RGP3_ARATH
ID RGP3_ARATH Reviewed; 362 AA.
AC O22666; Q8GWR6; Q9SR90;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=UDP-arabinopyranose mutase 3 {ECO:0000305};
DE EC=5.4.99.30 {ECO:0000269|PubMed:21478444};
DE AltName: Full=Reversibly glycosylated polypeptide 3 {ECO:0000303|PubMed:21478444};
DE Short=AtRGP3 {ECO:0000303|PubMed:21478444};
DE AltName: Full=UDP-L-arabinose mutase 3 {ECO:0000305};
GN Name=RGP3 {ECO:0000303|PubMed:21478444};
GN OrderedLocusNames=At3g08900 {ECO:0000312|Araport:AT3G08900};
GN ORFNames=T16O11.16 {ECO:0000312|EMBL:AAF07834.1};
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=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] OF 144-362.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 Preferentially catalyzes the formation of UDP-Arap from UDP-Araf. At
CC thermodynamic equilibrium in vitro the ratio of the pyranose form over
CC the furanose form is 95:5. Is not active on other UDP-sugars (UDP-Gal,
CC UDP-Xyl, UDP-Glc, GDP-Man and GDP-Fuc). Is probably active as heteromer
CC in vivo. {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: Heterodimer with RGP1. {ECO:0000269|PubMed:21478444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21478444}.
CC Golgi apparatus {ECO:0000269|PubMed:21478444}. Note=Soluble and
CC membrane-associated.
CC -!- TISSUE SPECIFICITY: Specifically expressed in developing seeds.
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 -!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF07834.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC43271.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF034255; AAC50002.2; -; mRNA.
DR EMBL; AC010871; AAF07834.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74693.1; -; Genomic_DNA.
DR EMBL; AK118676; BAC43271.1; ALT_INIT; mRNA.
DR RefSeq; NP_187502.2; NM_111724.3.
DR AlphaFoldDB; O22666; -.
DR BioGRID; 5373; 1.
DR STRING; 3702.AT3G08900.1; -.
DR CAZy; GT75; Glycosyltransferase Family 75.
DR PaxDb; O22666; -.
DR PRIDE; O22666; -.
DR ProteomicsDB; 236854; -.
DR EnsemblPlants; AT3G08900.1; AT3G08900.1; AT3G08900.
DR GeneID; 820039; -.
DR Gramene; AT3G08900.1; AT3G08900.1; AT3G08900.
DR KEGG; ath:AT3G08900; -.
DR Araport; AT3G08900; -.
DR TAIR; locus:2097653; AT3G08900.
DR eggNOG; ENOG502QSDP; Eukaryota.
DR HOGENOM; CLU_061976_0_0_1; -.
DR InParanoid; O22666; -.
DR OMA; TGMVTWI; -.
DR OrthoDB; 662486at2759; -.
DR PhylomeDB; O22666; -.
DR BioCyc; ARA:AT3G08900-MON; -.
DR BRENDA; 5.4.99.30; 399.
DR PRO; PR:O22666; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O22666; baseline and differential.
DR Genevisible; O22666; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0016866; F:intramolecular transferase activity; IDA:UniProtKB.
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:0033356; P:UDP-L-arabinose metabolic process; IDA: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 Cell wall biogenesis/degradation; Cytoplasm; Glycoprotein; Golgi apparatus;
KW Isomerase; Reference proteome.
FT CHAIN 1..362
FT /note="UDP-arabinopyranose mutase 3"
FT /id="PRO_0000410986"
FT MOTIF 106..108
FT /note="DXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT SITE 154
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT SITE 161
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT CARBOHYD 154
FT /note="N-linked (Glc...) arginine"
FT /evidence="ECO:0000250|UniProtKB:P80607"
SQ SEQUENCE 362 AA; 41282 MW; FCAF64DFA481F4B9 CRC64;
MAQLYSSVKP TPMLKDELDI VIPTIRNLDF LEMWRPFFEQ YHLIIVQDGD PSKVINIPVG
FDYELYNRND INRILGPKAS CISFKDSACR CFGYMVSKKK YIYTIDDDCF VAKDPTGKEI
NALEQHIKNL LSPSTPHFFN TLYDPYRDGA DFVRGYPFSM REGAITAVSH GLWLNIPDYD
APTQLVKPLE KNSRYVDAVM TIPKGTLFPM CGMNLAFDRE LIGPAMYFGL MGDGQPIGRY
DDMWAGWCVK VICDHMGWGV KTGLPYIWHS KASNPFVNLK KEYNGIFWQE EAIPFFQSVT
LPKECTSVQQ CYLELAKLVR EKLGKVDPYF ITLATGMVTW IEAWEELNSA EGTEAEAPKG
KN
