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Reviewed, UniProtKB/Swiss-Prot O80722 (PME4_ARATH)

Last modified February 9, 2010. Version 68. 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:
    Pectinesterase 4
      Short name=PE 4
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase 4
      Short name=AtPME4
    Pectin methylesterase 18
      Short name=AtPME18
    VANGUARD1-like protein 1
      Short name=VGD1-like protein 1
Gene names
Name: PME4
Synonyms: ARATH18, VGDH1
Ordered Locus Names: At2g47030
ORF Names: F14M4.14
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length588 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. Plays an important role in growth of pollen tubes in female floral tissues, possibly via enhancing the interaction between the pollen tube and female floral tissues by modification of the cell walls. Ref.1

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

Secretedcell wall Probable.

Tissue specificity

Expressed in pollen grains and pollen tubes. Ref.1

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 AAN15509.1 differs from that shown. Reason: Miscellaneous discrepancy. Probable cloning artifact leading to a large internal deletion.

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

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

Signal peptide1 – 2424 Potential
Chain25 – 588564Pectinesterase 4
PRO_0000023476

Sites

Active site4061Proton donor By similarity
Active site4271Nucleophile By similarity
Binding site3531Substrate By similarity
Binding site3831Substrate By similarity
Binding site4961Substrate By similarity
Binding site4981Substrate By similarity
Site4051Transition state stabilizer By similarity

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict461Q → R in AAV91509. Ref.1
Sequence conflict2751T → A in AAV91509. Ref.1
Sequence conflict3241K → N in AAV91509. Ref.1
Sequence conflict359 – 3602Missing in AAC27719. Ref.2
Sequence conflict5501V → A in AAV91509. Ref.1
Sequence conflict5631N → S in AAV91509. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O80722-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 70E9A966040D67F2

FASTA58864,138
        10         20         30         40         50         60 
MIGKVVVSVA SILLIVGVAI GVVAFINKNG DANLSPQMKA VQGICQSTSD KASCVKTLEP 

        70         80         90        100        110        120 
VKSEDPNKLI KAFMLATKDE LTKSSNFTGQ TEVNMGSSIS PNNKAVLDYC KRVFMYALED 

       130        140        150        160        170        180 
LATIIEEMGE DLSQIGSKID QLKQWLIGVY NYQTDCLDDI EEDDLRKAIG EGIANSKILT 

       190        200        210        220        230        240 
TNAIDIFHTV VSAMAKINNK VDDLKNMTGG IPTPGAPPVV DESPVADPDG PARRLLEDID 

       250        260        270        280        290        300 
ETGIPTWVSG ADRKLMAKAG RGRRGGRGGG ARVRTNFVVA KDGSGQFKTV QQAVDACPEN 

       310        320        330        340        350        360 
NRGRCIIYIK AGLYREQVII PKKKNNIFMF GDGARKTVIS YNRSVALSRG TTTSLSATVQ 

       370        380        390        400        410        420 
VESEGFMAKW MGFKNTAGPM GHQAAAIRVN GDRAVIFNCR FDGYQDTLYV NNGRQFYRNC 

       430        440        450        460        470        480 
VVSGTVDFIF GKSATVIQNT LIVVRKGSKG QYNTVTADGN ELGLGMKIGI VLQNCRIVPD 

       490        500        510        520        530        540 
RKLTPERLTV ATYLGRPWKK FSTTVIMSTE MGDLIRPEGW KIWDGESFHK SCRYVEYNNR 

       550        560        570        580 
GPGAFANRRV NWAKVARSAA EVNGFTAANW LGPINWIQEA NVPVTIGL 

« Hide

References

« Hide 'large scale' references
[1]"VANGUARD1 encodes a pectin methylesterase that enhances pollen tube growth in the Arabidopsis style and transmitting tract."
Jiang L., Yang S.-L., Xie L.-F., Puah C.S., Zhang X.-Q., Yang W.-C., Sundaresan V., Ye D.
Plant Cell 17:584-596(2005) [PubMed: 15659637] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Strain: cv. Landsberg erecta.
[2]"Molecular characterization of AtPME4: a flower-specific gene encoding pectin methylesterase in Arabidopsis thaliana."
Richard L., Micheli F., Goldberg R.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Wassilewskija.
Tissue: Flower.
[3]"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.
[4]"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.
[5]"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.
[6]"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: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY830949 mRNA. Translation: AAV91509.1.
AF077855 Genomic DNA. Translation: AAC27719.1.
AC004411 Genomic DNA. Translation: AAC34241.1.
AY054462 mRNA. Translation: AAK96654.1.
BT000190 mRNA. Translation: AAN15509.1. Sequence problems.
IPIIPI00546660.
PIRT02184.
T52330.
RefSeqNP_182226.1.
UniGeneAt.22342

3D structure databases

SMRO80722. Positions 39-188, 271-588.
ModBaseSearch...

Proteomic databases

PRIDEO80722.

Genome annotation databases

GeneID819317.
GenomeReviewsGene locus AT2G47030 in contig CT485783_GR.
KEGGath:AT2G47030.
NMPDRfig|3702.1.peg.11894.

Organism-specific databases

GeneFarm161. 8.
TAIRAt2g47030.

Phylogenomic databases

eggNOGCOG4677.
HOGENOMHBG747179.
InParanoidO80722.
OMASVEHTES.

Enzyme and pathway databases

BRENDA3.1.1.11. 302.

Gene expression databases

GenevestigatorO80722.
GermOnlineAT2G47030. Arabidopsis thaliana.

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]
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME4_ARATH
AccessionPrimary (citable) accession number: O80722
Secondary accession number(s): Q5MFV7, Q8H194, Q9T0P8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1998
Last modified: February 9, 2010
This is version 68 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