Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5MFV8 (PME5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pectinesterase 5

Short name=PE 5
EC=3.1.1.11
Alternative name(s):
Pectin methylesterase 5
Short name=AtPME5
Pectin methylesterase 67
Short name=AtPME67
Protein VANGUARD 1
Gene names
Name:PME5
Synonyms:ARATH67, VGD1
Ordered Locus Names:At2g47040
ORF Names:F14M4.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length595 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

Cell membrane. Secretedcell wall. Note: Distributed in the whole pollen tube, including the plasma membrane and pollen tube wall. Ref.1

Tissue specificity

Expressed in pollen grains and pollen tubes. Ref.1

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 595571Pectinesterase 5
PRO_0000023477

Sites

Active site4131Proton donor By similarity
Active site4341Nucleophile By similarity
Binding site3601Substrate By similarity
Binding site3901Substrate By similarity
Binding site5031Substrate By similarity
Binding site5051Substrate By similarity
Site4121Transition state stabilizer By similarity

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation3491N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict501D → V in AAV91508. Ref.1
Sequence conflict931G → E in CAB58974. Ref.2
Sequence conflict1381K → E in AAV91508. Ref.1
Sequence conflict2671T → A Ref.1
Sequence conflict2671T → A Ref.2
Sequence conflict5371K → Q in AAV91508. Ref.1
Sequence conflict5451N → S in AAV91508. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5MFV8 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: E314E53201F3CD77

FASTA59564,728
        10         20         30         40         50         60 
MIGKVVVSVA SILLIVGVAI GVVAYINKNG DANLSPQMKA VRGICEATSD KASCVKTLEP 

        70         80         90        100        110        120 
VKSDDPNKLI KAFMLATRDA ITQSSNFTGK TEGNLGSGIS PNNKAVLDYC KKVFMYALED 

       130        140        150        160        170        180 
LSTIVEEMGE DLNQIGSKID QLKQWLTGVY NYQTDCLDDI EEDDLRKTIG EGIASSKILT 

       190        200        210        220        230        240 
SNAIDIFHTV VSAMAKLNLK VEDFKNMTGG IFAPSDKGAA PVNKGTPPVA DDSPVADPDG 

       250        260        270        280        290        300 
PARRLLEDID ETGIPTWVSG ADRKLMTKAG RGSNDGGARI RATFVVAKDG SGQFKTVQQA 

       310        320        330        340        350        360 
VNACPEKNPG RCIIHIKAGI YREQVIIPKK KNNIFMFGDG ARKTVISYNR SVKLSPGTTT 

       370        380        390        400        410        420 
SLSGTVQVES EGFMAKWIGF KNTAGPMGHQ AVAIRVNGDR AVIFNCRFDG YQDTLYVNNG 

       430        440        450        460        470        480 
RQFYRNIVVS GTVDFIFGKS ATVIQNSLIV VRKGNKGQFN TVTADGNEKG LAMKIGIVLQ 

       490        500        510        520        530        540 
NCRIVPDKKL AAERLIVESY LGRPWKKFST TVIINSEIGD VIRPEGWKIW DGESFHKSCR 

       550        560        570        580        590 
YVEYNNRGPG AITNRRVNWV KIARSAAEVN DFTVANWLGP INWIQEANVP VTLGL 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Strain: cv. Landsberg erecta.
[2]"Characterization of a flower-specific gene encoding pectin methylesterase in Arabidopsis thaliana."
Torki M., Mache R., Mandaron P., Falconet D.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Flower bud.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Pectin methylesterases: sequence-structural features and phylogenetic relationships."
Markovic O., Janecek S.
Carbohydr. Res. 339:2281-2295(2004) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Web resources

Protein Spotlight

When tough is soft - Issue 106 of June 2009

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY830948 mRNA. Translation: AAV91508.1.
AJ250430 mRNA. Translation: CAB58974.1.
AC004411 Genomic DNA. Translation: AAC34240.1.
CP002685 Genomic DNA. Translation: AEC10791.1.
AY091768 mRNA. Translation: AAM10316.1.
BT001120 mRNA. Translation: AAN64511.1.
PIRT02183.
T52327.
RefSeqNP_182227.1. NM_130272.3.
UniGeneAt.24875.

3D structure databases

ProteinModelPortalQ5MFV8.
SMRQ5MFV8. Positions 285-595.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid4653. 2 interactions.
STRING3702.AT2G47040.1-P.

Proteomic databases

PaxDbQ5MFV8.
PRIDEQ5MFV8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G47040.1; AT2G47040.1; AT2G47040.
GeneID819318.
KEGGath:AT2G47040.

Organism-specific databases

GeneFarm443. 8.
TAIRAT2G47040.

Phylogenomic databases

eggNOGCOG4677.
HOGENOMHOG000217409.
InParanoidQ5MFV8.
OMATHANILM.
PhylomeDBQ5MFV8.

Enzyme and pathway databases

BioCycARA:AT2G47040-MONOMER.
BRENDA3.1.1.11. 399.
UniPathwayUPA00545; UER00823.

Gene expression databases

GenevestigatorQ5MFV8.

Family and domain databases

Gene3D1.20.140.40. 1 hit.
2.160.20.10. 1 hit.
InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib_dom.
[Graphical view]
PfamPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
SMARTSM00856. PMEI. 1 hit.
[Graphical view]
SUPFAMSSF101148. SSF101148. 1 hit.
SSF51126. SSF51126. 1 hit.
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME5_ARATH
AccessionPrimary (citable) accession number: Q5MFV8
Secondary accession number(s): O80721, Q9SMV9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 14, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names