Reviewed, UniProtKB/Swiss-Prot Q9SMY6 (PME45_ARATH)

Names and origin

Protein names

Recommended name:
    Putative pectinesterase/pectinesterase inhibitor 45
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 45
        Alternative name(s):
            Pectin methylesterase inhibitor 45
    2- Recommended name:
            Pectinesterase 45
                Short name=PE 45
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 45
              Short name=AtPME45

Gene names

Name:	PME45
Synonyms:	ARATH45
Ordered Locus Names:	At4g33230
ORF Names:	F4I10.160

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	609 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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	Membrane; Single-pass membrane protein Potential.
Tissue specificity	Expressed in flower buds and pollen. Ref.2 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
Cellular component	Membrane
Domain	Transmembrane
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: InterPro integral to membrane 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
	Chain	1 – 609	609	Putative pectinesterase/pectinesterase inhibitor 45		PRO_0000371694
Regions
	Transmembrane	25 – 45	21	Potential
	Region	89 – 241	153	Pectinesterase inhibitor 45
	Region	296 – 593	298	Pectinesterase 45
Sites
	Active site	424	1	Proton donor; for pectinesterase activity By similarity
	Active site	445	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	371	1	Substrate; for pectinesterase activity By similarity
	Binding site	401	1	Substrate; for pectinesterase activity By similarity
	Binding site	513	1	Substrate; for pectinesterase activity By similarity
	Binding site	515	1	Substrate; for pectinesterase activity By similarity
	Site	423	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	51	1	N-linked (GlcNAc...) Potential
	Glycosylation	62	1	N-linked (GlcNAc...) Potential
	Glycosylation	100	1	N-linked (GlcNAc...) Potential
	Glycosylation	114	1	N-linked (GlcNAc...) Potential
	Glycosylation	183	1	N-linked (GlcNAc...) Potential
	Glycosylation	229	1	N-linked (GlcNAc...) Potential
	Glycosylation	296	1	N-linked (GlcNAc...) Potential
	Glycosylation	306	1	N-linked (GlcNAc...) Potential
	Glycosylation	346	1	N-linked (GlcNAc...) Potential
	Glycosylation	362	1	N-linked (GlcNAc...) Potential
	Glycosylation	491	1	N-linked (GlcNAc...) Potential
	Disulfide bond	438 ↔ 458		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9SMY6-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: B2F7468D91DEE899	FASTA	609	67,742
	10 20 30 40 50 60 MAFQDFDKIQ ERVNAERKRK FRKRIILGVV SVLVVAAAII GGAFAYVTYE NKTQEQGKTT 70 80 90 100 110 120 NNKSKDSPTK SESPSPKPPS SAAQTVKAGQ VDKIIQTLCN STLYKPTCQN TLKNETKKDT 130 140 150 160 170 180 PQTDPRSLLK SAIVAVNDDL DQVFKRVLSL KTENKDDKDA IAQCKLLVDE AKEELGTSMK 190 200 210 220 230 240 RINDSEVNNF AKIVPDLDSW LSAVMSYQET CVDGFEEGKL KTEIRKNFNS SQVLTSNSLA 250 260 270 280 290 300 MIKSLDGYLS SVPKVKTRLL LEARSSAKET DHITSWLSNK ERRMLKAVDV KALKPNATVA 310 320 330 340 350 360 KDGSGNFTTI NAALKAMPAK YQGRYTIYIK HGIYDESVII DKKKPNVTMV GDGSQKTIVT 370 380 390 400 410 420 GNKSHAKKIR TFLTATFVAQ GEGFMAQSMG FRNTAGPEGH QAVAIRVQSD RSVFLNCRFE 430 440 450 460 470 480 GYQDTLYAYT HRQYYRSCVI IGTVDFIFGD AAAIFQNCDI FIRKGLPGQK NTVTAQGRVD 490 500 510 520 530 540 KFQTTGFVIH NCTVAPNEDL KPVKAQFKSY LGRPWKPHSR TVVMESTIED VIDPVGWLRW 550 560 570 580 590 600 QETDFAIDTL SYAEYKNDGP SGATAARVKW PGFRVLNKEE AMKFTVGPFL QGEWIQAIGS PVKLGLYDA

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]	"Transcriptional profiling of Arabidopsis tissues reveals the unique characteristics of the pollen transcriptome." Becker J.D., Boavida L.C., Carneiro J., Haury M., Feijo J.A. Plant Physiol. 133:713-725(2003) [PubMed: 14500793] [Abstract] Cited for: TISSUE SPECIFICITY.
[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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL035525 Genomic DNA. Translation: CAB36797.1. AL161583 Genomic DNA. Translation: CAB80040.1.
IPI	IPI00525898.
PIR	T05203.
RefSeq	NP_195049.1.
UniGene	At.54586
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBase	Search...
Proteomic databases
PRIDE	Q9SMY6.
Genome annotation databases
GeneID	829459.
GenomeReviews	Gene locus AT4G33230 in contig CT486007_GR.
KEGG	ath:AT4G33230.
NMPDR	fig|3702.1.peg.21365.
Organism-specific databases
GeneFarm	410. 8.
TAIR	At4g33230.
Phylogenomic databases
OMA	RINDSEV.
Gene expression databases
ArrayExpress	Q9SMY6.
Genevestigator	Q9SMY6.
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. False negative. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME45_ARATH

Accession

Primary (citable) accession number: Q9SMY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)