RGP5_ARATH
ID RGP5_ARATH Reviewed; 348 AA.
AC Q9FFD2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable UDP-arabinopyranose mutase 5 {ECO:0000305};
DE EC=5.4.99.30 {ECO:0000250|UniProtKB:Q9SRT9};
DE AltName: Full=Reversibly glycosylated polypeptide 5 {ECO:0000303|PubMed:21478444};
DE Short=AtRGP5 {ECO:0000303|PubMed:21478444};
DE AltName: Full=UDP-L-arabinose mutase 5 {ECO:0000305};
GN Name=RGP5 {ECO:0000303|PubMed:21478444};
GN OrderedLocusNames=At5g16510 {ECO:0000312|Araport:AT5G16510};
GN ORFNames=MQK4.26 {ECO:0000312|EMBL:BAB09620.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY
RP 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: Probable UDP-L-arabinose mutase involved in the biosynthesis
CC of cell wall non-cellulosic polysaccharides.
CC {ECO:0000250|UniProtKB:Q9SRT9}.
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:0000250|UniProtKB:Q9SRT9};
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 and RGP2. {ECO:0000269|PubMed:21478444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21478444}.
CC Golgi apparatus {ECO:0000269|PubMed:21478444}. Note=Localized
CC predominantly in the cytosol.
CC -!- TISSUE SPECIFICITY: Widely expressed at low levels.
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}.
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DR EMBL; AB005242; BAB09620.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92302.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92303.1; -; Genomic_DNA.
DR EMBL; AY091141; AAM14090.1; -; mRNA.
DR EMBL; AY114087; AAM45135.1; -; mRNA.
DR EMBL; AY088511; AAM66046.1; -; mRNA.
DR RefSeq; NP_197155.1; NM_121657.2.
DR RefSeq; NP_850831.1; NM_180500.3.
DR AlphaFoldDB; Q9FFD2; -.
DR BioGRID; 16789; 3.
DR IntAct; Q9FFD2; 1.
DR STRING; 3702.AT5G16510.2; -.
DR CAZy; GT75; Glycosyltransferase Family 75.
DR iPTMnet; Q9FFD2; -.
DR PaxDb; Q9FFD2; -.
DR PRIDE; Q9FFD2; -.
DR ProteomicsDB; 236969; -.
DR DNASU; 831513; -.
DR EnsemblPlants; AT5G16510.1; AT5G16510.1; AT5G16510.
DR EnsemblPlants; AT5G16510.2; AT5G16510.2; AT5G16510.
DR GeneID; 831513; -.
DR Gramene; AT5G16510.1; AT5G16510.1; AT5G16510.
DR Gramene; AT5G16510.2; AT5G16510.2; AT5G16510.
DR KEGG; ath:AT5G16510; -.
DR Araport; AT5G16510; -.
DR TAIR; locus:2171362; AT5G16510.
DR eggNOG; ENOG502QRG2; Eukaryota.
DR HOGENOM; CLU_061976_0_0_1; -.
DR InParanoid; Q9FFD2; -.
DR OMA; DVWNGLC; -.
DR OrthoDB; 662486at2759; -.
DR PhylomeDB; Q9FFD2; -.
DR BioCyc; ARA:AT5G16510-MON; -.
DR PRO; PR:Q9FFD2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFD2; baseline and differential.
DR Genevisible; Q9FFD2; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0016866; F:intramolecular transferase activity; IEA:InterPro.
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; IBA:GO_Central.
DR InterPro; IPR004901; RGP.
DR InterPro; IPR037595; RGP_fam.
DR PANTHER; PTHR31682; PTHR31682; 1.
DR Pfam; PF03214; RGP; 1.
DR PIRSF; PIRSF016429; UPTG; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Cytoplasm; Glycoprotein; Golgi apparatus;
KW Isomerase; Reference proteome.
FT CHAIN 1..348
FT /note="Probable UDP-arabinopyranose mutase 5"
FT /id="PRO_0000410988"
FT MOTIF 100..102
FT /note="DXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT SITE 148
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT SITE 155
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT CARBOHYD 148
FT /note="N-linked (Glc...) arginine"
FT /evidence="ECO:0000250|UniProtKB:P80607"
SQ SEQUENCE 348 AA; 38585 MW; C47FA7684890CB6E CRC64;
MSLAEINKNE VDIVIGALNA DLTQFLTSWR PFFSGFHLIV VKDPELKEEL NIPEGFDVDV
YSKTDMEKVV GASNSTMFSG YSCRYFGYLV SKKKYIVSID DDCVPAKDPK GFLVDAVTQH
VINLENPATP LFFNTLYDPY CEGADFVRGY PFSLRSGVPC AASCGLWLNL ADLDAPTQAL
KTEKRNTAYV DAVMTVPAKA MLPISGINIA FNRELVGPAL VPALRLAGEG KVRWETLEDV
WCGMCLKHIS DHLGYGVKTG LPYVWRNERG DAVESLRKKW EGMKLMEKSV PFFDSLKLPE
TALKVEDCVI ELAKAVKEQL GSDDPAFTQA ADAMVKWVQL WNSVNSSA
