Reviewed, UniProtKB/Swiss-Prot Q1PEC0 (PME42_ARATH)

Names and origin

Protein names

Recommended name:
    Probable pectinesterase/pectinesterase inhibitor 42
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 42
        Alternative name(s):
            Pectin methylesterase inhibitor 42
    2- Recommended name:
            Pectinesterase 42
                Short name=PE 42
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 42
              Short name=AtPME42

Gene names

Name:	PME42
Synonyms:	ARATH42
Ordered Locus Names:	At4g03930
ORF Names:	T24M8.6

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	524 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 but not in flower buds. Ref.4
Developmental stage	Expression restricted to early to mid-stage of silique development. 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.
Sequence caution	The sequence AAC28220.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence ABK28620.1 differs from that shown. Reason: Erroneous termination at position 525. Translated as stop. The sequence CAB80816.1 differs from that shown. Reason: Erroneous gene model prediction.

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 – 22	22	Potential
	Chain	23 – 524	502	Probable pectinesterase/pectinesterase inhibitor 42		PRO_0000370185
Regions
	Region	23 – 172	150	Pectinesterase inhibitor 42
	Region	215 – 510	296	Pectinesterase 42
Sites
	Active site	343	1	Proton donor; for pectinesterase activity By similarity
	Active site	364	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	290	1	Substrate; for pectinesterase activity By similarity
	Binding site	430	1	Substrate; for pectinesterase activity By similarity
	Binding site	432	1	Substrate; for pectinesterase activity By similarity
	Site	342	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	265	1	N-linked (GlcNAc...) Potential
	Glycosylation	281	1	N-linked (GlcNAc...) Potential
	Glycosylation	412	1	N-linked (GlcNAc...) Potential
	Disulfide bond	357 ↔ 377		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1PEC0-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: D6161EDBDD4694FB	FASTA	524	58,591
	10 20 30 40 50 60 MLVKVFSFFI LMITMVVIGV SKEYCDDKHS CQNFLLELKT ASSSLSEIRR RDLLIIVLKN 70 80 90 100 110 120 SVRKIDMAMI GVMEDTKQHE EMENDKLCLK EDTNLFEEMM ESAKDRMIRS VEELLGGEFP 130 140 150 160 170 180 YLGSYENIHT WLSGVLTSYI TCIDEIGDGA YKRRVEPQLQ DLISKAKVAL ALFISISPRD 190 200 210 220 230 240 NTELNSVVPN SPSWLSHVDK KDLYLNAEAL KKIADVVVAK DGTGKYNTVN AAIAAAPQHS 250 260 270 280 290 300 HKRFIIYIKT GIYDEIVAIE NTKPNLTLIG DGQDSTIITG NLSASNVRRT FYTATFASNG 310 320 330 340 350 360 KGFIGVDMCF RNTVGPAKGP AVALRVSGDM SVIYRCRVEG YQDALYPHID RQFYRECFIT 370 380 390 400 410 420 GTVDFICGNA AAVFQFCQIV ARQPNMGQSN FITAQSRETK DDKSGFSIQN CNITASSDLD 430 440 450 460 470 480 TATVKTYLGR PWRIFSTVAV LQSFIGDLVD PAGWTPWEGE TGLSTLHYRE YQNRGPGAVT 490 500 510 520 SRRVKWSGFK VMKDPKQATE FTVAKLLDGE TWLKESRIPY KSGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations." Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P. Plant Biotechnol. J. 4:317-324(2006) [PubMed: 17147637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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	AF077409 Genomic DNA. Translation: AAC28220.1. Sequence problems. AL161498 Genomic DNA. Translation: CAB80816.1. Sequence problems. DQ446798 mRNA. Translation: ABE66043.1. DQ653177 mRNA. Translation: ABK28620.1. Sequence problems.
IPI	IPI00524425.
PIR	T01870.
RefSeq	NP_192302.3.
UniGene	At.3982
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	825703.
GenomeReviews	Gene locus AT4G03930 in contig CT486007_GR.
KEGG	ath:AT4G03930.
Organism-specific databases
GeneFarm	440. 8.
TAIR	At4g03930.
Gene expression databases
Genevestigator	Q1PEC0.
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]
PROSITE	PS00800. PECTINESTERASE_1. 1 hit. PS00503. PECTINESTERASE_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME42_ARATH

Accession

Primary (citable) accession number: Q1PEC0
Secondary accession number(s): A0MF51, O81516

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	May 16, 2006
Last modified:	October 13, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)