RGP2_ARATH
ID RGP2_ARATH Reviewed; 360 AA.
AC Q9LFW1; O22428; Q8LB19;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=UDP-arabinopyranose mutase 2 {ECO:0000305};
DE EC=5.4.99.30 {ECO:0000269|PubMed:21478444};
DE AltName: Full=Reversibly glycosylated polypeptide 2 {ECO:0000303|PubMed:21478444};
DE Short=AtRGP2 {ECO:0000303|PubMed:21478444};
DE AltName: Full=UDP-L-arabinose mutase 2 {ECO:0000305};
GN Name=RGP2 {ECO:0000303|PubMed:21478444};
GN OrderedLocusNames=At5g15650 {ECO:0000312|Araport:AT5G15650};
GN ORFNames=F14F8_30 {ECO:0000312|EMBL:CAC01764.1};
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].
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 RGP1, RGP4 and RGP5.
CC {ECO:0000269|PubMed:17071651}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus. Note=Soluble
CC and membrane-associated. {ECO:0000269|PubMed:17071651,
CC 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}.
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:0000250|UniProtKB:Q9SRT9}.
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; AF013628; AAC50001.1; -; mRNA.
DR EMBL; AL391144; CAC01764.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92188.1; -; Genomic_DNA.
DR EMBL; AY039846; AAK63950.1; -; mRNA.
DR EMBL; AY120691; AAM52234.1; -; mRNA.
DR EMBL; AY087476; AAM65020.1; -; mRNA.
DR PIR; T51394; T51394.
DR RefSeq; NP_197069.1; NM_121569.3.
DR AlphaFoldDB; Q9LFW1; -.
DR BioGRID; 16695; 4.
DR IntAct; Q9LFW1; 2.
DR STRING; 3702.AT5G15650.1; -.
DR CAZy; GT75; Glycosyltransferase Family 75.
DR iPTMnet; Q9LFW1; -.
DR PaxDb; Q9LFW1; -.
DR PRIDE; Q9LFW1; -.
DR ProMEX; Q9LFW1; -.
DR ProteomicsDB; 236245; -.
DR EnsemblPlants; AT5G15650.1; AT5G15650.1; AT5G15650.
DR GeneID; 831419; -.
DR Gramene; AT5G15650.1; AT5G15650.1; AT5G15650.
DR KEGG; ath:AT5G15650; -.
DR Araport; AT5G15650; -.
DR TAIR; locus:2143171; AT5G15650.
DR eggNOG; ENOG502QSDP; Eukaryota.
DR HOGENOM; CLU_061976_0_0_1; -.
DR InParanoid; Q9LFW1; -.
DR OMA; WIQAWDG; -.
DR OrthoDB; 662486at2759; -.
DR PhylomeDB; Q9LFW1; -.
DR BioCyc; ARA:AT5G15650-MON; -.
DR BRENDA; 5.4.99.30; 399.
DR PRO; PR:Q9LFW1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFW1; baseline and differential.
DR Genevisible; Q9LFW1; 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:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
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:0019567; P:arabinose biosynthetic process; IMP:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:TAIR.
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:0007744|PubMed:22223895"
FT CHAIN 2..360
FT /note="UDP-arabinopyranose mutase 2"
FT /id="PRO_0000410985"
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:0007744|PubMed:22223895"
FT CARBOHYD 158
FT /note="N-linked (Glc...) arginine"
FT /evidence="ECO:0000250|UniProtKB:P80607"
FT CONFLICT 9
FT /note="G -> R (in Ref. 5; AAM65020)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="W -> R (in Ref. 5; AAM65020)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="I -> N (in Ref. 1; AAC50001)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="G -> V (in Ref. 1; AAC50001)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="A -> SLRAV (in Ref. 1; AAC50001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 40890 MW; 8FE4D48C555F97F1 CRC64;
MVEPANTVGL PVNPTPLLKD ELDIVIPTIR NLDFLEMWRP FLQPYHLIIV QDGDPSKKIH
VPEGYDYELY NRNDINRILG PKASCISFKD SACRCFGYMV SKKKYIFTID DDCFVAKDPS
GKAVNALEQH IKNLLCPSSP FFFNTLYDPY REGADFVRGY PFSLREGVST AVSHGLWLNI
PDYDAPTQLV KPKERNTRYV DAVMTIPKGT LFPMCGMNLA FDRDLIGPAM YFGLMGDGQP
IGRYDDMWAG WCIKVICDHL SLGVKTGLPY IYHSKASNPF VNLKKEYKGI FWQEEIIPFF
QNAKLSKEAV TVQQCYIELS KMVKEKLSSL DPYFDKLADA MVTWIEAWDE LNPPAASGKA
