Reviewed, UniProtKB/Swiss-Prot Q9LXK7 (PME32_ARATH)

Names and origin

Protein names

Recommended name:
    Probable pectinesterase/pectinesterase inhibitor 32
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 32
        Alternative name(s):
            Pectin methylesterase inhibitor 32
    2- Recommended name:
            Pectinesterase 32
                Short name=PE 32
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 32
              Short name=AtPME32

Gene names

Name:	PME32
Synonyms:	ARATH32
Ordered Locus Names:	At3g43270
ORF Names:	F7K15.120

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	527 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 siliques. Ref.4
Developmental stage	Expressed during late developmental phases of siliques. Ref.4
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
Coding sequence diversity	Alternative splicing
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9LXK7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9LXK7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     296-305: AVSGRGFIAR → GKSKFIISFT
     306-527: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 527	503	Probable pectinesterase/pectinesterase inhibitor 32		PRO_0000371684
Regions
	Region	25 – 165	141	Pectinesterase inhibitor 32
	Region	214 – 511	298	Pectinesterase 32
	Compositional bias	259 – 262	4	Poly-Lys
Sites
	Active site	342	1	Proton donor; for pectinesterase activity By similarity
	Active site	363	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	289	1	Substrate; for pectinesterase activity By similarity
	Binding site	319	1	Substrate; for pectinesterase activity By similarity
	Binding site	431	1	Substrate; for pectinesterase activity By similarity
	Binding site	433	1	Substrate; for pectinesterase activity By similarity
	Site	341	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	110	1	N-linked (GlcNAc...) Potential
	Glycosylation	209	1	N-linked (GlcNAc...) Potential
	Glycosylation	224	1	N-linked (GlcNAc...) Potential
	Glycosylation	280	1	N-linked (GlcNAc...) Potential
	Glycosylation	423	1	N-linked (GlcNAc...) Potential
	Glycosylation	494	1	N-linked (GlcNAc...) Potential
	Glycosylation	501	1	N-linked (GlcNAc...) Potential
	Disulfide bond	356 ↔ 376		By similarity
Natural variations
	Alternative sequence	296 – 305	10	AVSGRGFIAR → GKSKFIISFT in isoform 2.		VSP_037089
	Alternative sequence	306 – 527	222	Missing in isoform 2.		VSP_037090

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: CBC47903AB23A29C	FASTA	527	57,636
	10 20 30 40 50 60 MAKFRQMGSS IFFLFLIIIS LCSAHKEAFS STDLVQMECL RVPPLEFAEA AKTVVDAITK 70 80 90 100 110 120 AVAIVSKFDK KAGKSRVSNA IVDCVDLLDS AAEELSWIIS ASQSPNGKDN STGDVGSDLR 130 140 150 160 170 180 TWISAALSNQ DTCLDGFEGT NGIIKKIVAG GLSKVGTTVR NLLTMVHSPP SKPKPKPIKA 190 200 210 220 230 240 QTMTKAHSGF SKFPSWVKPG DRKLLQTDNI TVADAVVAAD GTGNFTTISD AVLAAPDYST 250 260 270 280 290 300 KRYVIHVKRG VYVENVEIKK KKWNIMMVGD GIDATVITGN RSFIDGWTTF RSATFAVSGR 310 320 330 340 350 360 GFIARDITFQ NTAGPEKHQA VAIRSDTDLG VFYRCAMRGY QDTLYAHSMR QFFRECIITG 370 380 390 400 410 420 TVDFIFGDAT AVFQSCQIKA KQGLPNQKNS ITAQGRKDPN EPTGFTIQFS NIAADTDLLL 430 440 450 460 470 480 NLNTTATYLG RPWKLYSRTV FMQNYMSDAI NPVGWLEWNG NFALDTLYYG EYMNSGPGAS 490 500 510 520 LDRRVKWPGY HVLNTSAEAN NFTVSQLIQG NLWLPSTGIT FIAGLVS
	Isoform 2. Checksum: 3051D91851FB7AD5	FASTA	305	32,937
	10 20 30 40 50 60 MAKFRQMGSS IFFLFLIIIS LCSAHKEAFS STDLVQMECL RVPPLEFAEA AKTVVDAITK 70 80 90 100 110 120 AVAIVSKFDK KAGKSRVSNA IVDCVDLLDS AAEELSWIIS ASQSPNGKDN STGDVGSDLR 130 140 150 160 170 180 TWISAALSNQ DTCLDGFEGT NGIIKKIVAG GLSKVGTTVR NLLTMVHSPP SKPKPKPIKA 190 200 210 220 230 240 QTMTKAHSGF SKFPSWVKPG DRKLLQTDNI TVADAVVAAD GTGNFTTISD AVLAAPDYST 250 260 270 280 290 300 KRYVIHVKRG VYVENVEIKK KKWNIMMVGD GIDATVITGN RSFIDGWTTF RSATFGKSKF IISFT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [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] (ISOFORMS 1 AND 2). Strain: cv. Columbia.
[3]	"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.
[4]	"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	AL353871 Genomic DNA. Translation: CAB89048.1. AY070071 mRNA. Translation: AAL49828.1. AY096694 mRNA. Translation: AAM20328.1. AY065349 mRNA. Translation: AAL38790.1. AY096720 mRNA. Translation: AAM20354.1.
IPI	IPI00547727. IPI00929955.
PIR	T49241.
RefSeq	NP_189913.3.
UniGene	At.28622
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9LXK7.
Proteomic databases
PRIDE	Q9LXK7.
Genome annotation databases
GeneID	823402.
GenomeReviews	Gene locus AT3G43270 in contig BA000014_GR.
KEGG	ath:AT3G43270.
NMPDR	fig|3702.1.peg.15534.
Organism-specific databases
GeneFarm	312. 8.
TAIR	At3g43270.
Phylogenomic databases
OMA	DELSWSM.
Gene expression databases
Genevestigator	Q9LXK7.
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.
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

PME32_ARATH

Accession

Primary (citable) accession number: Q9LXK7
Secondary accession number(s): Q8VZ27

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)