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Q5MFV6 (PME37_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable pectinesterase/pectinesterase inhibitor VGDH2
Alternative name(s):
VANGUARD1-like protein 2
Short name=VGD1-like protein 2

Including the following 2 domains:

  1. Pectinesterase inhibitor VGDH2
    Alternative name(s):
    Pectin methylesterase inhibitor VGDH2
  2. Pectinesterase VGDH2
    Short name=PE VGDH2
    EC=3.1.1.11
    Alternative name(s):
    Pectin methylesterase 37
    Short name=AtPME37
    Pectin methylesterase VGDH2
Gene names
Name:VGDH2
Synonyms:ARATH37
Ordered Locus Names:At3g62170
ORF Names:T17J13.130
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

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 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 Probable.

Tissue specificity

Expressed in flower buds, 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 588566Probable pectinesterase/pectinesterase inhibitor VGDH2
PRO_0000023478

Regions

Region42 – 193152Pectinesterase inhibitor VGDH2
Region276 – 574299Pectinesterase VGDH2
Compositional bias262 – 27110Poly-Gly

Sites

Active site4061Proton donor; for pectinesterase activity By similarity
Active site4271Nucleophile; for pectinesterase activity By similarity
Binding site3531Substrate; for pectinesterase activity By similarity
Binding site3831Substrate; for pectinesterase activity By similarity
Binding site4961Substrate; for pectinesterase activity By similarity
Binding site4981Substrate; for pectinesterase activity By similarity
Site4051Transition state stabilizer By similarity

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict531Q → L in AAV91510. Ref.1
Sequence conflict1651D → G in AAV91510. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5MFV6 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: BAEF057677EA7848

FASTA58862,958
        10         20         30         40         50         60 
MAVGKVVVSV ASLLLVVGVA IGVITFVNKG GGANGDSNGP INSHQKAVQT ICQSTTDQGS 

        70         80         90        100        110        120 
CAKTLDPVKS DDPSKLVKAF LMATKDAITK SSNFTASTEG GMGTNMNATS KAVLDYCKRV 

       130        140        150        160        170        180 
LMYALEDLET IVEEMGEDLQ QSGTKLDQLK QWLTGVFNYQ TDCLDDIEEV ELKKIMGEGI 

       190        200        210        220        230        240 
SNSKVLTSNA IDIFHSVVTA MAQMGVKVDD MKNITMGAGA GGAARRLLED NDSKGLPKWF 

       250        260        270        280        290        300 
SGKDRKLMAK AGRGAPAGGD DGIGEGGGGG GKIKATHVVA KDGSGQFKTI SEAVMACPDK 

       310        320        330        340        350        360 
NPGRCIIHIK AGIYNEQVRI PKKKNNIFMF GDGATQTIIT FDRSVKLSPG TTTSLSGTVQ 

       370        380        390        400        410        420 
VESEGFMAKW IGFKNTAGPL GHQAVALRVN GDRAVIFNCR FDGYQDTLYV NNGRQFYRNI 

       430        440        450        460        470        480 
VVSGTVDFIF GKSATVIQNS LILVRKGSPG QSNYVTADGN EKGAAMKIGI VLHNCRIIPD 

       490        500        510        520        530        540 
KELEADKLTI KSYLGRPWKK FATTVIIGTE IGDLIKPEGW TEWQGEQNHK TAKYIEFNNR 

       550        560        570        580 
GPGAATTQRP PWVKVAKSAA EVETYTVANW VGPANWIQEA NVPVQLGL

« 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], TISSUE SPECIFICITY.
Strain: cv. Landsberg erecta.
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
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]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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		AY830950 mRNA. Translation: AAV91510.1.
AL138651 Genomic DNA. Translation: CAB71877.1.
CP002686 Genomic DNA. Translation: AEE80318.1.
AY093237 mRNA. Translation: AAM13236.1.
AY084580 mRNA. Translation: AAM61145.1.
IPIIPI00532727.
PIRT48009.
RefSeqNP_191776.1. NM_116082.2.
UniGeneAt.34168.

3D structure databases

ProteinModelPortalQ5MFV6.
SMRQ5MFV6. Positions 272-588.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5MFV6.

Proteomic databases

PRIDEQ5MFV6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G62170.1; AT3G62170.1; AT3G62170.
GeneID825390.
GenomeReviewsGene locus AT3G62170 in contig BA000014_GR.
KEGGath:AT3G62170.
NMPDRfig|3702.1.peg.17600.

Organism-specific databases

GeneFarm445. 8.
TAIRAt3g62170.

Phylogenomic databases

eggNOGCOG4677.
GeneTreeEPGT00070000028024.
HOGENOMHBG747179.
InParanoidQ5MFV6.
OMAANWIQEA.
PhylomeDBQ5MFV6.
ProtClustDBPLN02197.

Enzyme and pathway databases

BRENDA3.1.1.11. 399.

Gene expression databases

GenevestigatorQ5MFV6.
GermOnlineAT3G62170. 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]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
SSF101148. Pectinesterase_inhib. 1 hit.
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME37_ARATH
AccessionPrimary (citable) accession number: Q5MFV6
Secondary accession number(s): Q9M1Q7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: December 14, 2011
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents