Reviewed, UniProtKB/Swiss-Prot Q42534 (PME2_ARATH)

Names and origin

Protein names

Recommended name:
    Pectinesterase 2
      Short name=PE 2
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase 2
      Short name=AtPME2

Gene names

Name:	PME2
Synonyms:	ARATH8
Ordered Locus Names:	At1g53830
ORF Names:	T18A20.6

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	587 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 Probable.
Tissue specificity	Expressed in flower buds. Ref.5
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	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW plant-type cell wall 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 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 – 40	40	Potential
	Chain	41 – 587	547	Pectinesterase 2		PRO_0000023475
Sites
	Active site	404	1	Proton donor By similarity
	Active site	425	1	Nucleophile By similarity
	Binding site	351	1	Substrate By similarity
	Binding site	381	1	Substrate By similarity
	Binding site	493	1	Substrate By similarity
	Binding site	495	1	Substrate By similarity
	Site	403	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	99	1	N-linked (GlcNAc...) Potential
	Glycosylation	218	1	N-linked (GlcNAc...) Potential
	Disulfide bond	418 ↔ 438		By similarity
Experimental info
	Sequence conflict	55	1	S → F in AAC50023. Ref.3
	Sequence conflict	233 – 241	9	SSTFTNNNN → FFNLHQQQQ in AAC50023. Ref.3
	Sequence conflict	288 – 291	4	TTVA → DNGS in AAC50023. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q42534-1 [UniParc]. Last modified December 13, 2001. Version 2. Checksum: FA8AB0F92D19A1E4	FASTA	587	64,173
	10 20 30 40 50 60 MAPIKEFISK FSDFKNNKKL ILSSAAIALL LLASIVGIAA TTTNQNKNQK ITTLSSTSHA 70 80 90 100 110 120 ILKSVCSSTL YPELCFSAVA ATGGKELTSQ KEVIEASLNL TTKAVKHNYF AVKKLIAKRK 130 140 150 160 170 180 GLTPREVTAL HDCLETIDET LDELHVAVED LHQYPKQKSL RKHADDLKTL ISSAITNQGT 190 200 210 220 230 240 CLDGFSYDDA DRKVRKALLK GQVHVEHMCS NALAMIKNMT ETDIANFELR DKSSTFTNNN 250 260 270 280 290 300 NRKLKEVTGD LDSDGWPKWL SVGDRRLLQG STIKADATVA DDGSGDFTTV AAAVAAAPEK 310 320 330 340 350 360 SNKRFVIHIK AGVYRENVEV TKKKTNIMFL GDGRGKTIIT GSRNVVDGST TFHSATVAAV 370 380 390 400 410 420 GERFLARDIT FQNTAGPSKH QAVALRVGSD FSAFYQCDMF AYQDTLYVHS NRQFFVKCHI 430 440 450 460 470 480 TGTVDFIFGN AAAVLQDCDI NARRPNSGQK NMVTAQGRSD PNQNTGIVIQ NCRIGGTSDL 490 500 510 520 530 540 LAVKGTFPTY LGRPWKEYSR TVIMQSDISD VIRPEGWHEW SGSFALDTLT YREYLNRGGG 550 560 570 580 AGTANRVKWK GYKVITSDTE AQPFTAGQFI GGGGWLASTG FPFSLSL

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]	"Clustered genes within the genome of Arabidopsis thaliana encoding pectin methylesterase-like enzymes." Richard L., Qin L.X., Goldberg R. Gene 170:207-211(1996) [PubMed: 8666246] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-587.
[4]	"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.
[5]	"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
EMBLGenBankDDBJ	AC009324 Genomic DNA. Translation: AAF02856.1. AF361637 mRNA. Translation: AAK32805.1. AY133609 mRNA. Translation: AAM91439.1. U25649 Genomic DNA. Translation: AAC50023.1.
IPI	IPI00520451.
PIR	D96578. PC4168.
RefSeq	NP_175786.1.
UniGene	At.10820 At.66848
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBase	Search...
Protein-protein interaction databases
STRING	Q42534.
Proteomic databases
PRIDE	Q42534.
Genome annotation databases
GeneID	841820.
GenomeReviews	Gene locus AT1G53830 in contig CT485782_GR.
KEGG	ath:AT1G53830.
NMPDR	fig|3702.1.peg.4887.
Organism-specific databases
GeneFarm	123. 8.
TAIR	At1g53830.
Phylogenomic databases
OMA	CDINARR.
Enzyme and pathway databases
BRENDA	3.1.1.11. 302.
Gene expression databases
ArrayExpress	Q42534.
Genevestigator	Q42534.
GermOnline	AT1G53830. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR012334. Pectin_lyas_fold. 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]
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

PME2_ARATH

Accession

Primary (citable) accession number: Q42534
Secondary accession number(s): Q9SSB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	December 13, 2001
Last modified:	November 3, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)