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Reviewed, UniProtKB/Swiss-Prot Q9SRX4 (PME7_ARATH)

Last modified November 3, 2009. Version 51. 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 7
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 7
        Alternative name(s):
            Pectin methylesterase inhibitor 7
    2- Recommended name:
            Pectinesterase 7
                Short name=PE 7
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 7
            Pectin methylesterase 1
              Short name=AtPME1
Gene names
Name: PME7
Synonyms: ARATH1
Ordered Locus Names: At1g02810
ORF Names: F22D16.20
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 length579 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 siliques. Ref.5

Developmental stage

Expressed throughout silique development. 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.

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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 – 2020 Potential
Chain21 – 579559Probable pectinesterase/pectinesterase inhibitor 7
PRO_0000371664

Regions

Region22 – 185164Pectinesterase inhibitor 7
Region265 – 564300Pectinesterase 7
Compositional bias193 – 1964Poly-Lys

Sites

Active site3951Proton donor; for pectinesterase activity By similarity
Active site4161Nucleophile; for pectinesterase activity By similarity
Binding site3421Substrate; for pectinesterase activity By similarity
Binding site3721Substrate; for pectinesterase activity By similarity
Binding site4841Substrate; for pectinesterase activity By similarity
Binding site4861Substrate; for pectinesterase activity By similarity
Site3941Transition state stabilizer By similarity

Amino acid modifications

Glycosylation271N-linked (GlcNAc...) Potential
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation2771N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation3261N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation4621N-linked (GlcNAc...) Potential
Glycosylation4751N-linked (GlcNAc...) Potential
Glycosylation5261N-linked (GlcNAc...) Potential
Glycosylation5331N-linked (GlcNAc...) Potential
Glycosylation5471N-linked (GlcNAc...) Potential
Glycosylation5531N-linked (GlcNAc...) Potential
Disulfide bond409 ↔ 429 By similarity

Experimental info

Sequence conflict4161D → N in BAF00855. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q9SRX4-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FE3543E143B109DE

FASTA57963,952
        10         20         30         40         50         60 
MESPIFILIT LSFFLQSVLA SSQTLSNSST ICKTTPDPKY CKSVFPHSQG NVQQYGCFSI 

        70         80         90        100        110        120 
RKSLSQSRKF IRTVDRYIKR NAHLSQPAVI RALQDCRFLA GLTMDYLLTS FETVNDTSAK 

       130        140        150        160        170        180 
TSFKPLSFPK ADDIQTLLSA ALTNEQTCLE GLTTAASYSA TWTVRTGVAL PLVNDTKLLG 

       190        200        210        220        230        240 
VSLALFTKGW VPKKKKRAGF AWAQPRSGSS THTKPFRLFR NGALPLKMTE KTKAVYESLS 

       250        260        270        280        290        300 
RRKLADGDSN GDGDDGSMVL ISDIVTVSQD GTGNFTNITA AVAAAPNNTD GSAGFFLIYV 

       310        320        330        340        350        360 
TAGIYEEYIS IAKNKRYMMM IGDGINQTVV TGNRSVVDGW TTFNSATFAV TAPNFVAVNI 

       370        380        390        400        410        420 
TFRNTAGPEK HQAVALRSGA DFSIFYSCSF EAYQDTLYTH SLRQFYRECD VYGTVDFIFG 

       430        440        450        460        470        480 
NAAVVFQNCN LYPRKPMPNQ FNAITAQGRS DPNQNTGTSI QNCTIKPADD LVSSNYTVKT 

       490        500        510        520        530        540 
YLGRPWKEYS RTVYMQSYID GFVEPVGWRE WNGDFALSTL YYAEYNNTGP GSNTTNRVTW 

       550        560        570 
PGYHVINSTD AANFTVTGLF IEADWIWKTG VPYTSGLIS

« Hide

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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.
[3]"Arabidopsis ORF clones."
Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [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.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AC009525 Genomic DNA. Translation: AAF02886.1.
AK228966 mRNA. Translation: BAF00855.1.
BT030371 mRNA. Translation: ABO38784.1.
IPIIPI00528323.
PIRB86158.
RefSeqNP_563662.1.
UniGeneAt.42579

3D structure databases

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

Proteomic databases

PRIDEQ9SRX4.

Genome annotation databases

GeneID838078.
GenomeReviewsGene locus AT1G02810 in contig CT485782_GR.
KEGGath:AT1G02810.
NMPDRfig|3702.1.peg.402.

Organism-specific databases

GeneFarm409. 8.
TAIRAt1g02810.

Phylogenomic databases

OMANSSTICK.

Gene expression databases

GenevestigatorQ9SRX4.

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.
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 namePME7_ARATH
AccessionPrimary (citable) accession number: Q9SRX4
Secondary accession number(s): Q0WPU4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 51 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