Q8RXK7 (PME41_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable pectinesterase/pectinesterase inhibitor 41

Including the following 2 domains:

1. Pectinesterase inhibitor 41
   Alternative name(s):
   Pectin methylesterase inhibitor 41
2. Pectinesterase 41
   Short name=PE 41
   EC=3.1.1.11
   Alternative name(s):
   AtPMEpcrB
   Pectin methylesterase 41
   Short name=AtPME41

Gene names

Name:	PME41
Synonyms:	ARATH41
Ordered Locus Names:	At4g02330
ORF Names:	T14P8.14

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	573 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 flowers, siliques, floral stems and rosettes leaves. Ref.4 Ref.6
Developmental stage	Expressed throughout silique development. 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 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 brassinosteroid stimulus Inferred from expression pattern. Source: TAIR response to cold Inferred from expression pattern. Source: TAIR
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 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 – 22	22	Potential
	Chain	23 – 573	551	Probable pectinesterase/pectinesterase inhibitor 41		PRO_0000371691
Regions
	Region	25 – 184	160	Pectinesterase inhibitor 41
	Region	259 – 557	299	Pectinesterase 41
	Compositional bias	192 – 195	4	Poly-Lys
Sites
	Active site	389	1	Proton donor; for pectinesterase activity By similarity
	Active site	410	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	336	1	Substrate; for pectinesterase activity By similarity
	Binding site	366	1	Substrate; for pectinesterase activity By similarity
	Binding site	478	1	Substrate; for pectinesterase activity By similarity
	Binding site	480	1	Substrate; for pectinesterase activity By similarity
	Site	388	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	29	1	N-linked (GlcNAc...) Potential
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Glycosylation	173	1	N-linked (GlcNAc...) Potential
	Glycosylation	264	1	N-linked (GlcNAc...) Potential
	Glycosylation	268	1	N-linked (GlcNAc...) Potential
	Glycosylation	281	1	N-linked (GlcNAc...) Potential
	Glycosylation	320	1	N-linked (GlcNAc...) Potential
	Glycosylation	353	1	N-linked (GlcNAc...) Potential
	Glycosylation	456	1	N-linked (GlcNAc...) Potential
	Glycosylation	469	1	N-linked (GlcNAc...) Potential
	Glycosylation	520	1	N-linked (GlcNAc...) Potential
	Glycosylation	541	1	N-linked (GlcNAc...) Potential
	Glycosylation	547	1	N-linked (GlcNAc...) Potential
	Disulfide bond	403 ↔ 423		By similarity
Experimental info
	Sequence conflict	446	1	P → Q in AAL87311. Ref.3
	Sequence conflict	455	1	H → Y in AAC02974. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8RXK7 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 863625D6142BB587	FASTA	573	63,944
	10 20 30 40 50 60 MLSLKLFLVT LFLSLQTLFI ASQTLLPSNS SSTICKTTPD PKFCKSVFPQ TSQGDVREYG 70 80 90 100 110 120 RFSLRKSLTQ SRKFTRTIDR YLKRNNALLS QSAVGALQDC RYLASLTTDY LITSFETVNI 130 140 150 160 170 180 TTSSKTLSFS KADEIQTLLS AALTNEQTCL DGINTAASSS WTIRNGVALP LINDTKLFSV 190 200 210 220 230 240 SLALFTKGWV PKKKKQVASY SWAHPKNTHS HTKPFRHFRN GALPLKMTEH TRAVYESLSR 250 260 270 280 290 300 RKLADDDNDV NTVLVSDIVT VNQNGTGNFT TITEAVNSAP NKTDGTAGYF VIYVTSGVYE 310 320 330 340 350 360 ENVVIAKNKR YLMMIGDGIN RTVVTGNRNV VDGWTTFNSA TFAVTSPNFV AVNMTFRNTA 370 380 390 400 410 420 GPEKHQAVAM RSSADLSIFY SCSFEAYQDT LYTHSLRQFY RECDIYGTVD FIFGNAAVVF 430 440 450 460 470 480 QDCNLYPRQP MQNQFNAITA QGRTDPNQNT GISIHNCTIK PADDLVSSNY TVKTYLGRPW 490 500 510 520 530 540 KEYSRTVFMQ SYIDEVVEPV GWREWNGDFA LSTLYYAEYN NTGSGSSTTD RVVWPGYHVI 550 560 570 NSTDANNFTV ENFLLGDGWM VQSGVPYISG LLS

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]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"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.
[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: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 406-484, 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	AF069298 Genomic DNA. Translation: AAC19280.1. AL161494 Genomic DNA. Translation: CAB80726.1. CP002687 Genomic DNA. Translation: AEE82156.1. AY150433 mRNA. Translation: AAN12975.1. AY080836 mRNA. Translation: AAL87311.1. AF033206 Genomic DNA. Translation: AAC02974.1.
IPI	IPI00537029.
PIR	T01317.
RefSeq	NP_567227.1. NM_116466.3.
UniGene	At.43016.
3D structure databases
HSSP	HSSP built from PDB template 1XG2 based on UniProtKB P14280.
ProteinModelPortal	Q8RXK7.
SMR	Q8RXK7. Positions 255-572.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8RXK7.
Proteomic databases
PRIDE	Q8RXK7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G02330.1; AT4G02330.1; AT4G02330.
GeneID	828064.
GenomeReviews	Gene locus AT4G02330 in contig CT486007_GR.
KEGG	ath:AT4G02330.
Organism-specific databases
GeneFarm	408. 8.
TAIR	At4g02330.
Phylogenomic databases
eggNOG	euNOG17330.
GeneTree	EPGT00070000027901.
HOGENOM	HBG747179.
OMA	FVAVNMT.
PhylomeDB	Q8RXK7.
ProtClustDB	PLN02713.
Gene expression databases
Genevestigator	Q8RXK7.
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. False negative. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME41_ARATH

Accession

Primary (citable) accession number: Q8RXK7
Secondary accession number(s): O49008, O81300

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 5, 2009
Last modified:	December 14, 2011
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program