Reviewed, UniProtKB/Swiss-Prot O22149 (PME17_ARATH)

Names and origin

Protein names

Recommended name:
    Probable pectinesterase/pectinesterase inhibitor 17
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 17
        Alternative name(s):
            Pectin methylesterase inhibitor 17
    2- Recommended name:
            Pectinesterase 17
                Short name=PE 17
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 17
              Short name=AtPME17

Gene names

Name:	PME17
Synonyms:	ARATH17
Ordered Locus Names:	At2g45220
ORF Names:	F4L23.27

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	511 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. Ref.4 Ref.6
Developmental stage	Expressed during late developmental phases of siliques. 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
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 membrane Inferred from direct assay. Source: TAIR
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 – 23	23	Potential
	Chain	24 – 511	488	Probable pectinesterase/pectinesterase inhibitor 17		PRO_0000371674
Regions
	Region	24 – 171	148	Pectinesterase inhibitor 17
	Region	237 – 414	178	Pectinesterase 17
Sites
	Active site	330	1	Proton donor; for pectinesterase activity By similarity
	Active site	351	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	277	1	Substrate; for pectinesterase activity By similarity
	Binding site	307	1	Substrate; for pectinesterase activity By similarity
	Binding site	418	1	Substrate; for pectinesterase activity By similarity
	Binding site	420	1	Substrate; for pectinesterase activity By similarity
	Site	329	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	112	1	N-linked (GlcNAc...) Potential
	Glycosylation	160	1	N-linked (GlcNAc...) Potential
	Disulfide bond	344 ↔ 364		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O22149-1 [UniParc]. Last modified June 1, 2002. Version 2. Checksum: 96487096A87F9375	FASTA	511	55,977
	10 20 30 40 50 60 MMAFRAYIIN FVILCILVAS TVSGYNQKDV KAWCSQTPNP KPCEYFLTHN SNNEPIKSES 70 80 90 100 110 120 EFLKISMKLV LDRAILAKTH AFTLGPKCRD TREKAAWEDC IKLYDLTVSK INETMDPNVK 130 140 150 160 170 180 CSKLDAQTWL STALTNLDTC RAGFLELGVT DIVLPLMSNN VSNLLCNTLA INKVPFNYTP 190 200 210 220 230 240 PEKDGFPSWV KPGDRKLLQS STPKDNAVVA KDGSGNFKTI KEAIDAASGS GRFVIYVKQG 250 260 270 280 290 300 VYSENLEIRK KNVMLRGDGI GKTIITGSKS VGGGTTTFNS ATVAAVGDGF IARGITFRNT 310 320 330 340 350 360 AGASNEQAVA LRSGSDLSVF YQCSFEAYQD TLYVHSNRQF YRDCDVYGTV DFIFGNAAAV 370 380 390 400 410 420 LQNCNIFARR PRSKTNTITA QGRSDPNQNT GIIIHNSRVT AASDLRPVLG STKTYLGRPW 430 440 450 460 470 480 RQYSRTVFMK TSLDSLIDPR GWLEWDGNFA LKTLFYAEFQ NTGPGASTSG RVTWPGFRVL 490 500 510 GSASEASKFT VGTFLAGGSW IPSSVPFTSG L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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.
[3]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 394-511. 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: 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
EMBLGenBankDDBJ	AC002387 Genomic DNA. Translation: AAB82640.2. AF361829 mRNA. Translation: AAK32841.1. AK220726 mRNA. Translation: BAD93862.1. Different initiation.
IPI	IPI00523541.
PIR	H84887.
RefSeq	NP_566038.1.
UniGene	At.27946
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBase	Search...
Proteomic databases
PRIDE	O22149.
Genome annotation databases
GeneID	819130.
GenomeReviews	Gene locus AT2G45220 in contig CT485783_GR.
KEGG	ath:AT2G45220.
NMPDR	fig|3702.1.peg.11701.
Organism-specific databases
GeneFarm	141. 8.
TAIR	At2g45220.
Phylogenomic databases
OMA	SEASKFT.
Gene expression databases
ArrayExpress	O22149.
Genevestigator	O22149.
Family and domain databases
InterPro	IPR006633. Carb-bd_sugar_hydrolysis-dom. 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]
SMART	SM00722. CASH. 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

PME17_ARATH

Accession

Primary (citable) accession number: O22149
Secondary accession number(s): Q570I2, Q9ASU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	June 1, 2002
Last modified:	November 3, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)