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Reviewed, UniProtKB/Swiss-Prot Q7Y201 (PME13_ARATH)

Last modified October 13, 2009. Version 37. 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

Names and origin

Protein namesRecommended name:
    Probable pectinesterase/pectinesterase inhibitor 13
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 13
        Alternative name(s):
            Pectin methylesterase inhibitor 13
    2- Recommended name:
            Pectinesterase 13
                Short name=PE 13
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 13
              Short name=AtPME13
Gene names
Name: PME13
Synonyms: ARATH13
Ordered Locus Names: At2g26450
ORF Names: T9J22.12
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

Membrane; Single-pass membrane protein Potential.

Tissue specificity

Expressed in flower buds. Ref.5

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.

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 614614Probable pectinesterase/pectinesterase inhibitor 13
PRO_0000371670

Regions

Transmembrane25 – 4521 Potential
Region103 – 255153Pectinesterase inhibitor 13
Region301 – 598298Pectinesterase 13
Compositional bias55 – 617Poly-Gln

Sites

Active site4291Proton donor; for pectinesterase activity By similarity
Active site4501Nucleophile; for pectinesterase activity By similarity
Binding site3761Substrate; for pectinesterase activity By similarity
Binding site4061Substrate; for pectinesterase activity By similarity
Binding site5181Substrate; for pectinesterase activity By similarity
Binding site5201Substrate; for pectinesterase activity By similarity
Site4281Transition state stabilizer By similarity

Amino acid modifications

Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation2431N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential
Glycosylation3511N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential
Glycosylation5221N-linked (GlcNAc...) Potential
Glycosylation5881N-linked (GlcNAc...) Potential
Disulfide bond443 ↔ 463 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7Y201-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 2DC7535F11DE9B89

FASTA61468,533
        10         20         30         40         50         60 
MAFQDFDKIQ ERVNANRKRK FRKRIIVGTV SLLVVVAAIV GGAFAYVAYE KRNEQQQQQQ 

        70         80         90        100        110        120 
QAKNHNKSGS GNNVVKDSDK KSPSPPTPSQ KAPVSAAQSV KPGQGDKIIQ TLCSSTLYMQ 

       130        140        150        160        170        180 
ICEKTLKNRT DKGFALDNPT TFLKSAIEAV NEDLDLVLEK VLSLKTENQD DKDAIEQCKL 

       190        200        210        220        230        240 
LVEDAKEETV ASLNKINVTE VNSFEKVVPD LESWLSAVMS YQETCLDGFE EGNLKSEVKT 

       250        260        270        280        290        300 
SVNSSQVLTS NSLALIKTFT ENLSPVMKVV ERHLLDGIPS WVSNDDRRML RAVDVKALKP 

       310        320        330        340        350        360 
NATVAKDGSG DFTTINDALR AMPEKYEGRY IIYVKQGIYD EYVTVDKKKA NLTMVGDGSQ 

       370        380        390        400        410        420 
KTIVTGNKSH AKKIRTFLTA TFVAQGEGFM AQSMGFRNTA GSEGHQAVAI RVQSDRSIFL 

       430        440        450        460        470        480 
NCRFEGYQDT LYAYTHRQYY RSCVIVGTID FIFGDAAAIF QNCNIFIRKG LPGQKNTVTA 

       490        500        510        520        530        540 
QGRVDKFQTT GFVVHNCKIA ANEDLKPVKE EYKSYLGRPW KNYSRTIIME SKIENVIDPV 

       550        560        570        580        590        600 
GWLRWQETDF AIDTLYYAEY NNKGSSGDTT SRVKWPGFKV INKEEALNYT VGPFLQGDWI 

       610 
SASGSPVKLG LYDA 

« Hide

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]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"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.
[5]"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.

Cross-references

Sequence databases

AC002505 Genomic DNA. Translation: AAC14494.1. Different initiation.
BT008681 mRNA. Translation: AAP40488.1.
AK229600 mRNA. Translation: BAF01447.1.
IPIIPI00521390.
PIRT00978.

3D structure databases

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

Genome annotation databases

GenomeReviewsGene locus AT2G26450 in contig CT485783_GR.

Organism-specific databases

GeneFarm229. 8.
TAIRAt2g26450.

Gene expression databases

GenevestigatorQ7Y201.

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...

Entry information

Entry namePME13_ARATH
AccessionPrimary (citable) accession number: Q7Y201
Secondary accession number(s): O48712
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: October 1, 2003
Last modified: October 13, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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