Q84JX1 (PME19_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable pectinesterase/pectinesterase inhibitor 19

Including the following 2 domains:

1. Pectinesterase inhibitor 19
   Alternative name(s):
   Pectin methylesterase inhibitor 19
2. Pectinesterase 19
   Short name=PE 19
   EC=3.1.1.11
   Alternative name(s):
   Pectin methylesterase 19
   Short name=AtPME19
   Pectin methylesterase 5
   Short name=AtPME5

Gene names

Name:	PME19
Synonyms:	ARATH5
Ordered Locus Names:	At1g11590
ORF Names:	T23J18.25

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	524 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, but not in flower buds. Ref.5
Developmental stage	Expression restricted to early to mid-stage of silique development. Not found in vegetative stage. Expressed in the micropyle area of the ovule just after fertilization. Ref.5
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 AAF16638.1 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	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
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 – 22	22	Potential
	Chain	23 – 524	502	Probable pectinesterase/pectinesterase inhibitor 19		PRO_0000371675
Regions
	Region	23 – 172	150	Pectinesterase inhibitor 19
	Region	215 – 510	296	Pectinesterase 19
Sites
	Active site	343	1	Proton donor; for pectinesterase activity By similarity
	Active site	364	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	290	1	Substrate; for pectinesterase activity By similarity
	Binding site	430	1	Substrate; for pectinesterase activity By similarity
	Binding site	432	1	Substrate; for pectinesterase activity By similarity
	Site	342	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	265	1	N-linked (GlcNAc...) Potential
	Glycosylation	281	1	N-linked (GlcNAc...) Potential
	Glycosylation	412	1	N-linked (GlcNAc...) Potential
	Disulfide bond	357 ↔ 377		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q84JX1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 56405865F937BA1D	FASTA	524	58,692
	10 20 30 40 50 60 MLVKVFSFFI LMITMVVIGV SKEYCDDKQS CQNFLLELKA GSSSLSEIRR RDLLIIVLKN 70 80 90 100 110 120 SVRRIDMVMI GVMDDTKQHE EMENDLLGVK EDTKLFEEMM ESTKDRMIRS VEELLGGEFP 130 140 150 160 170 180 NRGSYENVHT WLSSVLTSYI TCIDEIGEGA YKRRVEPKLE DLISRARIAL ALFISISPRD 190 200 210 220 230 240 NTELISVIPN SPSWLFHVDK KDLYLNAEAL KKIADVVVAK DGTGKYSTVN AAIAAAPQHS 250 260 270 280 290 300 QKRFVIYIKT GIYDEIVVIE NTKPNLTLIG DGQDLTIITS NLSASNVRRT FNTATVASNG 310 320 330 340 350 360 NGFIGVDMCF RNTAGPAKGP AVALRVSGDM SVIYRCRVEG YQDALYPHSD RQFYRECFIT 370 380 390 400 410 420 GTVDFICGNA VAVFQFCQIV ARQPKMGQSN VITAQSRAFK DIYSGFTIQK CNITASSDLD 430 440 450 460 470 480 TTTVKTYLGR PWRIFSTVAV MQSFIGDLVD PAGWTPWEGE TGLSTLHYRE YQNRGPGAVT 490 500 510 520 SRRVKWSGFK VMKDPKQATE FTVAKLLDGE TWLKETRIPY ESGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [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]. 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC011661 Genomic DNA. Translation: AAF16638.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE28756.1. BT003962 mRNA. Translation: AAO42007.1. BT004987 mRNA. Translation: AAO50520.1.
IPI	IPI00526754.
RefSeq	NP_172625.3. NM_101032.3.
UniGene	At.42121.
3D structure databases
HSSP	HSSP built from PDB template 1XG2 based on UniProtKB P14280.
ProteinModelPortal	Q84JX1.
SMR	Q84JX1. Positions 212-524.
ModBase	Search...
Protein-protein interaction databases
STRING	Q84JX1.
Proteomic databases
PRIDE	Q84JX1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G11590.1; AT1G11590.1; AT1G11590.
GeneID	837702.
GenomeReviews	Gene locus AT1G11590 in contig CT485782_GR.
KEGG	ath:AT1G11590.
NMPDR	fig|3702.1.peg.1414.
Organism-specific databases
TAIR	At1g11590.
Phylogenomic databases
eggNOG	COG4677.
GeneTree	EPGT00070000028024.
HOGENOM	HBG747179.
InParanoid	Q84JX1.
OMA	RESEDDN.
PhylomeDB	Q84JX1.
ProtClustDB	PLN02488.
Gene expression databases
ArrayExpress	Q84JX1.
Genevestigator	Q84JX1.
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.
KO	K01051.
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.
PROSITE	PS00800. PECTINESTERASE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME19_ARATH

Accession

Primary (citable) accession number: Q84JX1
Secondary accession number(s): Q9LPX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	June 1, 2003
Last modified:	December 14, 2011
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program