AQDTLLDDKG RHFFKECFIQ 

       250        260        270        280        290        300 
GSIDFIFGNG RSLYQDCTIN SIAKGNTSGV TGSITAQGRQ SEDEQSGFSF VNCKIDGSGE 

       310        320        330        340        350        360 
ILLGRAWGAY ATVVFSNTYM SGIITPEGWN NWGDSTKEKT VTFGEHKCYG PGADYKERVL 

       370        380        390        400 
FGKQLTDSEA SSFIDVSFID GDEWLRHTNI VSEHTSKDIG DDLIGFY

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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].
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.

Hide | Top

Cross-references

Sequence databases

AC006282 Genomic DNA. Translation: AAD20147.1.
BT002906 mRNA. Translation: AAO22722.1.
IPIIPI00517565.
PIRG84783.
RefSeqNP_181209.1.
UniGeneAt.37520

3D structure databases

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

Genome annotation databases

GeneID818243.
GenomeReviewsGene locus AT2G36710 in contig CT485783_GR.
KEGGath:AT2G36710.
NMPDRfig|3702.1.peg.10775.

Organism-specific databases

GeneFarm460. 8.
TAIRAt2g36710.

Phylogenomic databases

OMAWLGRAWG.

Gene expression databases

GenevestigatorQ9ZQA3.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF01095. Pectinesterase. 1 hit.
[Graphical view]
PROSITEPS00800. PECTINESTERASE_1. False negative.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry namePME15_ARATH
AccessionPrimary (citable) accession number: Q9ZQA3
Secondary accession number(s): Q84WQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 1, 1999
Last modified: November 3, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

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