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O48711 (PME12_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 71. 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 12

Including the following 2 domains:

  1. Pectinesterase inhibitor 12
    Alternative name(s):
    Pectin methylesterase inhibitor 12
  2. Pectinesterase 12
    Short name=PE 12
    EC=3.1.1.11
    Alternative name(s):
    Pectin methylesterase 12
    Short name=AtPME12
Gene names
Name:PME12
Synonyms:ARATH12
Ordered Locus Names:At2g26440
ORF Names:T9J22.11
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 length547 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. Ref.6

Developmental stage

Expressed throughout silique development. 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 caution

The sequence BAD93990.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 547524Probable pectinesterase/pectinesterase inhibitor 12
PRO_0000371669

Regions

Region31 – 185155Pectinesterase inhibitor 12
Region237 – 533297Pectinesterase 12

Sites

Active site3651Proton donor; for pectinesterase activity By similarity
Active site3861Nucleophile; for pectinesterase activity By similarity
Binding site3121Substrate; for pectinesterase activity By similarity
Binding site3421Substrate; for pectinesterase activity By similarity
Binding site4541Substrate; for pectinesterase activity By similarity
Binding site4561Substrate; for pectinesterase activity By similarity
Site3641Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation2471N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation4321N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Glycosylation5231N-linked (GlcNAc...) Potential
Disulfide bond379 ↔ 399 By similarity

Sequences

Sequence LengthMass (Da)Tools
O48711 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 9CEB99E60E6378C7

FASTA54760,417
        10         20         30         40         50         60 
MALSSFNLSS LLFLLFFTPS VFSYSYQPSL NPHETSATSF CKNTPYPDAC FTSLKLSISI 

        70         80         90        100        110        120 
NISPNILSFL LQTLQTALSE AGKLTDLLSG AGVSNNLVEG QRGSLQDCKD LHHITSSFLK 

       130        140        150        160        170        180 
RSISKIQDGV NDSRKLADAR AYLSAALTNK ITCLEGLESA SGPLKPKLVT SFTTTYKHIS 

       190        200        210        220        230        240 
NSLSALPKQR RTTNPKTGGN TKNRRLLGLF PDWVYKKDHR FLEDSSDGYD EYDPSESLVV 

       250        260        270        280        290        300 
AADGTGNFST INEAISFAPN MSNDRVLIYV KEGVYDENID IPIYKTNIVL IGDGSDVTFI 

       310        320        330        340        350        360 
TGNRSVGDGW TTFRSATLAV SGEGFLARDI MITNTAGPEK HQAVALRVNA DFVALYRCVI 

       370        380        390        400        410        420 
DGYQDTLYTH SFRQFYRECD IYGTIDYIFG NAAVVFQGCN IVSKLPMPGQ FTVITAQSRD 

       430        440        450        460        470        480 
TQDEDTGISM QNCSILASED LFNSSNKVKS YLGRPWREFS RTVVMESYID EFIDGSGWSK 

       490        500        510        520        530        540 
WNGGEALDTL YYGEYNNNGP GSETVKRVNW PGFHIMGYED AFNFTATEFI TGDGWLGSTS 


FPYDNGI

« Hide

References

« Hide 'large scale' references
[1]"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.
[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]"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 (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 447-547.
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: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC002505 Genomic DNA. Translation: AAC14493.1.
CP002685 Genomic DNA. Translation: AEC07839.1.
AY072224 mRNA. Translation: AAL60045.1.
AY122952 mRNA. Translation: AAM67485.1.
AK220775 mRNA. Translation: BAD93990.1. Different initiation.
IPIIPI00519605.
PIRT00977.
RefSeqNP_180212.1. NM_128201.4.
UniGeneAt.38895.

3D structure databases

HSSPHSSP built from PDB template 1XG2 based on UniProtKB P14280.
ProteinModelPortalO48711.
SMRO48711. Positions 234-547.
ModBaseSearch...

Proteomic databases

PRIDEO48711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G26440.1; AT2G26440.1; AT2G26440.
GeneID817184.
GenomeReviewsGene locus AT2G26440 in contig CT485783_GR.
KEGGath:AT2G26440.
NMPDRfig|3702.1.peg.9664.

Organism-specific databases

TAIRAt2g26440.

Phylogenomic databases

eggNOGeuNOG09608.
GeneTreeEPGT00070000027901.
HOGENOMHBG747179.
InParanoidO48711.
OMADEYDPSE.
PhylomeDBO48711.
ProtClustDBPLN02416.

Gene expression databases

ArrayExpressO48711.
GenevestigatorO48711.

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 namePME12_ARATH
AccessionPrimary (citable) accession number: O48711
Secondary accession number(s): Q570D4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: June 1, 1998
Last modified: December 14, 2011
This is version 71 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

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