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Q5MFV8

- PME5_ARATH

UniProt

Q5MFV8 - PME5_ARATH

Protein

Pectinesterase 5

Gene

PME5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (15 Mar 2005)
      Previous versions | rss
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    Functioni

    Acts in the modification of cell walls via demethylesterification of cell wall pectin. Plays an important role in growth of pollen tubes in female floral tissues, possibly via enhancing the interaction between the pollen tube and female floral tissues by modification of the cell walls.1 Publication

    Catalytic activityi

    Pectin + n H2O = n methanol + pectate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei360 – 3601SubstrateBy similarity
    Binding sitei390 – 3901SubstrateBy similarity
    Sitei412 – 4121Transition state stabilizerBy similarity
    Active sitei413 – 4131Proton donorPROSITE-ProRule annotation
    Active sitei434 – 4341NucleophilePROSITE-ProRule annotation
    Binding sitei503 – 5031SubstrateBy similarity
    Binding sitei505 – 5051SubstrateBy similarity

    GO - Molecular functioni

    1. aspartyl esterase activity Source: UniProtKB-KW
    2. enzyme inhibitor activity Source: InterPro
    3. pectinesterase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell wall modification Source: InterPro
    2. pectin catabolic process Source: UniProtKB-UniPathway
    3. pollen tube growth Source: TAIR

    Keywords - Molecular functioni

    Aspartyl esterase, Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciARA:AT2G47040-MONOMER.
    BRENDAi3.1.1.11. 399.
    UniPathwayiUPA00545; UER00823.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pectinesterase 5 (EC:3.1.1.11)
    Short name:
    PE 5
    Alternative name(s):
    Pectin methylesterase 5
    Short name:
    AtPME5
    Pectin methylesterase 67
    Short name:
    AtPME67
    Protein VANGUARD 1
    Gene namesi
    Name:PME5
    Synonyms:ARATH67, VGD1
    Ordered Locus Names:At2g47040
    ORF Names:F14M4.13
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G47040.

    Subcellular locationi

    Cell membrane 1 Publication. Secretedcell wall 1 Publication
    Note: Distributed in the whole pollen tube, including the plasma membrane and pollen tube wall.

    GO - Cellular componenti

    1. cell wall Source: UniProtKB-SubCell
    2. extracellular region Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell
    4. pollen tube Source: TAIR

    Keywords - Cellular componenti

    Cell membrane, Cell wall, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 595571Pectinesterase 5PRO_0000023477Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ5MFV8.
    PRIDEiQ5MFV8.

    Expressioni

    Tissue specificityi

    Expressed in pollen grains and pollen tubes.1 Publication

    Developmental stagei

    Expressed throughout silique development.1 Publication

    Gene expression databases

    GenevestigatoriQ5MFV8.

    Interactioni

    Protein-protein interaction databases

    BioGridi4653. 2 interactions.
    STRINGi3702.AT2G47040.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5MFV8.
    SMRiQ5MFV8. Positions 285-595.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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

    eggNOGiCOG4677.
    HOGENOMiHOG000217409.
    InParanoidiQ5MFV8.
    OMAiTHANILM.
    PhylomeDBiQ5MFV8.

    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.
    IPR018040. Pectinesterase_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.
    PROSITEiPS00800. PECTINESTERASE_1. 1 hit.
    PS00503. PECTINESTERASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q5MFV8-1 [UniParc]FASTAAdd to Basket

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    MIGKVVVSVA SILLIVGVAI GVVAYINKNG DANLSPQMKA VRGICEATSD    50
    KASCVKTLEP VKSDDPNKLI KAFMLATRDA ITQSSNFTGK TEGNLGSGIS 100
    PNNKAVLDYC KKVFMYALED LSTIVEEMGE DLNQIGSKID QLKQWLTGVY 150
    NYQTDCLDDI EEDDLRKTIG EGIASSKILT SNAIDIFHTV VSAMAKLNLK 200
    VEDFKNMTGG IFAPSDKGAA PVNKGTPPVA DDSPVADPDG PARRLLEDID 250
    ETGIPTWVSG ADRKLMTKAG RGSNDGGARI RATFVVAKDG SGQFKTVQQA 300
    VNACPEKNPG RCIIHIKAGI YREQVIIPKK KNNIFMFGDG ARKTVISYNR 350
    SVKLSPGTTT SLSGTVQVES EGFMAKWIGF KNTAGPMGHQ AVAIRVNGDR 400
    AVIFNCRFDG YQDTLYVNNG RQFYRNIVVS GTVDFIFGKS ATVIQNSLIV 450
    VRKGNKGQFN TVTADGNEKG LAMKIGIVLQ NCRIVPDKKL AAERLIVESY 500
    LGRPWKKFST TVIINSEIGD VIRPEGWKIW DGESFHKSCR YVEYNNRGPG 550
    AITNRRVNWV KIARSAAEVN DFTVANWLGP INWIQEANVP VTLGL 595
    Length:595
    Mass (Da):64,728
    Last modified:March 15, 2005 - v2
    Checksum:iE314E53201F3CD77
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501D → V in AAV91508. (PubMed:15659637)Curated
    Sequence conflicti93 – 931G → E in CAB58974. 1 PublicationCurated
    Sequence conflicti138 – 1381K → E in AAV91508. (PubMed:15659637)Curated
    Sequence conflicti267 – 2671T → A(PubMed:15659637)Curated
    Sequence conflicti267 – 2671T → A1 PublicationCurated
    Sequence conflicti537 – 5371K → Q in AAV91508. (PubMed:15659637)Curated
    Sequence conflicti545 – 5451N → S in AAV91508. (PubMed:15659637)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY830948 mRNA. Translation: AAV91508.1.
    AJ250430 mRNA. Translation: CAB58974.1.
    AC004411 Genomic DNA. Translation: AAC34240.1.
    CP002685 Genomic DNA. Translation: AEC10791.1.
    AY091768 mRNA. Translation: AAM10316.1.
    BT001120 mRNA. Translation: AAN64511.1.
    PIRiT02183.
    T52327.
    RefSeqiNP_182227.1. NM_130272.3.
    UniGeneiAt.24875.

    Genome annotation databases

    EnsemblPlantsiAT2G47040.1; AT2G47040.1; AT2G47040.
    GeneIDi819318.
    KEGGiath:AT2G47040.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    When tough is soft - Issue 106 of June 2009

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY830948 mRNA. Translation: AAV91508.1 .
    AJ250430 mRNA. Translation: CAB58974.1 .
    AC004411 Genomic DNA. Translation: AAC34240.1 .
    CP002685 Genomic DNA. Translation: AEC10791.1 .
    AY091768 mRNA. Translation: AAM10316.1 .
    BT001120 mRNA. Translation: AAN64511.1 .
    PIRi T02183.
    T52327.
    RefSeqi NP_182227.1. NM_130272.3.
    UniGenei At.24875.

    3D structure databases

    ProteinModelPortali Q5MFV8.
    SMRi Q5MFV8. Positions 285-595.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 4653. 2 interactions.
    STRINGi 3702.AT2G47040.1-P.

    Proteomic databases

    PaxDbi Q5MFV8.
    PRIDEi Q5MFV8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G47040.1 ; AT2G47040.1 ; AT2G47040 .
    GeneIDi 819318.
    KEGGi ath:AT2G47040.

    Organism-specific databases

    GeneFarmi 443. 8.
    TAIRi AT2G47040.

    Phylogenomic databases

    eggNOGi COG4677.
    HOGENOMi HOG000217409.
    InParanoidi Q5MFV8.
    OMAi THANILM.
    PhylomeDBi Q5MFV8.

    Enzyme and pathway databases

    UniPathwayi UPA00545 ; UER00823 .
    BioCyci ARA:AT2G47040-MONOMER.
    BRENDAi 3.1.1.11. 399.

    Gene expression databases

    Genevestigatori Q5MFV8.

    Family and domain databases

    Gene3Di 1.20.140.40. 1 hit.
    2.160.20.10. 1 hit.
    InterProi IPR012334. Pectin_lyas_fold.
    IPR011050. Pectin_lyase_fold/virulence.
    IPR018040. Pectinesterase_AS.
    IPR000070. Pectinesterase_cat.
    IPR006501. Pectinesterase_inhib_dom.
    [Graphical view ]
    Pfami PF01095. Pectinesterase. 1 hit.
    PF04043. PMEI. 1 hit.
    [Graphical view ]
    SMARTi SM00856. PMEI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101148. SSF101148. 1 hit.
    SSF51126. SSF51126. 1 hit.
    TIGRFAMsi TIGR01614. PME_inhib. 1 hit.
    PROSITEi PS00800. PECTINESTERASE_1. 1 hit.
    PS00503. PECTINESTERASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "VANGUARD1 encodes a pectin methylesterase that enhances pollen tube growth in the Arabidopsis style and transmitting tract."
      Jiang L., Yang S.-L., Xie L.-F., Puah C.S., Zhang X.-Q., Yang W.-C., Sundaresan V., Ye D.
      Plant Cell 17:584-596(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Strain: cv. Landsberg erecta.
    2. "Characterization of a flower-specific gene encoding pectin methylesterase in Arabidopsis thaliana."
      Torki M., Mache R., Mandaron P., Falconet D.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Flower bud.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "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.
    6. "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.
    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] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiPME5_ARATH
    AccessioniPrimary (citable) accession number: Q5MFV8
    Secondary accession number(s): O80721, Q9SMV9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 85 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3