Q9SRT9 (RGP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-arabinopyranose mutase 1
EC=5.4.99.30

Alternative name(s):
Reversibly glycosylated polypeptide 1
Short name=AtRGP1
UDP-L-arabinose mutase 1

Gene names

Name:	RGP1
Ordered Locus Names:	At3g02230
ORF Names:	F14P3.12

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6
Catalytic activity	UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose.
Cofactor	Manganese or Magnesium By similarity.
Subunit structure	Heteromers with RGP2, RGP3, RGP4 and RGP5. Ref.5
Subcellular location	Cytoplasm › cytosol. Golgi apparatus. Note: Soluble and associated with peripheral membrane and endomembrane system. Ref.5 Ref.6
Tissue specificity	Predominantly expressed in shoot and root apical meristems. Expressed in epidermal cells of leaves, inflorescence stems and seed coat. Expressed in pollen. Ref.1 Ref.5 Ref.6
Domain	The conserved DXD motif is involved in enzyme activity By similarity.
Post-translational modification	Reversibly glycosylated in vitro by UDP-glucose, UDP-xylose and UDP-galactose, but not UDP-mannose. Ref.1
Disruption phenotype	No visible phenotype under normal growth condition, but significant reduction in total cell wall arabinose. Ref.5 Ref.6
Miscellaneous	The double mutant rgp1/rgp2 is male gametophyte lethal, with an arrest in pollen mitosis. Plants silencing both RGP1 and RGP2 show severe developmental defects and strong reduction in total cell wall arabinose.
Sequence similarities	Belongs to the RGP family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cytoplasm Golgi apparatus
Molecular function	Isomerase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-L-arabinose metabolic process Inferred from mutant phenotype Ref.6. Source: TAIR cellulose biosynthetic process Inferred from electronic annotation. Source: InterPro plant-type cell wall biogenesis Traceable author statement PubMed 9207152. Source: TAIR pollen development Inferred from genetic interaction Ref.5. Source: UniProtKB response to salt stress Inferred from expression pattern PubMed 17916636. Source: TAIR
Cellular_component	Golgi trans cisterna Inferred from direct assay PubMed 9207152. Source: TAIR cell wall Inferred from direct assay PubMed 16287169. Source: TAIR cytosolic ribosome Inferred from direct assay PubMed 15734919. Source: TAIR vacuolar membrane Inferred from direct assay PubMed 17151019. Source: TAIR
Molecular_function	UDP-arabinopyranose mutase activity Inferred from direct assay Ref.6. Source: TAIR cellulose synthase (UDP-forming) activity Inferred from sequence or structural similarity PubMed 9207152. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 357	357	UDP-arabinopyranose mutase 1		PRO_0000410984
Regions
	Motif	110 – 112	3	DXD motif
Sites
	Site	158	1	Required for activity By similarity
	Site	165	1	Required for activity By similarity
Experimental info
	Sequence conflict	42	1	L → F in AAC50000. Ref.1
	Sequence conflict	221	1	F → Y in AAC50000. Ref.1
	Sequence conflict	303	1	A → P in AAC50000. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9SRT9 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 363BA6049415C465	FASTA	357	40,629
	10 20 30 40 50 60 MVEPANTVGI PVNHIPLLKD ELDIVIPTIR NLDFLEMWRP FLQPYHLIIV QDGDPSKTIA 70 80 90 100 110 120 VPEGFDYELY NRNDINRILG PKASCISFKD SACRCFGYMV SKKKYIFTID DDCFVAKDPS 130 140 150 160 170 180 GKAVNALEQH IKNLLCPSTP FFFNTLYDPY REGADFVRGY PFSLREGVST AVSHGLWLNI 190 200 210 220 230 240 PDYDAPTQLV KPKERNTRYV DAVMTIPKGT LFPMCGMNLA FDRELIGPAM YFGLMGDGQP 250 260 270 280 290 300 IGRYDDMWAG WCIKVICDHL GLGVKTGLPY IYHSKASNPF VNLKKEYKGI FWQEDIIPFF 310 320 330 340 350 QSAKLTKEAV TVQQCYMELS KLVKEKLSPI DPYFDKLADA MVTWIEAWDE LNPPTKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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], TISSUE SPECIFICITY, GLYCOSYLATION.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(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]	"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.
[6]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF013627 mRNA. Translation: AAC50000.1. AC009755 Genomic DNA. Translation: AAF02115.1. CP002686 Genomic DNA. Translation: AEE73781.1. BT002409 mRNA. Translation: AAO00769.1. BT008841 mRNA. Translation: AAP68280.1.
IPI	IPI00538961.
RefSeq	NP_186872.1. NM_111090.3.
UniGene	At.24058.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9SRT9. 1 interaction.
STRING	3702.AT3G02230.1-P.
Protein family/group databases
CAZy	GT75. Glycosyltransferase Family 75.
Proteomic databases
PRIDE	Q9SRT9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	821233.
KEGG	ath:AT3G02230.
Organism-specific databases
TAIR	At3g02230.
Phylogenomic databases
eggNOG	NOG82578.
HOGENOM	HOG000234443.
InParanoid	Q9SRT9.
KO	K13379.
OMA	PTKTIRV.
PhylomeDB	Q9SRT9.
ProtClustDB	PLN03180.
Enzyme and pathway databases
BioCyc	ARA:AT3G02230-MONOMER. MetaCyc:AT3G02230-MONOMER.
Gene expression databases
Genevestigator	Q9SRT9.
Family and domain databases
InterPro	IPR004901. RGP_fam. [Graphical view]
Pfam	PF03214. RGP. 1 hit. [Graphical view]
PIRSF	PIRSF016429. UPTG. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RGP1_ARATH

Accession

Primary (citable) accession number: Q9SRT9
Secondary accession number(s): O22427

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program