Q9FM79 (PME62_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectinesterase QRT1
Short name=AtQRT1
Short name=PE QRT1
EC=3.1.1.11

Alternative name(s):
Pectin methylesterase 62
Short name=AtPME62
Pectin methylesterase QRT1
Protein QUARTET 1

Gene names

Name:	QRT1
Synonyms:	ARATH62
Ordered Locus Names:	At5g55590
ORF Names:	MDF20.3

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	380 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	Pectinesterase required for cell type-specific pectin degradation to separate microspores. Ref.1 Ref.4 Ref.5
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 Probable.
Tissue specificity	Expressed in flower buds, siliques, developing guard cells, floral nectares, at the stigmatic surface, in the hypocotyl-root transition zone and the area of lateral root emergence. Not expressed in mature leaves. Ref.1 Ref.7
Developmental stage	Expressed in anther tissues shortly after meiosis is completed and during the late developmental phases of siliques. Ref.1 Ref.7
Disruption phenotype	The mature pollen grains are arranged in a tetrad. Ref.1
Sequence similarities	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 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 pectin catabolic process Inferred from mutant phenotype Ref.5. Source: TAIR
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 pectinesterase activity Inferred from direct assay Ref.1. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Potential
	Chain	27 – 380	354	Pectinesterase QRT1		PRO_0000369432
Sites
	Active site	221	1	Proton donor By similarity
	Active site	242	1	Nucleophile By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	198	1	Substrate By similarity
	Binding site	298	1	Substrate By similarity
	Binding site	300	1	Substrate By similarity
	Site	220	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	74	1	N-linked (GlcNAc...) Potential
	Glycosylation	137	1	N-linked (GlcNAc...) Potential
	Glycosylation	227	1	N-linked (GlcNAc...) Potential
	Glycosylation	302	1	N-linked (GlcNAc...) Potential
	Disulfide bond	235 ↔ 255		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9FM79 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: E5F90B49EB73EF64	FASTA	380	42,475
	10 20 30 40 50 60 MKVEAFIPAV LLLCFGVMLC LKSSCALQIG NNNELKNYIS WEDLRVVEDG RIERSFSIKE 70 80 90 100 110 120 NSNWVTTNAN ANANATNVRR VIVVDKNGGG DSVTVQGAVD MVPDSNSQRV KIFILPGIYR 130 140 150 160 170 180 EKVIVPKSKP YISFIGNESY AGDTVISWSD KASDLGCDGK ELGTYRTASV SIESDFFCAT 190 200 210 220 230 240 AITFENTVVA EAGEQGRQAV ALRIIGDKAV FYRVRVLGSQ DTLFDDNGSH YFYQCYIQGN 250 260 270 280 290 300 VDFIFGNAKS LYQDCDIHST AKRYGAIAAH HRDSETEDTG FSFVNCDISG TGQIYLGRAW 310 320 330 340 350 360 GNYSRTVYSN CFIADIITPV GWSDWKHPER QRKVMFGEYN CRGRGAERGG RVPWSKTLTR 370 380 DEVKPFLGRE FIYGDQWLRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Separation of Arabidopsis pollen tetrads is regulated by QUARTET1, a pectin methylesterase gene." Francis K.E., Lam S.Y., Copenhaver G.P. Plant Physiol. 142:1004-1013(2006) [PubMed: 16980565] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE. Strain: cv. Columbia.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones." Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S. DNA Res. 5:41-54(1998) [PubMed: 9628582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Tetrad analysis possible in Arabidopsis with mutation of the QUARTET (QRT) genes." Preuss D., Rhee S.Y., Davis R.W. Science 264:1458-1460(1994) [PubMed: 8197459] [Abstract] Cited for: FUNCTION.
[5]	"Tetrad pollen formation in quartet mutants of Arabidopsis thaliana is associated with persistence of pectic polysaccharides of the pollen mother cell wall." Rhee S.Y., Somerville C.R. Plant J. 15:79-88(1998) [PubMed: 9744097] [Abstract] Cited for: FUNCTION.
[6]	"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.
[7]	"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	DQ979876 mRNA. Translation: ABI97858.1. AB009050 Genomic DNA. Translation: BAB09226.1. CP002688 Genomic DNA. Translation: AED96653.1.
IPI	IPI00524041.
RefSeq	NP_200370.1. NM_124941.2.
UniGene	At.29433. At.6552.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortal	Q9FM79.
SMR	Q9FM79. Positions 74-379.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9FM79.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G55590.1; AT5G55590.1; AT5G55590.
GeneID	835653.
GenomeReviews	Gene locus AT5G55590 in contig BA000015_GR.
KEGG	ath:AT5G55590.
NMPDR	fig|3702.1.peg.27486.
Organism-specific databases
GeneFarm	235. 8.
TAIR	At5g55590.
Phylogenomic databases
eggNOG	euNOG09608.
GeneTree	EPGT00070000028060.
HOGENOM	HBG747179.
InParanoid	Q9FM79.
OMA	GAVDMVP.
PhylomeDB	Q9FM79.
ProtClustDB	PLN02671.
Gene expression databases
Genevestigator	Q9FM79.
Family and domain databases
InterPro	IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. IPR000070. Pectinesterase_cat. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
Pfam	PF01095. Pectinesterase. 1 hit. [Graphical view]
SUPFAM	SSF51126. Pectin_lyas_like. 1 hit.
PROSITE	PS00800. PECTINESTERASE_1. False negative. PS00503. PECTINESTERASE_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME62_ARATH

Accession

Primary (citable) accession number: Q9FM79

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	March 1, 2001
Last modified:	December 14, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program