Q9M3B0 (PME34_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable pectinesterase/pectinesterase inhibitor 34

Including the following 2 domains:

1. Pectinesterase inhibitor 34
   Alternative name(s):
   Pectin methylesterase inhibitor 34
2. Pectinesterase 34
   Short name=PE 34
   EC=3.1.1.11
   Alternative name(s):
   Pectin methylesterase 34
   Short name=AtPME34

Gene names

Name:	PME34
Synonyms:	ARATH34
Ordered Locus Names:	At3g49220
ORF Names:	F2K15.80

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	598 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 siliques. Ref.6
Developmental stage	Expressed throughout silique development. 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 AAG40402.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Aspartyl esterase Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell wall modification Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9M3B0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9M3B0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     367-377: AATGAGFIARD → GEFFLTSLFLF
     378-598: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 598	598	Probable pectinesterase/pectinesterase inhibitor 34		PRO_0000371686
Regions
	Transmembrane	46 – 66	21	Helical; Potential
	Region	81 – 232	152	Pectinesterase inhibitor 34
	Region	284 – 582	299	Pectinesterase 34
Sites
	Active site	413	1	Proton donor; for pectinesterase activity By similarity
	Active site	434	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	360	1	Substrate; for pectinesterase activity By similarity
	Binding site	390	1	Substrate; for pectinesterase activity By similarity
	Binding site	502	1	Substrate; for pectinesterase activity By similarity
	Binding site	504	1	Substrate; for pectinesterase activity By similarity
	Site	412	1	Transition state stabilizer By similarity
Amino acid modifications
	Disulfide bond	427 ↔ 447		By similarity
Natural variations
	Alternative sequence	367 – 377	11	AATGAGFIARD → GEFFLTSLFLF in isoform 2.		VSP_037091
	Alternative sequence	378 – 598	221	Missing in isoform 2.		VSP_037092

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 7FDB338A79857A6D	FASTA	598	65,307
	10 20 30 40 50 60 MGYERLGPSG ATGSVTTSTT TAPILNQVST SEQPENNNRR SKKKLVVSSI VLAISLILAA 70 80 90 100 110 120 AIFAGVRSRL KLNQSVPGLA RKPSQAISKA CELTRFPELC VDSLMDFPGS LAASSSKDLI 130 140 150 160 170 180 HVTVNMTLHH FSHALYSSAS LSFVDMPPRA RSAYDSCVEL LDDSVDALSR ALSSVVSSSA 190 200 210 220 230 240 KPQDVTTWLS AALTNHDTCT EGFDGVDDGG VKDHMTAALQ NLSELVSNCL AIFSASHDGD 250 260 270 280 290 300 DFAGVPIQNR RLLGVEEREE KFPRWMRPKE REILEMPVSQ IQADIIVSKD GNGTCKTISE 310 320 330 340 350 360 AIKKAPQNST RRIIIYVKAG RYEENNLKVG RKKINLMFVG DGKGKTVISG GKSIFDNITT 370 380 390 400 410 420 FHTASFAATG AGFIARDITF ENWAGPAKHQ AVALRIGADH AVIYRCNIIG YQDTLYVHSN 430 440 450 460 470 480 RQFFRECDIY GTVDFIFGNA AVVLQNCSIY ARKPMDFQKN TITAQNRKDP NQNTGISIHA 490 500 510 520 530 540 SRVLAASDLQ ATNGSTQTYL GRPWKLFSRT VYMMSYIGGH VHTRGWLEWN TTFALDTLYY 550 560 570 580 590 GEYLNSGPGS GLGQRVSWPG YRVINSTAEA NRFTVAEFIY GSSWLPSTGV SFLAGLSI
	Isoform 2 [UniParc]. Checksum: EE457950C82DF5F8	FASTA	377	40,896
	10 20 30 40 50 60 MGYERLGPSG ATGSVTTSTT TAPILNQVST SEQPENNNRR SKKKLVVSSI VLAISLILAA 70 80 90 100 110 120 AIFAGVRSRL KLNQSVPGLA RKPSQAISKA CELTRFPELC VDSLMDFPGS LAASSSKDLI 130 140 150 160 170 180 HVTVNMTLHH FSHALYSSAS LSFVDMPPRA RSAYDSCVEL LDDSVDALSR ALSSVVSSSA 190 200 210 220 230 240 KPQDVTTWLS AALTNHDTCT EGFDGVDDGG VKDHMTAALQ NLSELVSNCL AIFSASHDGD 250 260 270 280 290 300 DFAGVPIQNR RLLGVEEREE KFPRWMRPKE REILEMPVSQ IQADIIVSKD GNGTCKTISE 310 320 330 340 350 360 AIKKAPQNST RRIIIYVKAG RYEENNLKVG RKKINLMFVG DGKGKTVISG GKSIFDNITT 370 FHTASFGEFF LTSLFLF

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]	"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] (ISOFORM 1). Strain: cv. Columbia.
[4]	"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] (ISOFORMS 1 AND 2). 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL132956 Genomic DNA. Translation: CAB66401.1. CP002686 Genomic DNA. Translation: AEE78512.1. AY059834 mRNA. Translation: AAL24316.1. BT008355 mRNA. Translation: AAP37714.1. AF325050 mRNA. Translation: AAG40402.1. Different initiation. AK226562 mRNA. Translation: BAE98692.1. AK226672 mRNA. Translation: BAE98780.1. AK229067 mRNA. Translation: BAF00948.1.
IPI	IPI00526905. IPI00929940.
PIR	T45827.
RefSeq	NP_190491.1. NM_114781.4.
UniGene	At.24776.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortal	Q9M3B0.
SMR	Q9M3B0. Positions 84-236, 247-596.
ModBase	Search...
Proteomic databases
PRIDE	Q9M3B0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G49220.1; AT3G49220.1; AT3G49220.
GeneID	824083.
GenomeReviews	Gene locus AT3G49220 in contig BA000014_GR.
KEGG	ath:AT3G49220.
NMPDR	fig|3702.1.peg.16166.
Organism-specific databases
TAIR	At3g49220.
Phylogenomic databases
eggNOG	COG4677.
GeneTree	EPGT00070000027901.
InParanoid	Q9M3B0.
OMA	TCKTISE.
PhylomeDB	Q9M3B0.
ProtClustDB	PLN02484.
Gene expression databases
Genevestigator	Q9M3B0.
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]
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME34_ARATH

Accession

Primary (citable) accession number: Q9M3B0
Secondary accession number(s): Q0WPK1, Q0WVR8, Q9FPG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program