Reviewed, UniProtKB/Swiss-Prot Q84R10 (PME36_ARATH)

Names and origin

Protein names

Recommended name:
    Probable pectinesterase/pectinesterase inhibitor 36
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 36
        Alternative name(s):
            Pectin methylesterase inhibitor 36
    2- Recommended name:
            Pectinesterase 36
                Short name=PE 36
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 36
              Short name=AtPME36

Gene names

Name:	PME36
Synonyms:	ARATH36
Ordered Locus Names:	At3g60730
ORF Names:	T4C21.140

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	519 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.5
Developmental stage	Expressed during early seed development and late developmental phases of siliques. Ref.5 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.
Sequence caution	The sequence CAB82677.1 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	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 – 25	25	Potential
	Chain	26 – 519	494	Probable pectinesterase/pectinesterase inhibitor 36		PRO_0000370181
Regions
	Region	27 – 141	115	Pectinesterase inhibitor 36
	Region	205 – 505	301	Pectinesterase 36
Sites
	Active site	336	1	Proton donor; for pectinesterase activity By similarity
	Active site	357	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	283	1	Substrate; for pectinesterase activity By similarity
	Binding site	313	1	Substrate; for pectinesterase activity By similarity
	Binding site	425	1	Substrate; for pectinesterase activity By similarity
	Binding site	427	1	Substrate; for pectinesterase activity By similarity
	Site	335	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	130	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q84R10-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D7270920705B1034	FASTA	519	57,931
	10 20 30 40 50 60 MSTFVKVTDL ITIMFFLAIA AVITASNTAE LDVLEMARTA VVEAKTSFGS MAVTEATSEV 70 80 90 100 110 120 AGSYYKLGLS ECEKLYDESE ARLSKLVVDH ENFTVEDVRT WLSGVLANHH TCLDGLIQQR 130 140 150 160 170 180 QGHKPLVHSN VTFVLHEALA FYKKSRGHMK KRLHGPARQG HGPTRPKHRP TRPNHGPGRS 190 200 210 220 230 240 HHGPSRPNQN GGMLVSWNPT SSRADFVVAR DGSATHRTIN QALAAVSRMG KSRLNRVIIY 250 260 270 280 290 300 IKAGVYNEKI EIDRHMKNIM LVGDGMDRTI VTNNRNVPDG STTYGSATFG VSGDGFWARD 310 320 330 340 350 360 ITFENTAGPH KHQAVALRVS SDLSLFYRCS FKGYQDTLFT HSLRQFYRDR HIYGTIDFIF 370 380 390 400 410 420 GDAAAVFQNC DIFVRRPMDH QGNMITAQGR DDPHTNSGIS IQHSRIRAAP EFEAVKGRFK 430 440 450 460 470 480 SYLGRPWKKY SRTVFLKTDI DELIDPRGWR EWSGSYALST LYYGEFMNTG AGAGTGRRVN 490 500 510 WPGFHVLRGE EEASPFTVSR FIQGDSWIPI TGVPFSAGV

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]	"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 (JUL-2006) 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, DEVELOPMENTAL STAGE.
[6]	"Computational and experimental analysis identifies Arabidopsis genes specifically expressed during early seed development." Becerra C., Puigdomenech P., Vicient C.M. BMC Genomics 7:38-38(2006) [PubMed: 16504176] [Abstract] Cited for: DEVELOPMENTAL STAGE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL162295 Genomic DNA. Translation: CAB82677.1. Sequence problems. BT006181 mRNA. Translation: AAP04164.1. AK228563 mRNA. Translation: BAF00482.1.
IPI	IPI00534345.
PIR	T47884.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBase	Search...
Proteomic databases
PRIDE	Q84R10.
Genome annotation databases
GenomeReviews	Gene locus AT3G60730 in contig BA000014_GR.
Organism-specific databases
GeneFarm	438. 8.
TAIR	At3g60730.
Gene expression databases
ArrayExpress	Q84R10.
Genevestigator	Q84R10.
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.
Pfam	PF01095. Pectinesterase. 1 hit. PF04043. PMEI. 1 hit. [Graphical view]
PROSITE	PS00800. PECTINESTERASE_1. False negative. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME36_ARATH

Accession

Primary (citable) accession number: Q84R10
Secondary accession number(s): Q9LZZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	June 1, 2003
Last modified:	October 13, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)