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Protein

Probable pectinesterase/pectinesterase inhibitor 41

Gene

PME41

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Acts in the modification of cell walls via demethylesterification of cell wall pectin.By similarity

Catalytic activityi

Pectin + n H2O = n methanol + pectate.

Pathwayi: pectin degradation

This protein is involved in step 1 of the subpathway that synthesizes 2-dehydro-3-deoxy-D-gluconate from pectin.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Probable pectinesterase/pectinesterase inhibitor 7 (PME7), Probable pectinesterase 48 (PME48), Probable pectinesterase 49 (PME49), Probable pectinesterase 50 (PME50), Pectinesterase, Probable pectinesterase/pectinesterase inhibitor 19 (PME19), Probable pectinesterase/pectinesterase inhibitor 42 (PME42), Probable pectinesterase 15 (PME15), Probable pectinesterase/pectinesterase inhibitor 40 (PME40), Putative pectinesterase 14 (PME14), Pectinesterase (At3g10720), Probable pectinesterase 55 (PME55), Probable pectinesterase/pectinesterase inhibitor 23 (PME23), Pectinesterase 4 (PME4), Putative pectinesterase/pectinesterase inhibitor 22 (PME22), Probable pectinesterase/pectinesterase inhibitor 39 (PME39), Pectinesterase (At3g14310), Pectinesterase/pectinesterase inhibitor 18 (PME18), Putative pectinesterase/pectinesterase inhibitor 43 (PME43), Probable pectinesterase/pectinesterase inhibitor 34 (PME34), Pectinesterase 1 (PME1), Putative pectinesterase 63 (PME63), Probable pectinesterase/pectinesterase inhibitor 64 (PME64), Putative pectinesterase 10 (PME10), Pectinesterase (F14I3.7), Pectinesterase 2 (PME2), Probable pectinesterase 29 (PME29), Pectinesterase, Probable pectinesterase/pectinesterase inhibitor 21 (PME21), Putative pectinesterase/pectinesterase inhibitor 45 (PME45), Probable pectinesterase/pectinesterase inhibitor 12 (PME12), Probable pectinesterase 8 (PME8), Probable pectinesterase/pectinesterase inhibitor 44 (PME44), Pectinesterase, Pectinesterase/pectinesterase inhibitor 3 (PME3), Pectinesterase 31 (PME31), Probable pectinesterase/pectinesterase inhibitor 25 (PME25), Probable pectinesterase/pectinesterase inhibitor 51 (PME51), Probable pectinesterase/pectinesterase inhibitor 58 (PME58), Putative pectinesterase 57 (PME57), Pectinesterase (At3g62170), Probable pectinesterase/pectinesterase inhibitor 20 (PME20), Pectinesterase (T27B3.30), Probable pectinesterase/pectinesterase inhibitor 60 (PME60), Pectinesterase QRT1 (QRT1), Probable pectinesterase/pectinesterase inhibitor 59 (PME59), Putative pectinesterase 11 (PME11), Pectinesterase PPME1 (PPME1), Probable pectinesterase/pectinesterase inhibitor 32 (PME32), Probable pectinesterase/pectinesterase inhibitor 33 (PME33), Probable pectinesterase/pectinesterase inhibitor 36 (PME36), Probable pectinesterase/pectinesterase inhibitor 13 (PME13), Putative pectinesterase 52 (PME52), Pectinesterase, Probable pectinesterase/pectinesterase inhibitor 54 (PME54), Pectinesterase, Pectinesterase (At1g53840), Probable pectinesterase/pectinesterase inhibitor 16 (PME16), Pectinesterase 5 (PME5), Probable pectinesterase 30 (PME30), Probable pectinesterase/pectinesterase inhibitor VGDH2 (VGDH2), Putative pectinesterase/pectinesterase inhibitor 24 (PME24), Putative pectinesterase/pectinesterase inhibitor 26 (PME26), Probable pectinesterase 68 (PME68), Probable pectinesterase/pectinesterase inhibitor 35 (PME35), Pectinesterase, Probable pectinesterase 67 (PME67), Putative pectinesterase/pectinesterase inhibitor 38 (PME38), Probable pectinesterase 56 (PME56), Pectinesterase, Putative pectinesterase/pectinesterase inhibitor 28 (PME28), Probable pectinesterase/pectinesterase inhibitor 47 (PME47), Probable pectinesterase/pectinesterase inhibitor 46 (PME46), Probable pectinesterase 53 (PME53), Probable pectinesterase/pectinesterase inhibitor 17 (PME17), Probable pectinesterase/pectinesterase inhibitor 41 (PME41), Probable pectinesterase/pectinesterase inhibitor 61 (PME61), Probable pectinesterase 66 (PME66), Probable pectinesterase/pectinesterase inhibitor 6 (PME6)
  2. Pectate lyase (T26I12.20), Probable pectate lyase 7 (At3g01270), Probable pectate lyase 18 (At4g24780), Probable pectate lyase 16 (At4g22080), Putative pectate lyase 17 (At4g22090), Putative pectate lyase 14 (At4g13210), Pectate lyase (At3g55140), Probable pectate lyase 20 (At5g48900), Probable pectate lyase 6 (At2g02720), Pectate lyase (At1g14420), Pectate lyase (At3g01270), Pectate lyase (At2g02720), Probable pectate lyase 22 (At5g63180), Pectate lyase (T5E8_80), Pectate lyase (At3g01270), Pectate lyase (At3g55140), Putative pectate lyase 2 (At1g11920), Pectate lyase (At3g07010), Pectate lyase, Probable pectate lyase 8 (At3g07010), Probable pectate lyase 4 (At1g30350), Probable pectate lyase 19 (At5g15110), Pectate lyase (F11F8_12), Probable pectate lyase 13 (PMR6), Probable pectate lyase 3 (AT59), Probable pectate lyase 5 (At1g67750), Putative pectate lyase 21 (At5g55720), Pectate lyase (At4g13210), Probable pectate lyase 12 (At3g53190), Pectate lyase (At4g24780), Pectate lyase (At5g04310), Pectate lyase (At4g13710), Probable pectate lyase 15 (At4g13710), Pectate lyase (At3g53190), Pectate lyase (At3g01270), Putative pectate lyase 11 (At3g27400), Pectate lyase (At5g04310), Pectate lyase (At3g07010), Probable pectate lyase 9 (At3g24230), Probable pectate lyase 1 (At1g04680), Probable pectate lyase 10 (At3g24670)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
This subpathway is part of the pathway pectin degradation, which is itself part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-dehydro-3-deoxy-D-gluconate from pectin, the pathway pectin degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei336 – 3361Substrate; for pectinesterase activityBy similarity
Binding sitei366 – 3661Substrate; for pectinesterase activityBy similarity
Sitei388 – 3881Transition state stabilizerBy similarity
Active sitei389 – 3891Proton donor; for pectinesterase activityPROSITE-ProRule annotation
Active sitei410 – 4101Nucleophile; for pectinesterase activityPROSITE-ProRule annotation
Binding sitei478 – 4781Substrate; for pectinesterase activityBy similarity
Binding sitei480 – 4801Substrate; for pectinesterase activityBy similarity

GO - Molecular functioni

  • aspartyl esterase activity Source: UniProtKB-KW
  • pectinesterase activity Source: TAIR
  • pectinesterase inhibitor activity Source: GO_Central

GO - Biological processi

  • cell wall modification Source: InterPro
  • negative regulation of catalytic activity Source: GOC
  • pectin catabolic process Source: UniProtKB-UniPathway
  • response to brassinosteroid Source: TAIR
  • response to cold Source: TAIR
  • response to fungus Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl esterase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciARA:AT4G02330-MONOMER.
UniPathwayiUPA00545; UER00823.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable pectinesterase/pectinesterase inhibitor 41
Including the following 2 domains:
Pectinesterase inhibitor 41
Alternative name(s):
Pectin methylesterase inhibitor 41
Pectinesterase 41 (EC:3.1.1.11)
Short name:
PE 41
Alternative name(s):
AtPMEpcrB
Pectin methylesterase 41
Short name:
AtPME41
Gene namesi
Name:PME41
Synonyms:ARATH41
Ordered Locus Names:At4g02330
ORF Names:T14P8.14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G02330.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 573551Probable pectinesterase/pectinesterase inhibitor 41PRO_0000371691Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi29 – 291N-linked (GlcNAc...)Sequence analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence analysis
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence analysis
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence analysis
Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence analysis
Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence analysis
Glycosylationi320 – 3201N-linked (GlcNAc...)Sequence analysis
Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence analysis
Disulfide bondi403 ↔ 423By similarity
Glycosylationi456 – 4561N-linked (GlcNAc...)Sequence analysis
Glycosylationi469 – 4691N-linked (GlcNAc...)Sequence analysis
Glycosylationi520 – 5201N-linked (GlcNAc...)Sequence analysis
Glycosylationi541 – 5411N-linked (GlcNAc...)Sequence analysis
Glycosylationi547 – 5471N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8RXK7.
PRIDEiQ8RXK7.

Expressioni

Tissue specificityi

Expressed in flowers, siliques, floral stems and rosettes leaves.2 Publications

Developmental stagei

Expressed throughout silique development.1 Publication

Gene expression databases

GenevisibleiQ8RXK7. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G02330.1.

Structurei

3D structure databases

ProteinModelPortaliQ8RXK7.
SMRiQ8RXK7. Positions 261-571.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 184160Pectinesterase inhibitor 41Add
BLAST
Regioni259 – 557299Pectinesterase 41Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi192 – 1954Poly-Lys

Sequence similaritiesi

In the N-terminal section; belongs to the PMEI family.Curated
In the C-terminal section; belongs to the pectinesterase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFP7. Eukaryota.
COG4677. LUCA.
HOGENOMiHOG000217409.
InParanoidiQ8RXK7.
KOiK01051.
OMAiPKNTHSH.
PhylomeDBiQ8RXK7.

Family and domain databases

Gene3Di1.20.140.40. 1 hit.
2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR033131. Pectinesterase_Asp_AS.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib_dom.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
SMARTiSM00856. PMEI. 1 hit.
[Graphical view]
SUPFAMiSSF101148. SSF101148. 1 hit.
SSF51126. SSF51126. 1 hit.
TIGRFAMsiTIGR01614. PME_inhib. 1 hit.
PROSITEiPS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8RXK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLKLFLVT LFLSLQTLFI ASQTLLPSNS SSTICKTTPD PKFCKSVFPQ
60 70 80 90 100
TSQGDVREYG RFSLRKSLTQ SRKFTRTIDR YLKRNNALLS QSAVGALQDC
110 120 130 140 150
RYLASLTTDY LITSFETVNI TTSSKTLSFS KADEIQTLLS AALTNEQTCL
160 170 180 190 200
DGINTAASSS WTIRNGVALP LINDTKLFSV SLALFTKGWV PKKKKQVASY
210 220 230 240 250
SWAHPKNTHS HTKPFRHFRN GALPLKMTEH TRAVYESLSR RKLADDDNDV
260 270 280 290 300
NTVLVSDIVT VNQNGTGNFT TITEAVNSAP NKTDGTAGYF VIYVTSGVYE
310 320 330 340 350
ENVVIAKNKR YLMMIGDGIN RTVVTGNRNV VDGWTTFNSA TFAVTSPNFV
360 370 380 390 400
AVNMTFRNTA GPEKHQAVAM RSSADLSIFY SCSFEAYQDT LYTHSLRQFY
410 420 430 440 450
RECDIYGTVD FIFGNAAVVF QDCNLYPRQP MQNQFNAITA QGRTDPNQNT
460 470 480 490 500
GISIHNCTIK PADDLVSSNY TVKTYLGRPW KEYSRTVFMQ SYIDEVVEPV
510 520 530 540 550
GWREWNGDFA LSTLYYAEYN NTGSGSSTTD RVVWPGYHVI NSTDANNFTV
560 570
ENFLLGDGWM VQSGVPYISG LLS
Length:573
Mass (Da):63,944
Last modified:May 5, 2009 - v2
Checksum:i863625D6142BB587
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti446 – 4461P → Q in AAL87311 (PubMed:14593172).Curated
Sequence conflicti455 – 4551H → Y in AAC02974 (PubMed:9767082).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069298 Genomic DNA. Translation: AAC19280.1.
AL161494 Genomic DNA. Translation: CAB80726.1.
CP002687 Genomic DNA. Translation: AEE82156.1.
AY150433 mRNA. Translation: AAN12975.1.
AY080836 mRNA. Translation: AAL87311.1.
AF033206 Genomic DNA. Translation: AAC02974.1.
PIRiT01317.
RefSeqiNP_567227.1. NM_116466.3.
UniGeneiAt.43016.

Genome annotation databases

EnsemblPlantsiAT4G02330.1; AT4G02330.1; AT4G02330.
GeneIDi828064.
GrameneiAT4G02330.1; AT4G02330.1; AT4G02330.
KEGGiath:AT4G02330.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069298 Genomic DNA. Translation: AAC19280.1.
AL161494 Genomic DNA. Translation: CAB80726.1.
CP002687 Genomic DNA. Translation: AEE82156.1.
AY150433 mRNA. Translation: AAN12975.1.
AY080836 mRNA. Translation: AAL87311.1.
AF033206 Genomic DNA. Translation: AAC02974.1.
PIRiT01317.
RefSeqiNP_567227.1. NM_116466.3.
UniGeneiAt.43016.

3D structure databases

ProteinModelPortaliQ8RXK7.
SMRiQ8RXK7. Positions 261-571.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G02330.1.

Proteomic databases

PaxDbiQ8RXK7.
PRIDEiQ8RXK7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G02330.1; AT4G02330.1; AT4G02330.
GeneIDi828064.
GrameneiAT4G02330.1; AT4G02330.1; AT4G02330.
KEGGiath:AT4G02330.

Organism-specific databases

TAIRiAT4G02330.

Phylogenomic databases

eggNOGiENOG410IFP7. Eukaryota.
COG4677. LUCA.
HOGENOMiHOG000217409.
InParanoidiQ8RXK7.
KOiK01051.
OMAiPKNTHSH.
PhylomeDBiQ8RXK7.

Enzyme and pathway databases

UniPathwayiUPA00545; UER00823.
BioCyciARA:AT4G02330-MONOMER.

Miscellaneous databases

PROiQ8RXK7.

Gene expression databases

GenevisibleiQ8RXK7. AT.

Family and domain databases

Gene3Di1.20.140.40. 1 hit.
2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR033131. Pectinesterase_Asp_AS.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib_dom.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
SMARTiSM00856. PMEI. 1 hit.
[Graphical view]
SUPFAMiSSF101148. SSF101148. 1 hit.
SSF51126. SSF51126. 1 hit.
TIGRFAMsiTIGR01614. PME_inhib. 1 hit.
PROSITEiPS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Characterization of the pectin methylesterase-like gene AtPME3: a new member of a gene family comprising at least 12 genes in Arabidopsis thaliana."
    Micheli F., Holliger C., Goldberg R., Richard L.
    Gene 220:13-20(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 406-484, TISSUE SPECIFICITY.
  5. "Pectin methylesterases: sequence-structural features and phylogenetic relationships."
    Markovic O., Janecek S.
    Carbohydr. Res. 339:2281-2295(2004) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiPME41_ARATH
AccessioniPrimary (citable) accession number: Q8RXK7
Secondary accession number(s): O49008, O81300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: March 16, 2016
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The PMEI region may act as an autoinhibitory domain and prevent untimely PME activity during transport.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.