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Protein

UDP-arabinopyranose mutase 2

Gene

RGP2

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

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

Mn2+By similarity, Mg2+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. UDP-arabinopyranose mutase activity Source: TAIR

GO - Biological processi

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

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 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G15650.

Subcellular locationi

  1. Cytoplasmcytosol
  2. Golgi apparatus

  3. 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
Complete GO annotation...

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.
ProMEXiQ9LFW1.

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

« Hide

        10         20         30         40         50
MVEPANTVGL PVNPTPLLKD ELDIVIPTIR NLDFLEMWRP FLQPYHLIIV
60 70 80 90 100
QDGDPSKKIH VPEGYDYELY NRNDINRILG PKASCISFKD SACRCFGYMV
110 120 130 140 150
SKKKYIFTID DDCFVAKDPS GKAVNALEQH IKNLLCPSSP FFFNTLYDPY
160 170 180 190 200
REGADFVRGY PFSLREGVST AVSHGLWLNI PDYDAPTQLV KPKERNTRYV
210 220 230 240 250
DAVMTIPKGT LFPMCGMNLA FDRDLIGPAM YFGLMGDGQP IGRYDDMWAG
260 270 280 290 300
WCIKVICDHL SLGVKTGLPY IYHSKASNPF VNLKKEYKGI FWQEEIIPFF
310 320 330 340 350
QNAKLSKEAV TVQQCYIELS KMVKEKLSSL DPYFDKLADA MVTWIEAWDE
360
LNPPAASGKA
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 (Ref. 5) Curated
Sequence conflicti38 – 381W → R in AAM65020 (Ref. 5) Curated
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

CAZyiGT75. Glycosyltransferase Family 75.

Proteomic databases

PRIDEiQ9LFW1.
ProMEXiQ9LFW1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT5G15650.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciARA:AT5G15650-MONOMER.

Miscellaneous databases

PROiQ9LFW1.

Gene expression databases

GenevestigatoriQ9LFW1.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 91 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

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 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.