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UDP-arabinopyranose mutase 1 (EC 5.4.99.30) (Reversibly glycosylated polypeptide 1) (AtRGP1) (UDP-L-arabinose mutase 1)

 RGP1_ARATH              Reviewed;         357 AA.
Q9SRT9; O22427; W8PVH6;
27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
31-JAN-2018, entry version 111.
RecName: Full=UDP-arabinopyranose mutase 1 {ECO:0000305};
EC=5.4.99.30 {ECO:0000269|PubMed:21478444};
AltName: Full=Reversibly glycosylated polypeptide 1 {ECO:0000303|PubMed:21478444};
Short=AtRGP1 {ECO:0000303|PubMed:21478444};
AltName: Full=UDP-L-arabinose mutase 1 {ECO:0000305};
Name=RGP1 {ECO:0000303|PubMed:21478444};
OrderedLocusNames=At3g02230 {ECO:0000312|Araport:AT3G02230};
ORFNames=F14P3.12 {ECO:0000312|EMBL:AAF02115.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND GLYCOSYLATION.
PubMed=9536051; DOI=10.1104/pp.116.4.1339;
Delgado I.J., Wang Z., de Rocher A., Keegstra K., Raikhel N.V.;
"Cloning and characterization of AtRGP1. A reversibly autoglycosylated
arabidopsis protein implicated in cell wall biosynthesis.";
Plant Physiol. 116:1339-1350(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
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.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=24905498; DOI=10.1111/tpj.12577;
Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
Smith-Moritz A.M., Plahar H., Chiu T.-Y.,
Gonzalez Fernandez-Nino S.M.G., Ebert B., Yang F., Christiansen K.M.,
Hansen S.F., Stonebloom S., Adams P.D., Ronald P.C., Hillson N.J.,
Hadi M.Z., Vega-Sanchez M.E., Loque D., Scheller H.V.,
Heazlewood J.L.;
"The plant glycosyltransferase clone collection for functional
genomics.";
Plant J. 79:517-529(2014).
[6]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
DISRUPTION PHENOTYPE.
PubMed=17071651; DOI=10.1104/pp.106.086363;
Drakakaki G., Zabotina O., Delgado I., Robert S., Keegstra K.,
Raikhel N.;
"Arabidopsis reversibly glycosylated polypeptides 1 and 2 are
essential for pollen development.";
Plant Physiol. 142:1480-1492(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[8]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION
PHENOTYPE.
PubMed=21478444; DOI=10.1105/tpc.111.083931;
Rautengarten C., Ebert B., Herter T., Petzold C.J., Ishii T.,
Mukhopadhyay A., Usadel B., Scheller H.V.;
"The interconversion of UDP-L-arabinopyranose and UDP-L-
arabinofuranose is indispensable for plant development in
Arabidopsis.";
Plant Cell 23:1373-1390(2011).
-!- 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) (PubMed:21478444). 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 (PubMed:17071651). {ECO:0000269|PubMed:17071651,
ECO:0000269|PubMed:21478444}.
-!- CATALYTIC ACTIVITY: UDP-beta-L-arabinofuranose = UDP-beta-L-
arabinopyranose. {ECO:0000269|PubMed:21478444}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q8H8T0};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q8H8T0};
-!- SUBUNIT: Heteromers with RGP2, RGP3, RGP4 and RGP5.
{ECO:0000269|PubMed:17071651}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus.
Note=Soluble and associated with peripheral membrane and
endomembrane system. {ECO:0000269|PubMed:17071651,
ECO:0000269|PubMed:21478444}.
-!- TISSUE SPECIFICITY: Predominantly expressed in shoot and root
apical meristems. Expressed in epidermal cells of leaves,
inflorescence stems and seed coat. Expressed in pollen.
{ECO:0000269|PubMed:17071651, ECO:0000269|PubMed:21478444,
ECO:0000269|PubMed:9536051}.
-!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
{ECO:0000250|UniProtKB:Q8H8T0}.
-!- PTM: Reversibly glycosylated in vitro by UDP-glucose, UDP-xylose
and UDP-galactose, but not UDP-mannose.
{ECO:0000269|PubMed:9536051}.
-!- DISRUPTION PHENOTYPE: 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). {ECO:0000269|PubMed:17071651,
ECO:0000269|PubMed:21478444}.
-!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF013627; AAC50000.1; -; mRNA.
EMBL; AC009755; AAF02115.1; -; Genomic_DNA.
EMBL; CP002686; AEE73781.1; -; Genomic_DNA.
EMBL; BT002409; AAO00769.1; -; mRNA.
EMBL; BT008841; AAP68280.1; -; mRNA.
EMBL; KJ138846; AHL38786.1; -; mRNA.
RefSeq; NP_186872.1; NM_111090.4.
UniGene; At.24058; -.
SMR; Q9SRT9; -.
BioGrid; 6566; 3.
IntAct; Q9SRT9; 1.
STRING; 3702.AT3G02230.1; -.
CAZy; GT75; Glycosyltransferase Family 75.
iPTMnet; Q9SRT9; -.
PaxDb; Q9SRT9; -.
PRIDE; Q9SRT9; -.
ProMEX; Q9SRT9; -.
EnsemblPlants; AT3G02230.1; AT3G02230.1; AT3G02230.
GeneID; 821233; -.
Gramene; AT3G02230.1; AT3G02230.1; AT3G02230.
KEGG; ath:AT3G02230; -.
Araport; AT3G02230; -.
TAIR; locus:2076482; AT3G02230.
eggNOG; ENOG410IHTP; Eukaryota.
eggNOG; ENOG411144T; LUCA.
HOGENOM; HOG000234443; -.
InParanoid; Q9SRT9; -.
KO; K13379; -.
OMA; HERNTRF; -.
OrthoDB; EOG09360C9G; -.
PhylomeDB; Q9SRT9; -.
BioCyc; ARA:AT3G02230-MONOMER; -.
BioCyc; MetaCyc:AT3G02230-MONOMER; -.
PRO; PR:Q9SRT9; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9SRT9; baseline and differential.
Genevisible; Q9SRT9; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005795; C:Golgi stack; IDA:TAIR.
GO; GO:0000138; C:Golgi trans cisterna; IDA:TAIR.
GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; ISS:TAIR.
GO; GO:0016866; F:intramolecular transferase activity; IDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
GO; GO:0052691; F:UDP-arabinopyranose mutase activity; IDA:TAIR.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
GO; GO:0009832; P:plant-type cell wall biogenesis; TAS:TAIR.
GO; GO:0071669; P:plant-type cell wall organization or biogenesis; IMP:UniProtKB.
GO; GO:0009555; P:pollen development; IGI:UniProtKB.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0033356; P:UDP-L-arabinose metabolic process; IMP:TAIR.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR004901; RGP.
InterPro; IPR037595; RGP_fam.
PANTHER; PTHR31682; PTHR31682; 1.
Pfam; PF03214; RGP; 1.
PIRSF; PIRSF016429; UPTG; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
Acetylation; Cell wall biogenesis/degradation; Complete proteome;
Cytoplasm; Glycoprotein; Golgi apparatus; Isomerase;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9LFW1}.
CHAIN 2 357 UDP-arabinopyranose mutase 1.
/FTId=PRO_0000410984.
MOTIF 110 112 DXD motif.
{ECO:0000250|UniProtKB:Q8H8T0}.
SITE 158 158 Required for activity.
{ECO:0000250|UniProtKB:Q8H8T0}.
SITE 165 165 Required for activity.
{ECO:0000250|UniProtKB:Q8H8T0}.
MOD_RES 2 2 N-acetylvaline.
{ECO:0000250|UniProtKB:Q9LFW1}.
CARBOHYD 158 158 N-linked (Glc...) arginine.
{ECO:0000250|UniProtKB:P80607}.
CONFLICT 42 42 L -> F (in Ref. 1; AAC50000).
{ECO:0000305}.
CONFLICT 221 221 F -> Y (in Ref. 1; AAC50000).
{ECO:0000305}.
CONFLICT 303 303 A -> P (in Ref. 1; AAC50000).
{ECO:0000305}.
SEQUENCE 357 AA; 40629 MW; 363BA6049415C465 CRC64;
MVEPANTVGI PVNHIPLLKD ELDIVIPTIR NLDFLEMWRP FLQPYHLIIV QDGDPSKTIA
VPEGFDYELY NRNDINRILG PKASCISFKD SACRCFGYMV SKKKYIFTID DDCFVAKDPS
GKAVNALEQH IKNLLCPSTP FFFNTLYDPY REGADFVRGY PFSLREGVST AVSHGLWLNI
PDYDAPTQLV KPKERNTRYV DAVMTIPKGT LFPMCGMNLA FDRELIGPAM YFGLMGDGQP
IGRYDDMWAG WCIKVICDHL GLGVKTGLPY IYHSKASNPF VNLKKEYKGI FWQEDIIPFF
QSAKLTKEAV TVQQCYMELS KLVKEKLSPI DPYFDKLADA MVTWIEAWDE LNPPTKA


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