Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9LYT5 (PME35_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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 35

Including the following 2 domains:

  1. Pectinesterase inhibitor 35
    Alternative name(s):
    Pectin methylesterase inhibitor 35
  2. Pectinesterase 35
    Short name=PE 35
    EC=3.1.1.11
    Alternative name(s):
    Pectin methylesterase 35
    Short name=AtPME35
Gene names
Name:PME35
Synonyms:ARATH35
Ordered Locus Names:At3g59010
ORF Names:F17J16.60
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 length529 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 By similarity.

Tissue specificity

Expressed in siliques and trichomes. Ref.5 Ref.6

Developmental stage

Expressed during late developmental phases of siliques. Ref.6

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 – 3434 Potential
Chain35 – 529495Probable pectinesterase/pectinesterase inhibitor 35
PRO_0000371687

Regions

Region36 – 180145Pectinesterase inhibitor 35
Region228 – 514287Pectinesterase 35
Compositional bias27 – 7347Ser-rich
Compositional bias188 – 1925Poly-Ser

Sites

Active site3551Proton donor; for pectinesterase activity By similarity
Active site3761Nucleophile; for pectinesterase activity By similarity
Binding site3021Substrate; for pectinesterase activity By similarity
Binding site3321Substrate; for pectinesterase activity By similarity
Binding site4341Substrate; for pectinesterase activity By similarity
Binding site4361Substrate; for pectinesterase activity By similarity
Site3541Transition state stabilizer By similarity

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation1691N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9LYT5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1DB3E14632285F79

FASTA52957,513
        10         20         30         40         50         60 
MATTSFSLPN HKFGIKLMLF LVLNLLSLQT SVFAHSSNSK FTKISRHPNS DSSSRTKPST 

        70         80         90        100        110        120 
SSNKGFLSSV QLSLDHALFA RSLAFNLTLS HRTSQTLMLD PVNDCLELLD DTLDMLYRIV 

       130        140        150        160        170        180 
VIKRKDHVND DVHTWLSAAL TNQETCKQSL SEKSSFNKEG IAIDSFARNL TGLLTNSLDM 

       190        200        210        220        230        240 
FVSDKQKSSS SSNLTGGRKL LSDHDFPTWV SSSDRKLLEA SVEELRPHAV VAADGSGTHM 

       250        260        270        280        290        300 
SVAEALASLE KGSGRSVIHL TAGTYKENLN IPSKQKNVML VGDGKGKTVI VGSRSNRGGW 

       310        320        330        340        350        360 
NTYQSATVAA MGDGFIARDI TFVNSAGPNS EQAVALRVGS DRSVVYRCSI DGYQDSLYTL 

       370        380        390        400        410        420 
SKRQFYRETD ITGTVDFIFG NSAVVFQSCN LVSRKGSSDQ NYVTAQGRSD PNQNTGISIH 

       430        440        450        460        470        480 
NCRITGSTKT YLGRPWKQYS RTVVMQSFID GSIHPSGWSP WSSNFALKTL YYGEFGNSGP 

       490        500        510        520 
GSSVSGRVSW AGYHPALTLT EAQGFTVSGF IDGNSWLPST GVVFDSGLL

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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.
[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]"Cell-specific protein profiling in Arabidopsis thaliana trichomes: identification of trichome-located proteins involved in sulfur metabolism and detoxification."
Wienkoop S., Zoeller D., Ebert B., Simon-Rosin U., Fisahn J., Glinski M., Weckwerth W.
Phytochemistry 65:1641-1649(2004) [PubMed: 15276459] [Abstract]
Cited for: TISSUE SPECIFICITY.
[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: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL163527 Genomic DNA. Translation: CAB86929.1.
CP002686 Genomic DNA. Translation: AEE79860.1.
AY060590 mRNA. Translation: AAL31215.1.
BT001078 mRNA. Translation: AAN46858.1.
IPIIPI00533350.
PIRT47783.
RefSeqNP_191460.1. NM_115763.2.
UniGeneAt.5019.
At.66487.
At.67354.

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortalQ9LYT5.
SMRQ9LYT5. Positions 223-528.
ModBaseSearch...

Proteomic databases

PRIDEQ9LYT5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G59010.1; AT3G59010.1; AT3G59010.
GeneID825070.
GenomeReviewsGene locus AT3G59010 in contig BA000014_GR.
KEGGath:AT3G59010.
NMPDRfig|3702.1.peg.17246.

Organism-specific databases

GeneFarm325. 8.
TAIRAt3g59010.

Phylogenomic databases

eggNOGCOG4677.
GeneTreeEPGT00070000027901.
HOGENOMHBG747179.
InParanoidQ9LYT5.
OMAMQSFIDG.
PhylomeDBQ9LYT5.
ProtClustDBPLN02170.

Gene expression databases

GenevestigatorQ9LYT5.

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.
PROSITEPS00800. PECTINESTERASE_1. False negative.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME35_ARATH
AccessionPrimary (citable) accession number: Q9LYT5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: October 1, 2000
Last modified: December 14, 2011
This is version 65 of the entry and version 1 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