Reviewed, UniProtKB/Swiss-Prot O49298 (PME6_ARATH)

Names and origin

Protein names

Recommended name:
    Probable pectinesterase/pectinesterase inhibitor 6
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 6
        Alternative name(s):
            Pectin methylesterase inhibitor 6
    2- Recommended name:
            Pectinesterase 6
                Short name=PE 6
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 6
              Short name=AtPME6

Gene names

Name:	PME6
Synonyms:	ARATH6
Ordered Locus Names:	At1g23200
ORF Names:	T26J12.4

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	554 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 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 rosette leaves, flower and siliques. Ref.4 Ref.6
Developmental stage	Low expression in vegetative and flower stages. No expression in young siliques but highly expressed in older 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.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Secreted
Domain	Signal
Molecular function	Aspartyl esterase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall modification Inferred from electronic annotation. Source: InterPro
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
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 – 32	32	Potential
	Chain	33 – 554	522	Probable pectinesterase/pectinesterase inhibitor 6		PRO_0000371663
Regions
	Region	29 – 183	155	Pectinesterase inhibitor 6
	Region	250 – 540	291	Pectinesterase 6
Sites
	Active site	380	1	Proton donor; for pectinesterase activity By similarity
	Active site	401	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	327	1	Substrate; for pectinesterase activity By similarity
	Binding site	357	1	Substrate; for pectinesterase activity By similarity
	Binding site	460	1	Substrate; for pectinesterase activity By similarity
	Binding site	462	1	Substrate; for pectinesterase activity By similarity
	Site	379	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Glycosylation	172	1	N-linked (GlcNAc...) Potential
	Disulfide bond	394 ↔ 414		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O49298-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: C2EAC4FDC2CAF387	FASTA	554	61,270
	10 20 30 40 50 60 MDHKILLTPP KSLYTKCIIT IIYVVSISHL NAHFITSCKQ TPYPSVCDHH MSNSPLKTLD 70 80 90 100 110 120 DQTDGFTFHD LVVSSTMDQA VQLHRLVSSL KQHHSLHKHA TSALFDCLEL YEDTIDQLNH 130 140 150 160 170 180 SRRSYGQYSS PHDRQTSLSA AIANQDTCRN GFRDFKLTSS YSKYFPVQFH RNLTKSISNS 190 200 210 220 230 240 LAVTKAAAEA EAVAEKYPST GFTKFSKQRS SAGGGSHRRL LLFSDEKFPS WFPLSDRKLL 250 260 270 280 290 300 EDSKTTAKAD LVVAKDGSGH YTSIQQAVNA AAKLPRRNQR LVIYVKAGVY RENVVIKKSI 310 320 330 340 350 360 KNVMVIGDGI DSTIVTGNRN VQDGTTTFRS ATFAVSGNGF IAQGITFENT AGPEKHQAVA 370 380 390 400 410 420 LRSSSDFSVF YACSFKGYQD TLYLHSSRQF LRNCNIYGTV DFIFGDATAI LQNCNIYARK 430 440 450 460 470 480 PMSGQKNTIT AQSRKEPDET TGFVIQSSTV ATASETYLGR PWRSHSRTVF MKCNLGALVS 490 500 510 520 530 540 PAGWLPWSGS FALSTLYYGE YGNTGAGASV SGRVKWPGYH VIKTVTEAEK FTVENFLDGN 550 YWITATGVPV NDGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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.
[3]	"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. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Characterization of the pectin methylesterase-like gene AtPME3: a new member of a gene family comprising at least 12 genes in Arabidopsis thaliana." Micheli F., Holliger C., Goldberg R., Richard L. Gene 220:13-20(1998) [PubMed: 9767082] [Abstract] Cited for: TISSUE SPECIFICITY.
[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	AC002311 Genomic DNA. Translation: AAC00600.1. AC005292 Genomic DNA. Translation: AAF86993.1. AY065263 mRNA. Translation: AAL38739.1. AY091325 mRNA. Translation: AAM14264.1. AK227025 mRNA. Translation: BAE99088.1.
IPI	IPI00524785.
PIR	C86366.
RefSeq	NP_173733.1.
UniGene	At.23382 At.67139
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
SMR	O49298. Positions 35-186.
ModBase	Search...
Proteomic databases
PRIDE	O49298.
Genome annotation databases
GeneID	838928.
GenomeReviews	Gene locus AT1G23200 in contig CT485782_GR.
KEGG	ath:AT1G23200.
NMPDR	fig|3702.1.peg.2697.
Organism-specific databases
GeneFarm	228. 8.
TAIR	At1g23200.
Phylogenomic databases
eggNOG	COG4677.
HOGENOM	HBG747179.
InParanoid	O49298.
Gene expression databases
ArrayExpress	O49298.
Genevestigator	O49298.
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. False negative. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME6_ARATH

Accession

Primary (citable) accession number: O49298

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	June 1, 1998
Last modified:	February 9, 2010
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)