RGP1_ARATH
ID RGP1_ARATH Reviewed; 357 AA.
AC Q9SRT9; O22427; W8PVH6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=UDP-arabinopyranose mutase 1 {ECO:0000305};
DE EC=5.4.99.30 {ECO:0000269|PubMed:21478444};
DE AltName: Full=Reversibly glycosylated polypeptide 1 {ECO:0000303|PubMed:21478444};
DE Short=AtRGP1 {ECO:0000303|PubMed:21478444};
DE AltName: Full=UDP-L-arabinose mutase 1 {ECO:0000305};
GN Name=RGP1 {ECO:0000303|PubMed:21478444};
GN OrderedLocusNames=At3g02230 {ECO:0000312|Araport:AT3G02230};
GN ORFNames=F14P3.12 {ECO:0000312|EMBL:AAF02115.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=9536051; DOI=10.1104/pp.116.4.1339;
RA Delgado I.J., Wang Z., de Rocher A., Keegstra K., Raikhel N.V.;
RT "Cloning and characterization of AtRGP1. A reversibly autoglycosylated
RT arabidopsis protein implicated in cell wall biosynthesis.";
RL Plant Physiol. 116:1339-1350(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17071651; DOI=10.1104/pp.106.086363;
RA Drakakaki G., Zabotina O., Delgado I., Robert S., Keegstra K., Raikhel N.;
RT "Arabidopsis reversibly glycosylated polypeptides 1 and 2 are essential for
RT pollen development.";
RL Plant Physiol. 142:1480-1492(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RX PubMed=21478444; DOI=10.1105/tpc.111.083931;
RA Rautengarten C., Ebert B., Herter T., Petzold C.J., Ishii T.,
RA Mukhopadhyay A., Usadel B., Scheller H.V.;
RT "The interconversion of UDP-L-arabinopyranose and UDP-L-arabinofuranose is
RT indispensable for plant development in Arabidopsis.";
RL Plant Cell 23:1373-1390(2011).
CC -!- FUNCTION: UDP-L-arabinose mutase involved in the biosynthesis of cell
CC wall non-cellulosic polysaccharides. Catalyzes the interconvertion of
CC UDP-L-arabinopyranose (UDP-Arap) and UDP-L-arabinofuranose (UDP-Araf)
CC in vitro. Preferentially catalyzes the formation of UDP-Arap from UDP-
CC Araf. At thermodynamic equilibrium in vitro the ratio of the pyranose
CC form over the furanose form is 95:5. Is not active on other UDP-sugars
CC (UDP-Gal, UDP-Xyl, UDP-Glc, GDP-Man and GDP-Fuc) (PubMed:21478444).
CC Functions redundantly with RGP2 and is essential for proper cell walls
CC and pollen development. Probably involved in the formation of the
CC pectocellulosic cell wall layer intine. Is probably active as heteromer
CC in vivo (PubMed:17071651). {ECO:0000269|PubMed:17071651,
CC ECO:0000269|PubMed:21478444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose;
CC Xref=Rhea:RHEA:28350, ChEBI:CHEBI:61457, ChEBI:CHEBI:61463;
CC EC=5.4.99.30; Evidence={ECO:0000269|PubMed:21478444};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8H8T0};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8H8T0};
CC -!- SUBUNIT: Heteromers with RGP2, RGP3, RGP4 and RGP5.
CC {ECO:0000269|PubMed:17071651}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus. Note=Soluble
CC and associated with peripheral membrane and endomembrane system.
CC {ECO:0000269|PubMed:17071651, ECO:0000269|PubMed:21478444}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in shoot and root apical
CC meristems. Expressed in epidermal cells of leaves, inflorescence stems
CC and seed coat. Expressed in pollen. {ECO:0000269|PubMed:17071651,
CC ECO:0000269|PubMed:21478444, ECO:0000269|PubMed:9536051}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:Q8H8T0}.
CC -!- PTM: Reversibly glycosylated in vitro by UDP-glucose, UDP-xylose and
CC UDP-galactose, but not UDP-mannose. {ECO:0000269|PubMed:9536051}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but significant reduction in total cell wall arabinose. Rgp1
CC and rgp2 double mutant is male gametophyte lethal, with an arrest in
CC pollen mitosis (PubMed:17071651). RNAi-mediated knockdown of both RGP1
CC and RGP2 causes severe developmental defects and strong reduction in
CC total cell wall arabinose (PubMed:21478444).
CC {ECO:0000269|PubMed:17071651, ECO:0000269|PubMed:21478444}.
CC -!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
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DR EMBL; AF013627; AAC50000.1; -; mRNA.
DR EMBL; AC009755; AAF02115.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73781.1; -; Genomic_DNA.
DR EMBL; BT002409; AAO00769.1; -; mRNA.
DR EMBL; BT008841; AAP68280.1; -; mRNA.
DR EMBL; KJ138846; AHL38786.1; -; mRNA.
DR RefSeq; NP_186872.1; NM_111090.4.
DR AlphaFoldDB; Q9SRT9; -.
DR BioGRID; 6566; 4.
DR IntAct; Q9SRT9; 2.
DR STRING; 3702.AT3G02230.1; -.
DR CAZy; GT75; Glycosyltransferase Family 75.
DR iPTMnet; Q9SRT9; -.
DR PaxDb; Q9SRT9; -.
DR PRIDE; Q9SRT9; -.
DR ProMEX; Q9SRT9; -.
DR ProteomicsDB; 236889; -.
DR EnsemblPlants; AT3G02230.1; AT3G02230.1; AT3G02230.
DR GeneID; 821233; -.
DR Gramene; AT3G02230.1; AT3G02230.1; AT3G02230.
DR KEGG; ath:AT3G02230; -.
DR Araport; AT3G02230; -.
DR TAIR; locus:2076482; AT3G02230.
DR eggNOG; ENOG502QSDP; Eukaryota.
DR HOGENOM; CLU_061976_0_0_1; -.
DR InParanoid; Q9SRT9; -.
DR OMA; WDELNNN; -.
DR OrthoDB; 662486at2759; -.
DR PhylomeDB; Q9SRT9; -.
DR BioCyc; ARA:AT3G02230-MON; -.
DR BioCyc; MetaCyc:AT3G02230-MON; -.
DR BRENDA; 5.4.99.30; 399.
DR PRO; PR:Q9SRT9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRT9; baseline and differential.
DR Genevisible; Q9SRT9; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IDA:TAIR.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; ISS:TAIR.
DR GO; GO:0016866; F:intramolecular transferase activity; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0052691; F:UDP-arabinopyranose mutase activity; IDA:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0071669; P:plant-type cell wall organization or biogenesis; IMP:UniProtKB.
DR GO; GO:0009555; P:pollen development; IGI:UniProtKB.
DR GO; GO:0033356; P:UDP-L-arabinose metabolic process; IMP:TAIR.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR004901; RGP.
DR InterPro; IPR037595; RGP_fam.
DR PANTHER; PTHR31682; PTHR31682; 1.
DR Pfam; PF03214; RGP; 1.
DR PIRSF; PIRSF016429; UPTG; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell wall biogenesis/degradation; Cytoplasm; Glycoprotein;
KW Golgi apparatus; Isomerase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9LFW1"
FT CHAIN 2..357
FT /note="UDP-arabinopyranose mutase 1"
FT /id="PRO_0000410984"
FT MOTIF 110..112
FT /note="DXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT SITE 158
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT SITE 165
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:Q9LFW1"
FT CARBOHYD 158
FT /note="N-linked (Glc...) arginine"
FT /evidence="ECO:0000250|UniProtKB:P80607"
FT CONFLICT 42
FT /note="L -> F (in Ref. 1; AAC50000)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="F -> Y (in Ref. 1; AAC50000)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="A -> P (in Ref. 1; AAC50000)"
FT /evidence="ECO:0000305"
SQ 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
