Pectinesterase 5 precursor - Arabidopsis thaliana (Mouse-ear cress)

Contribute

Send feedback

Read comments (?) or add your own

Q5MFV8 (PME5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	595 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Secreted › cell 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.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell membrane Cell wall Membrane Secreted
Domain	Signal
Molecular function	Aspartyl esterase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell wall modification Inferred from electronic annotation. Source: InterPro negative regulation of catalytic activity Inferred from electronic annotation. Source: GOC pectin catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway pollen tube growth Traceable author statement Ref.1. Source: TAIR
Cellular_component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell pollen tube Inferred from direct assay Ref.1. Source: TAIR
Molecular_function	aspartyl 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

Potential

Chain

25 – 595

571

Pectinesterase 5

PRO_0000023477

Sites

Active site

413

Proton donor By similarity

Active site

434

Nucleophile By similarity

Binding site

360

Substrate By similarity

Binding site

390

Substrate By similarity

Binding site

503

Substrate By similarity

Binding site

505

Substrate By similarity

Site

412

Transition state stabilizer By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

206

N-linked (GlcNAc...) Potential

Glycosylation

349

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

D → V in AAV91508. Ref.1

Sequence conflict

G → E in CAB58974. Ref.2

Sequence conflict

138

K → E in AAV91508. Ref.1

Sequence conflict

267

T → A Ref.1

Sequence conflict

267

T → A Ref.2

Sequence conflict

537

K → Q in AAV91508. Ref.1

Sequence conflict

545

N → S in AAV91508. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q5MFV8 [UniParc].

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

FASTA

595

64,728

        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' referencesShow '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. 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. 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.
IPI	IPI00525113.
PIR	T02183. T52327.
RefSeq	NP_182227.1. NM_130272.3.
UniGene	At.24875.
3D structure databases
ProteinModelPortal	Q5MFV8.
SMR	Q5MFV8. Positions 285-595.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT2G47040.1-P.
Proteomic databases
PaxDb	Q5MFV8.
PRIDE	Q5MFV8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G47040.1; AT2G47040.1; AT2G47040.
GeneID	819318.
KEGG	ath:AT2G47040.
Organism-specific databases
GeneFarm	443. 8.
TAIR	At2g47040.
Phylogenomic databases
eggNOG	COG4677.
HOGENOM	HOG000217409.
InParanoid	Q5MFV8.
OMA	EGIASSK.
PhylomeDB	Q5MFV8.
ProtClustDB	PLN02197.
Enzyme and pathway databases
BRENDA	3.1.1.11. 399.
UniPathway	UPA00545; UER00823.
Gene expression databases
Genevestigator	Q5MFV8.
GermOnline	AT2G47040. Arabidopsis thaliana.
Family and domain databases
Gene3D	1.20.140.40. 1 hit. 2.160.20.10. 1 hit.
InterPro	IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. IPR018040. Pectinesterase_AS. IPR000070. Pectinesterase_cat. IPR006501. Pectinesterase_inhib. [Graphical view]
Pfam	PF01095. Pectinesterase. 1 hit. PF04043. PMEI. 1 hit. [Graphical view]
SMART	SM00856. PMEI. 1 hit. [Graphical view]
SUPFAM	SSF51126. Pectin_lyas_like. 1 hit. SSF101148. Pectinesterase_inhib. 1 hit.
TIGRFAMs	TIGR01614. PME_inhib. 1 hit.
PROSITE	PS00800. PECTINESTERASE_1. 1 hit. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME5_ARATH

Accession

Primary (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 1, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents