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Q9LFW1

- RGP2_ARATH

UniProt

Q9LFW1 - RGP2_ARATH

Protein

UDP-arabinopyranose mutase 2

Gene

RGP2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides. Catalyzes the interconvertion of UDP-L-arabinopyranose (UDP-Arap) and UDP-L-arabinofuranose (UDP-Araf) in vitro. Preferentially catalyzes the formation of UDP-Arap from UDP-Araf. At thermodynamic equilibrium in vitro the ratio of the pyranose form over the furanose form is 95:5. Is not active on other UDP-sugars (UDP-Gal, UDP-Xyl, UDP-Glc, GDP-Man and GDP-Fuc). Functions redundantly with RGP2 and is essential for proper cell walls and pollen development. Probably involved in the formation of the pectocellulosic cell wall layer intine. Is probably active as heteromer in vivo.2 Publications

    Catalytic activityi

    UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose.

    Cofactori

    Manganese or Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei158 – 1581Required for activityBy similarity
    Sitei165 – 1651Required for activityBy similarity

    GO - Molecular functioni

    1. intramolecular transferase activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. UDP-arabinopyranose mutase activity Source: TAIR

    GO - Biological processi

    1. cellulose biosynthetic process Source: InterPro
    2. plant-type cell wall organization or biogenesis Source: UniProtKB
    3. pollen development Source: UniProtKB
    4. response to cadmium ion Source: TAIR
    5. response to salt stress Source: TAIR
    6. UDP-L-arabinose metabolic process Source: TAIR

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciARA:AT5G15650-MONOMER.

    Protein family/group databases

    CAZyiGT75. Glycosyltransferase Family 75.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-arabinopyranose mutase 2 (EC:5.4.99.30)
    Alternative name(s):
    Reversibly glycosylated polypeptide 2
    Short name:
    AtRGP2
    UDP-L-arabinose mutase 2
    Gene namesi
    Name:RGP2
    Ordered Locus Names:At5g15650
    ORF Names:F14F8.30
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G15650.

    Subcellular locationi

    Cytoplasmcytosol. Golgi apparatus
    Note: Soluble and membrane-associated.

    GO - Cellular componenti

    1. cell wall Source: TAIR
    2. cytosol Source: UniProtKB
    3. cytosolic ribosome Source: TAIR
    4. Golgi apparatus Source: UniProtKB
    5. membrane Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype under normal growth condition, but significant reduction in total cell wall arabinose. Rgp1 and rgp2 double mutant is male gametophyte lethal, with an arrest in pollen mitosis (PubMed:17071651). RNAi-mediated knockdown of both RGP1 and RGP2 causes severe developmental defects and strong reduction in total cell wall arabinose (PubMed:21478444).2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 360359UDP-arabinopyranose mutase 2PRO_0000410985Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylvaline1 Publication

    Post-translational modificationi

    Reversibly glycosylated in vitro by UDP-glucose, UDP-xylose and UDP-galactose, but not UDP-mannose.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    PRIDEiQ9LFW1.

    Expressioni

    Tissue specificityi

    Predominantly expressed in shoot and root apical meristems. Expressed in epidermal cells of leaves, inflorescence stems and seed coat. Expressed in pollen.2 Publications

    Gene expression databases

    GenevestigatoriQ9LFW1.

    Interactioni

    Subunit structurei

    Heteromers with RGP1, RGP4 and RGP5.1 Publication

    Protein-protein interaction databases

    BioGridi16695. 3 interactions.
    IntActiQ9LFW1. 2 interactions.
    STRINGi3702.AT5G15650.1-P.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi110 – 1123DXD motif

    Domaini

    The conserved DXD motif is involved in enzyme activity.By similarity

    Sequence similaritiesi

    Belongs to the RGP family.Curated

    Phylogenomic databases

    eggNOGiNOG82578.
    HOGENOMiHOG000234443.
    InParanoidiQ9LFW1.
    KOiK13379.
    OMAiQCYIELS.
    PhylomeDBiQ9LFW1.

    Family and domain databases

    InterProiIPR029044. Nucleotide-diphossugar_trans.
    IPR004901. RGP_fam.
    [Graphical view]
    PfamiPF03214. RGP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016429. UPTG. 1 hit.
    SUPFAMiSSF53448. SSF53448. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9LFW1-1 [UniParc]FASTAAdd to Basket

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    MVEPANTVGL PVNPTPLLKD ELDIVIPTIR NLDFLEMWRP FLQPYHLIIV    50
    QDGDPSKKIH VPEGYDYELY NRNDINRILG PKASCISFKD SACRCFGYMV 100
    SKKKYIFTID DDCFVAKDPS GKAVNALEQH IKNLLCPSSP FFFNTLYDPY 150
    REGADFVRGY PFSLREGVST AVSHGLWLNI PDYDAPTQLV KPKERNTRYV 200
    DAVMTIPKGT LFPMCGMNLA FDRDLIGPAM YFGLMGDGQP IGRYDDMWAG 250
    WCIKVICDHL SLGVKTGLPY IYHSKASNPF VNLKKEYKGI FWQEEIIPFF 300
    QNAKLSKEAV TVQQCYIELS KMVKEKLSSL DPYFDKLADA MVTWIEAWDE 350
    LNPPAASGKA 360
    Length:360
    Mass (Da):40,890
    Last modified:October 1, 2000 - v1
    Checksum:i8FE4D48C555F97F1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91G → R in AAM65020. 1 PublicationCurated
    Sequence conflicti38 – 381W → R in AAM65020. 1 PublicationCurated
    Sequence conflicti206 – 2061I → N in AAC50001. (PubMed:9536051)Curated
    Sequence conflicti233 – 2331G → V in AAC50001. (PubMed:9536051)Curated
    Sequence conflicti360 – 3601A → SLRAV in AAC50001. (PubMed:9536051)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF013628 mRNA. Translation: AAC50001.1.
    AL391144 Genomic DNA. Translation: CAC01764.1.
    CP002688 Genomic DNA. Translation: AED92188.1.
    AY039846 mRNA. Translation: AAK63950.1.
    AY120691 mRNA. Translation: AAM52234.1.
    AY087476 mRNA. Translation: AAM65020.1.
    PIRiT51394.
    RefSeqiNP_197069.1. NM_121569.2.
    UniGeneiAt.24638.

    Genome annotation databases

    EnsemblPlantsiAT5G15650.1; AT5G15650.1; AT5G15650.
    GeneIDi831419.
    KEGGiath:AT5G15650.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF013628 mRNA. Translation: AAC50001.1 .
    AL391144 Genomic DNA. Translation: CAC01764.1 .
    CP002688 Genomic DNA. Translation: AED92188.1 .
    AY039846 mRNA. Translation: AAK63950.1 .
    AY120691 mRNA. Translation: AAM52234.1 .
    AY087476 mRNA. Translation: AAM65020.1 .
    PIRi T51394.
    RefSeqi NP_197069.1. NM_121569.2.
    UniGenei At.24638.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 16695. 3 interactions.
    IntActi Q9LFW1. 2 interactions.
    STRINGi 3702.AT5G15650.1-P.

    Protein family/group databases

    CAZyi GT75. Glycosyltransferase Family 75.

    Proteomic databases

    PRIDEi Q9LFW1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G15650.1 ; AT5G15650.1 ; AT5G15650 .
    GeneIDi 831419.
    KEGGi ath:AT5G15650.

    Organism-specific databases

    TAIRi AT5G15650.

    Phylogenomic databases

    eggNOGi NOG82578.
    HOGENOMi HOG000234443.
    InParanoidi Q9LFW1.
    KOi K13379.
    OMAi QCYIELS.
    PhylomeDBi Q9LFW1.

    Enzyme and pathway databases

    BioCyci ARA:AT5G15650-MONOMER.

    Gene expression databases

    Genevestigatori Q9LFW1.

    Family and domain databases

    InterProi IPR029044. Nucleotide-diphossugar_trans.
    IPR004901. RGP_fam.
    [Graphical view ]
    Pfami PF03214. RGP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016429. UPTG. 1 hit.
    SUPFAMi SSF53448. SSF53448. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of AtRGP1. A reversibly autoglycosylated arabidopsis protein implicated in cell wall biosynthesis."
      Delgado I.J., Wang Z., de Rocher A., Keegstra K., Raikhel N.V.
      Plant Physiol. 116:1339-1350(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [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. "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.
    5. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Arabidopsis reversibly glycosylated polypeptides 1 and 2 are essential for pollen development."
      Drakakaki G., Zabotina O., Delgado I., Robert S., Keegstra K., Raikhel N.
      Plant Physiol. 142:1480-1492(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    7. "The interconversion of UDP-L-arabinopyranose and UDP-L-arabinofuranose is indispensable for plant development in Arabidopsis."
      Rautengarten C., Ebert B., Herter T., Petzold C.J., Ishii T., Mukhopadhyay A., Usadel B., Scheller H.V.
      Plant Cell 23:1373-1390(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, DISRUPTION PHENOTYPE.
    8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRGP2_ARATH
    AccessioniPrimary (citable) accession number: Q9LFW1
    Secondary accession number(s): O22428, Q8LB19
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 27, 2011
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3