O23447 (PME43_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative pectinesterase/pectinesterase inhibitor 43

Including the following 2 domains:

1. Pectinesterase inhibitor 43
   Alternative name(s):
   Pectin methylesterase inhibitor 43
2. Pectinesterase 43
   Short name=PE 43
   EC=3.1.1.11
   Alternative name(s):
   Pectin methylesterase 43
   Short name=AtPME43

Gene names

Name:	PME43
Synonyms:	ARATH43
Ordered Locus Names:	At4g15980
ORF Names:	dl4030c, FCAALL.248

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	701 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 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 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
Cellular component	apoplast Inferred from direct assay. Source: TAIR cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 701	679	Putative pectinesterase/pectinesterase inhibitor 43		PRO_0000371692
Regions
	Region	42 – 195	154	Pectinesterase inhibitor 43
	Region	391 – 688	298	Pectinesterase 43
	Compositional bias	225 – 336	112	Ser-rich
	Compositional bias	651 – 677	27	Arg-rich
Sites
	Active site	520	1	Proton donor; for pectinesterase activity By similarity
	Active site	541	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	467	1	Substrate; for pectinesterase activity By similarity
	Binding site	497	1	Substrate; for pectinesterase activity By similarity
	Binding site	609	1	Substrate; for pectinesterase activity By similarity
	Binding site	611	1	Substrate; for pectinesterase activity By similarity
	Site	519	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	267	1	N-linked (GlcNAc...) Potential
	Glycosylation	637	1	N-linked (GlcNAc...) Potential
	Disulfide bond	534 ↔ 554		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O23447 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: A7E7697AEAC28ECA	FASTA	701	78,573
	10 20 30 40 50 60 MNKYVLLGVT ALIMAMVICV EANDGNSPSR KMEEVHRESK LMITKTTVSI ICASTDYKQD 70 80 90 100 110 120 CTTSLATVRS PDPRNLIRSA FDLAIISIRS GIDRGMIDLK SRADADMHTR EALNTCRELM 130 140 150 160 170 180 DDAIDDLRKT RDKFRGFLFT RLSDFVEDLC VWLSGSITYQ QTCIDGFEGI DSEAAVMMER 190 200 210 220 230 240 VMRKGQHLTS NGLAIAANLD KLLKAFRIPF PFLRSRRGRL GILGSGSSRD ESVGSSQDSP 250 260 270 280 290 300 PNEDSSDDSP STVDSSENQP VDSSSENQSS DSSNNRPLDS SKNQQMESSE DTPKKSAFSG 310 320 330 340 350 360 NQPLDDSSDK LPQKSTSSEN QPLDSSENPP QKSTSSENRP LDPLRKLNPL NKLDSLKDRH 370 380 390 400 410 420 LSEEGEFPPW VTPHSRRLLA RRPRNNGIKA NVVVAKDGSG KCKTIAQALA MVPMKNTKKF 430 440 450 460 470 480 VIHIKEGVYK EKVEVTKKML HVMFVGDGPT KTVITGDIAF LPDQVGTYRT ASVAVNGDYF 490 500 510 520 530 540 MAKDIGFENT AGAARHQAVA LRVSADFAVF FNCHMNGYQD TLYVHTHRQF YRNCRVSGTI 550 560 570 580 590 600 DFVFGDAKAV FQNCEFVIRR PMEHQQCIVT AQGRKDRRET TGIVIHNSRI TGDASYLPVK 610 620 630 640 650 660 AKNRAFLGRP WKEFSRTIIM NTEIDDVIDP EGWLKWNETF ALNTLFYTEY RNRGRGSGQG 670 680 690 700 RRVRWRGIKR ISDRAAREFA PGNFLRGNTW IPQTRIPYNA N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana." Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N. Nature 391:485-488(1998) [PubMed: 9461215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[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
EMBL GenBank DDBJ	Z97340 Genomic DNA. Translation: CAB10377.1. AL161542 Genomic DNA. Translation: CAB78640.1. CP002687 Genomic DNA. Translation: AEE83677.1.
IPI	IPI00524133.
PIR	G71425.
RefSeq	NP_193333.1. NM_117691.1.
UniGene	At.54346.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortal	O23447.
SMR	O23447. Positions 47-199, 387-658.
ModBase	Search...
Proteomic databases
PRIDE	O23447.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G15980.1; AT4G15980.1; AT4G15980.
GeneID	827282.
GenomeReviews	Gene locus AT4G15980 in contig CT486007_GR.
KEGG	ath:AT4G15980.
NMPDR	fig|3702.1.peg.19352.
Organism-specific databases
GeneFarm	155. 8.
TAIR	At4g15980.
Phylogenomic databases
eggNOG	euNOG22784.
GeneTree	EPGT00070000028024.
HOGENOM	HBG747179.
InParanoid	O23447.
OMA	SENQPLD.
PhylomeDB	O23447.
ProtClustDB	CLSN2915948.
Enzyme and pathway databases
BRENDA	3.1.1.11. 399.
Gene expression databases
ArrayExpress	O23447.
Genevestigator	O23447.
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

PME43_ARATH

Accession

Primary (citable) accession number: O23447

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	January 1, 1998
Last modified:	December 14, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program