Reviewed, UniProtKB/Swiss-Prot Q5MFV8 (PME5_ARATH)

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) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

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
Gene Ontology (GO)
Biological process	cell wall modification Inferred from electronic annotation. Source: InterPro pollen tube growth Ref.1 Traceable author statement. 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
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	24	Potential
	Chain	25 – 595	571	Pectinesterase 5		PRO_0000023477
Sites
	Active site	413	1	Proton donor By similarity
	Active site	434	1	Nucleophile By similarity
	Binding site	360	1	Substrate By similarity
	Binding site	390	1	Substrate By similarity
	Binding site	503	1	Substrate By similarity
	Binding site	505	1	Substrate By similarity
	Site	412	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	206	1	N-linked (GlcNAc...) Potential
	Glycosylation	349	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	50	1	D → V in AAV91508. Ref.1
	Sequence conflict	93	1	G → E in CAB58974. Ref.2
	Sequence conflict	138	1	K → E in AAV91508. Ref.1
	Sequence conflict	267	1	T → A Ref.1
	Sequence conflict	267	1	T → A Ref.2
	Sequence conflict	537	1	K → Q in AAV91508. Ref.1
	Sequence conflict	545	1	N → S in AAV91508. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q5MFV8-1 [UniParc]. Last modified March 15, 2005. Version 2. Checksum: E314E53201F3CD77	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

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: 15659637] [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. , 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.
[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. , 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]	"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: 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. AY091768 mRNA. Translation: AAM10316.1. BT001120 mRNA. Translation: AAN64511.1.
IPI	IPI00525113.
PIR	T02183. T52327.
RefSeq	NP_182227.1.
UniGene	At.24875 Rra.2609 Rsa.22117 Rsa.4681
3D structure databases
SMR	Q5MFV8. Positions 39-188, 278-595.
ModBase	Search...
Proteomic databases
PRIDE	Q5MFV8.
Genome annotation databases
GeneID	819318.
GenomeReviews	Gene locus AT2G47040 in contig CT485783_GR.
KEGG	ath:AT2G47040.
NMPDR	fig|3702.1.peg.11895.
Organism-specific databases
GeneFarm	443. 8.
TAIR	At2g47040.
Phylogenomic databases
eggNOG	COG4677.
HOGENOM	HBG747179.
InParanoid	Q5MFV8.
Enzyme and pathway databases
BRENDA	3.1.1.11. 302.
Gene expression databases
Genevestigator	Q5MFV8.
GermOnline	AT2G47040. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. IPR018040. Pectinesterase_AS. IPR000070. Pectinesterase_cat. IPR006501. Pectinesterase_inhib. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit. G3DSA:1.20.140.40. Pectinesterase_inhib. 1 hit.
Pfam	PF01095. Pectinesterase. 1 hit. PF04043. PMEI. 1 hit. [Graphical view]
SMART	SM00856. PMEI. 1 hit. [Graphical view]
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:	February 9, 2010
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)