Q7Y201 (PME13_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable pectinesterase/pectinesterase inhibitor 13

Including the following 2 domains:

1. Pectinesterase inhibitor 13
   Alternative name(s):
   Pectin methylesterase inhibitor 13
2. Pectinesterase 13
   Short name=PE 13
   EC=3.1.1.11
   Alternative name(s):
   Pectin methylesterase 13
   Short name=AtPME13

Gene names

Name:	PME13
Synonyms:	ARATH13
Ordered Locus Names:	At2g26450
ORF Names:	T9J22.12

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	614 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.
Sequence caution	The sequence AAC14494.1 differs from that shown. Reason: Erroneous initiation.

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 – 614	614	Probable pectinesterase/pectinesterase inhibitor 13		PRO_0000371670
Regions
	Transmembrane	25 – 45	21	Helical; Potential
	Region	103 – 255	153	Pectinesterase inhibitor 13
	Region	301 – 598	298	Pectinesterase 13
	Compositional bias	55 – 61	7	Poly-Gln
Sites
	Active site	429	1	Proton donor; for pectinesterase activity By similarity
	Active site	450	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	376	1	Substrate; for pectinesterase activity By similarity
	Binding site	406	1	Substrate; for pectinesterase activity By similarity
	Binding site	518	1	Substrate; for pectinesterase activity By similarity
	Binding site	520	1	Substrate; for pectinesterase activity By similarity
	Site	428	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	66	1	N-linked (GlcNAc...) Potential
	Glycosylation	128	1	N-linked (GlcNAc...) Potential
	Glycosylation	197	1	N-linked (GlcNAc...) Potential
	Glycosylation	243	1	N-linked (GlcNAc...) Potential
	Glycosylation	301	1	N-linked (GlcNAc...) Potential
	Glycosylation	351	1	N-linked (GlcNAc...) Potential
	Glycosylation	367	1	N-linked (GlcNAc...) Potential
	Glycosylation	522	1	N-linked (GlcNAc...) Potential
	Glycosylation	588	1	N-linked (GlcNAc...) Potential
	Disulfide bond	443 ↔ 463		By similarity
Experimental info
	Sequence conflict	277	1	D → G in AAP40488. Ref.3
	Sequence conflict	277	1	D → G in BAF01447. Ref.4
	Sequence conflict	402	1	P → S in AAP40488. Ref.3
	Sequence conflict	402	1	P → S in BAF01447. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q7Y201 [UniParc]. Last modified May 3, 2011. Version 2. Checksum: AFEAEE5C9FF327D6	FASTA	614	68,601
	10 20 30 40 50 60 MAFQDFDKIQ ERVNANRKRK FRKRIIVGTV SLLVVVAAIV GGAFAYVAYE KRNEQQQQQQ 70 80 90 100 110 120 QAKNHNKSGS GNNVVKDSDK KSPSPPTPSQ KAPVSAAQSV KPGQGDKIIQ TLCSSTLYMQ 130 140 150 160 170 180 ICEKTLKNRT DKGFALDNPT TFLKSAIEAV NEDLDLVLEK VLSLKTENQD DKDAIEQCKL 190 200 210 220 230 240 LVEDAKEETV ASLNKINVTE VNSFEKVVPD LESWLSAVMS YQETCLDGFE EGNLKSEVKT 250 260 270 280 290 300 SVNSSQVLTS NSLALIKTFT ENLSPVMKVV ERHLLDDIPS WVSNDDRRML RAVDVKALKP 310 320 330 340 350 360 NATVAKDGSG DFTTINDALR AMPEKYEGRY IIYVKQGIYD EYVTVDKKKA NLTMVGDGSQ 370 380 390 400 410 420 KTIVTGNKSH AKKIRTFLTA TFVAQGEGFM AQSMGFRNTA GPEGHQAVAI RVQSDRSIFL 430 440 450 460 470 480 NCRFEGYQDT LYAYTHRQYY RSCVIVGTID FIFGDAAAIF QNCNIFIRKG LPGQKNTVTA 490 500 510 520 530 540 QGRVDKFQTT GFVVHNCKIA ANEDLKPVKE EYKSYLGRPW KNYSRTIIME SKIENVIDPV 550 560 570 580 590 600 GWLRWQETDF AIDTLYYAEY NNKGSSGDTT SRVKWPGFKV INKEEALNYT VGPFLQGDWI 610 SASGSPVKLG LYDA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [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]	"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.
[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	AC002505 Genomic DNA. Translation: AAC14494.1. Different initiation. CP002685 Genomic DNA. Translation: AEC07840.1. BT008681 mRNA. Translation: AAP40488.1. AK229600 mRNA. Translation: BAF01447.1.
IPI	IPI00521390.
PIR	T00978.
RefSeq	NP_850077.1. NM_179746.1.
UniGene	At.38894. At.70844.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortal	Q7Y201.
SMR	Q7Y201. Positions 296-611.
ModBase	Search...
Proteomic databases
PRIDE	Q7Y201.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G26450.1; AT2G26450.1; AT2G26450.
GeneID	817185.
GenomeReviews	Gene locus AT2G26450 in contig CT485783_GR.
KEGG	ath:AT2G26450.
Organism-specific databases
GeneFarm	229. 8.
TAIR	At2g26450.
Phylogenomic databases
eggNOG	euNOG09608.
GeneTree	EPGT00070000028024.
InParanoid	Q7Y201.
OMA	QGDWISA.
Gene expression databases
Genevestigator	Q7Y201.
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

PME13_ARATH

Accession

Primary (citable) accession number: Q7Y201
Secondary accession number(s): O48712

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 3, 2011
Last modified:	September 21, 2011
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program