Q8GX86 (PME21_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable pectinesterase/pectinesterase inhibitor 21

Including the following 2 domains:

1. Pectinesterase inhibitor 21
   Alternative name(s):
   Pectin methylesterase inhibitor 21
2. Pectinesterase 21
   Short name=PE 21
   EC=3.1.1.11
   Alternative name(s):
   Pectin methylesterase 21
   Short name=AtPME21

Gene names

Name:	PME21
Synonyms:	ARATH21
Ordered Locus Names:	At3g05610
ORF Names:	F18C1.12

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	669 AA.
Sequence status	Complete.
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. 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
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
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 component	cell wall Inferred from electronic annotation. Source: InterPro integral to membrane 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
	Chain	1 – 669	669	Probable pectinesterase/pectinesterase inhibitor 21		PRO_0000371677
Regions
	Transmembrane	16 – 36	21	Helical; Potential
	Region	52 – 205	154	Pectinesterase inhibitor 21
	Region	255 – 551	297	Pectinesterase 21
	Compositional bias	245 – 248	4	Poly-Ala
	Compositional bias	603 – 666	64	Ser-rich
Sites
	Active site	383	1	Proton donor; for pectinesterase activity By similarity
	Active site	404	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	330	1	Substrate; for pectinesterase activity By similarity
	Binding site	360	1	Substrate; for pectinesterase activity By similarity
	Binding site	472	1	Substrate; for pectinesterase activity By similarity
	Binding site	474	1	Substrate; for pectinesterase activity By similarity
	Site	382	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	52	1	N-linked (GlcNAc...) Potential
	Glycosylation	81	1	N-linked (GlcNAc...) Potential
	Glycosylation	94	1	N-linked (GlcNAc...) Potential
	Glycosylation	281	1	N-linked (GlcNAc...) Potential
	Glycosylation	300	1	N-linked (GlcNAc...) Potential
	Glycosylation	416	1	N-linked (GlcNAc...) Potential
	Disulfide bond	397 ↔ 417		By similarity
Experimental info
	Sequence conflict	330	1	T → A in BAC42986. Ref.3
	Sequence conflict	330	1	T → A in AAO64883. Ref.4
	Sequence conflict	383	1	D → N in BAC42986. Ref.3
	Sequence conflict	383	1	D → N in AAO64883. Ref.4
	Sequence conflict	630	1	S → F in BAC42986. Ref.3
	Sequence conflict	630	1	S → F in AAO64883. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8GX86 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 2D7DC0FF415EB573	FASTA	669	72,917
	10 20 30 40 50 60 MSYGYDDESK RKRRYIVITI SSVLLISMVV AVTVGVSLNK HDGDSKGKAE VNASVKAVKD 70 80 90 100 110 120 VCAPTDYRKT CEDTLIKNGK NTTDPMELVK TAFNVTMKQI TDAAKKSQTI MELQKDSRTR 130 140 150 160 170 180 MALDQCKELM DYALDELSNS FEELGKFEFH LLDEALINLR IWLSAAISHE ETCLEGFQGT 190 200 210 220 230 240 QGNAGETMKK ALKTAIELTH NGLAIISEMS NFVGQMQIPG LNSRRLLAEG FPSWVDQRGR 250 260 270 280 290 300 KLLQAAAAYS DVKPDIVVAQ DGSGQYKTIN EALQFVPKKR NTTFVVHIKA GLYKEYVQVN 310 320 330 340 350 360 KTMSHLVFIG DGPDKTIISG NKNYKDGITT YRTATVAIVG NYFIAKNIGF ENTAGAIKHQ 370 380 390 400 410 420 AVAVRVQSDE SIFFNCRFDG YQDTLYTHSH RQFFRDCTIS GTIDFLFGDA AAVFQNCTLL 430 440 450 460 470 480 VRKPLPNQAC PITAHGRKDP RESTGFVFQG CTIAGEPDYL AVKETSKAYL GRPWKEYSRT 490 500 510 520 530 540 IIMNTFIPDF VQPQGWQPWL GDFGLKTLFY SEVQNTGPGS ALANRVTWAG IKTLSEEDIL 550 560 570 580 590 600 KFTPAQYIQG DDWIPGKGVP YTTGLLAGNP AAATTTPSVS AAAPGFSTFT DTSGADSIAP 610 620 630 640 650 660 TASPAASPES SISMAYTGTA SPESSIKVSS STETASPESS FTEASTASPE SSIMVASTES SGSFFSMFT

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]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"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.
[4]	"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.
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC011620 Genomic DNA. Translation: AAF26136.1. CP002686 Genomic DNA. Translation: AEE74266.1. AK118374 mRNA. Translation: BAC42986.1. BT005948 mRNA. Translation: AAO64883.1.
IPI	IPI00538653.
RefSeq	NP_187212.1. NM_111434.2.
UniGene	At.40644.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortal	Q8GX86.
SMR	Q8GX86. Positions 56-210, 250-565.
ModBase	Search...
Proteomic databases
PRIDE	Q8GX86.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G05610.1; AT3G05610.1; AT3G05610.
GeneID	819727.
GenomeReviews	Gene locus AT3G05610 in contig BA000014_GR.
KEGG	ath:AT3G05610.
Organism-specific databases
GeneFarm	353. 8.
TAIR	At3g05610.
Phylogenomic databases
eggNOG	COG4677.
GeneTree	EPGT00070000028024.
OMA	ALTYQET.
PhylomeDB	Q8GX86.
Gene expression databases
Genevestigator	Q8GX86.
Family and domain databases
InterPro	IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. 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. False negative. PS00503. PECTINESTERASE_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME21_ARATH

Accession

Primary (citable) accession number: Q8GX86
Secondary accession number(s): Q9M9W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 5, 2009
Last modified:	December 14, 2011
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program