O49006 (PME3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectinesterase/pectinesterase inhibitor 3

Including the following 2 domains:

1. Pectinesterase inhibitor 3
   Alternative name(s):
   Pectin methylesterase inhibitor 3
2. Pectinesterase 3
   Short name=PE 3
   EC=3.1.1.11
   Alternative name(s):
   Pectin methylesterase 27
   Short name=AtPME27
   Pectin methylesterase 3

Gene names

Name:	PME3
Synonyms:	ARATH27
Ordered Locus Names:	At3g14310
ORF Names:	MLN21.10

Organism

Arabidopsis thaliana (Mouse-ear cress)

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	592 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 leaves, stems, flowers and siliques. Ref.1 Ref.7
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.
Sequence caution	The sequence AAL24278.1 differs from that shown. Reason: Frameshift at position 172. The sequence BAD94011.1 differs from that shown. Reason: Intron retention.

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 Reference proteome
Gene Ontology (GO)
Biological process	cell wall modification Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW response to nematode Inferred from mutant phenotype. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR cell wall Inferred from direct assay. Source: TAIR cytoplasm Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. 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 mutant phenotype. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 35	35	Potential
	Chain	36 – 592	557	Pectinesterase/pectinesterase inhibitor 3		PRO_0000371662
Regions
	Region	53 – 212	160	Pectinesterase inhibitor 3
	Region	281 – 578	298	Pectinesterase 3
Sites
	Active site	409	1	Proton donor; for pectinesterase activity By similarity
	Active site	430	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	356	1	Substrate; for pectinesterase activity By similarity
	Binding site	386	1	Substrate; for pectinesterase activity By similarity
	Binding site	498	1	Substrate; for pectinesterase activity By similarity
	Binding site	500	1	Substrate; for pectinesterase activity By similarity
	Site	408	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	215	1	N-linked (GlcNAc...) Potential
	Disulfide bond	423 ↔ 443		By similarity
Experimental info
	Sequence conflict	81 – 82	2	GV → AC in AAC72288. Ref.1
	Sequence conflict	280	1	A → R in AAC72288. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O49006 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 32AFAF1E6C471B2F	FASTA	592	64,256
	10 20 30 40 50 60 MAPSMKEIFS KDNFKKNKKL VLLSAAVALL FVAAVAGISA GASKANEKRT LSPSSHAVLR 70 80 90 100 110 120 SSCSSTRYPE LCISAVVTAG GVELTSQKDV IEASVNLTIT AVEHNYFTVK KLIKKRKGLT 130 140 150 160 170 180 PREKTALHDC LETIDETLDE LHETVEDLHL YPTKKTLREH AGDLKTLISS AITNQETCLD 190 200 210 220 230 240 GFSHDDADKQ VRKALLKGQI HVEHMCSNAL AMIKNMTDTD IANFEQKAKI TSNNRKLKEE 250 260 270 280 290 300 NQETTVAVDI AGAGELDSEG WPTWLSAGDR RLLQGSGVKA DATVAADGSG TFKTVAAAVA 310 320 330 340 350 360 AAPENSNKRY VIHIKAGVYR ENVEVAKKKK NIMFMGDGRT RTIITGSRNV VDGSTTFHSA 370 380 390 400 410 420 TVAAVGERFL ARDITFQNTA GPSKHQAVAL RVGSDFSAFY NCDMLAYQDT LYVHSNRQFF 430 440 450 460 470 480 VKCLIAGTVD FIFGNAAVVL QDCDIHARRP NSGQKNMVTA QGRTDPNQNT GIVIQKCRIG 490 500 510 520 530 540 ATSDLQSVKG SFPTYLGRPW KEYSQTVIMQ SAISDVIRPE GWSEWTGTFA LNTLTYREYS 550 560 570 580 590 NTGAGAGTAN RVKWRGFKVI TAAAEAQKYT AGQFIGGGGW LSSTGFPFSL GL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S. DNA Res. 7:131-135(2000) [PubMed: 10819329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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]	"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 (MAR-2005) to the EMBL/GenBank/DDBJ databases 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: 15337457] [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: 16622707] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF033204 Genomic DNA. Translation: AAC72288.1. AB022220 Genomic DNA. Translation: BAB01037.1. CP002686 Genomic DNA. Translation: AEE75500.1. AY037184 mRNA. Translation: AAK59769.1. AY052252 mRNA. Translation: AAK97722.1. AY143950 mRNA. Translation: AAN28889.1. AY058892 mRNA. Translation: AAL24278.1. Frameshift. AK221816 mRNA. Translation: BAD94011.1. Sequence problems.
IPI	IPI00546571.
RefSeq	NP_188048.1. NM_112289.2.
UniGene	At.43283. At.6066. At.67322. At.74977.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortal	O49006.
SMR	O49006. Positions 274-592.
ModBase	Search...
Protein-protein interaction databases
STRING	O49006.
Proteomic databases
PRIDE	O49006.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G14310.1; AT3G14310.1; AT3G14310.
GeneID	820651.
GenomeReviews	Gene locus AT3G14310 in contig BA000014_GR.
KEGG	ath:AT3G14310.
Organism-specific databases
GeneFarm	149. 8.
TAIR	At3g14310.
Phylogenomic databases
OMA	LLKGQIH.
PhylomeDB	O49006.
ProtClustDB	PLN02313.
Gene expression databases
Genevestigator	O49006.
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]
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

PME3_ARATH

Accession

Primary (citable) accession number: O49006
Secondary accession number(s): Q56X61, Q93YZ2, Q9LUL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 5, 2009
Last modified:	December 14, 2011
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program