Reviewed, UniProtKB/Swiss-Prot Q8GXA1 (PME23_ARATH)

Names and origin

Protein names

Recommended name:
    Probable pectinesterase/pectinesterase inhibitor 23
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 23
        Alternative name(s):
            Pectin methylesterase inhibitor 23
    2- Recommended name:
            Pectinesterase 23
                Short name=PE 23
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 23
              Short name=AtPME23

Gene names

Name:	PME23
Synonyms:	ARATH23
Ordered Locus Names:	At3g06830
ORF Names:	F3E22.3

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 › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	568 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 mature pollen grains in the anthers and on the stigma. Found in pollen tubes within the style. 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.
Sequence caution	The sequence AAF63815.1 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 – 33	33	Potential
	Chain	34 – 568	535	Probable pectinesterase/pectinesterase inhibitor 23		PRO_0000371679
Regions
	Region	45 – 198	154	Pectinesterase inhibitor 23
	Region	251 – 548	298	Pectinesterase 23
Sites
	Active site	386	1	Proton donor; for pectinesterase activity By similarity
	Active site	407	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	333	1	Substrate; for pectinesterase activity By similarity
	Binding site	363	1	Substrate; for pectinesterase activity By similarity
	Binding site	475	1	Substrate; for pectinesterase activity By similarity
	Binding site	477	1	Substrate; for pectinesterase activity By similarity
	Site	385	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	94	1	N-linked (GlcNAc...) Potential
	Glycosylation	210	1	N-linked (GlcNAc...) Potential
	Glycosylation	316	1	N-linked (GlcNAc...) Potential
	Disulfide bond	400 ↔ 420		By similarity
Experimental info
	Sequence conflict	107	1	K → E in BAC42959. Ref.2
	Sequence conflict	568	1	V → A in BAC42959. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8GXA1-1 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: FE92C797055361A7	FASTA	568	61,886
	10 20 30 40 50 60 MGSDGDKKKK FIVAGSVSGF LVIMVVSVAV VTSKHSPKDD ENHIRKTTKA VQAVCAPTDF 70 80 90 100 110 120 KDTCVNSLMG ASPDSDDPVD LIKLGFKVTI KSINESLEKA SGDIKAKADK NPEAKGAFEL 130 140 150 160 170 180 CEKLMIDAID DLKKCMDHGF SVDQIEVFVE DLRVWLSGSI AFQQTCMDSF GEIKSNLMQD 190 200 210 220 230 240 MLKIFKTSRE LSSNSLAMVT RISTLIPNSN LTGLTGALAK YARKLLSTED SIPTWVGPEA 250 260 270 280 290 300 RRLMAAQGGG PGPVKANAVV AQDGTGQFKT ITDALNAVPK GNKVPFIIHI KEGIYKEKVT 310 320 330 340 350 360 VTKKMPHVTF IGDGPNKTLI TGSLNFGIGK VKTFLTATIT IEGDHFTAKN IGIENTAGPE 370 380 390 400 410 420 GGQAVALRVS ADYAVFHSCQ IDGHQDTLYV HSHRQFYRDC TVSGTVDFIF GDAKCILQNC 430 440 450 460 470 480 KIVVRKPNKG QTCMVTAQGR SNVRESTGLV LHGCHITGDP AYIPMKSVNK AYLGRPWKEF 490 500 510 520 530 540 SRTIIMKTTI DDVIDPAGWL PWSGDFALKT LYYAEHMNTG PGSNQAQRVK WPGIKKLTPQ 550 560 DALLYTGDRF LRGDTWIPQT QVPYTAKV

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]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Arabidopsis ORF clones." Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC023912 Genomic DNA. Translation: AAF63815.1. Sequence problems. AK118345 mRNA. Translation: BAC42959.2. BT030353 mRNA. Translation: ABO38766.1.
IPI	IPI00523955.
RefSeq	NP_187339.2.
UniGene	At.40454
3D structure databases
HSSP	HSSP built from PDB template 1XG2 based on UniProtKB P14280.
SMR	Q8GXA1. Positions 50-201, 254-566.
ModBase	Search...
Proteomic databases
PRIDE	Q8GXA1.
Genome annotation databases
GeneID	819867.
GenomeReviews	Gene locus AT3G06830 in contig BA000014_GR.
KEGG	ath:AT3G06830.
Organism-specific databases
GeneFarm	484. 8.
TAIR	At3g06830.
Phylogenomic databases
eggNOG	COG4677.
HOGENOM	HBG747179.
Gene expression databases
Genevestigator	Q8GXA1.
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]
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

PME23_ARATH

Accession

Primary (citable) accession number: Q8GXA1
Secondary accession number(s): A4FVQ5, Q9M7Y9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	June 16, 2009
Last modified:	February 9, 2010
This is version 44 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)