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Probable UDP-arabinopyranose mutase 5 (EC 5.4.99.30) (Reversibly glycosylated polypeptide 5) (AtRGP5) (UDP-L-arabinose mutase 5)

 RGP5_ARATH              Reviewed;         348 AA.
Q9FFD2;
27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
31-JAN-2018, entry version 103.
RecName: Full=Probable UDP-arabinopyranose mutase 5 {ECO:0000305};
EC=5.4.99.30 {ECO:0000250|UniProtKB:Q9SRT9};
AltName: Full=Reversibly glycosylated polypeptide 5 {ECO:0000303|PubMed:21478444};
Short=AtRGP5 {ECO:0000303|PubMed:21478444};
AltName: Full=UDP-L-arabinose mutase 5 {ECO:0000305};
Name=RGP5 {ECO:0000303|PubMed:21478444};
OrderedLocusNames=At5g16510 {ECO:0000312|Araport:AT5G16510};
ORFNames=MQK4.26 {ECO:0000312|EMBL:BAB09620.1};
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9330910; DOI=10.1093/dnares/4.3.215;
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
features of the 1.6 Mb regions covered by twenty physically assigned
P1 clones.";
DNA Res. 4:215-230(1997).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION
BY MASS SPECTROMETRY.
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: Probable UDP-L-arabinose mutase involved in the
biosynthesis of cell wall non-cellulosic polysaccharides.
{ECO:0000250|UniProtKB:Q9SRT9}.
-!- CATALYTIC ACTIVITY: UDP-beta-L-arabinofuranose = UDP-beta-L-
arabinopyranose. {ECO:0000250|UniProtKB:Q9SRT9}.
-!- 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 RGP1 and RGP2.
{ECO:0000269|PubMed:21478444}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:21478444}. Golgi apparatus
{ECO:0000269|PubMed:21478444}. Note=Localized predominantly in the
cytosol.
-!- TISSUE SPECIFICITY: Widely expressed at low levels.
{ECO:0000269|PubMed:21478444}.
-!- 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:0000250|UniProtKB:Q9SRT9}.
-!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
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EMBL; AB005242; BAB09620.1; -; Genomic_DNA.
EMBL; CP002688; AED92302.1; -; Genomic_DNA.
EMBL; CP002688; AED92303.1; -; Genomic_DNA.
EMBL; AY091141; AAM14090.1; -; mRNA.
EMBL; AY114087; AAM45135.1; -; mRNA.
EMBL; AY088511; AAM66046.1; -; mRNA.
RefSeq; NP_197155.1; NM_121657.2.
RefSeq; NP_850831.1; NM_180500.3.
UniGene; At.6462; -.
BioGrid; 16789; 1.
IntAct; Q9FFD2; 1.
STRING; 3702.AT5G16510.1; -.
CAZy; GT75; Glycosyltransferase Family 75.
iPTMnet; Q9FFD2; -.
PaxDb; Q9FFD2; -.
PRIDE; Q9FFD2; -.
DNASU; 831513; -.
EnsemblPlants; AT5G16510.1; AT5G16510.1; AT5G16510.
EnsemblPlants; AT5G16510.2; AT5G16510.2; AT5G16510.
GeneID; 831513; -.
Gramene; AT5G16510.1; AT5G16510.1; AT5G16510.
Gramene; AT5G16510.2; AT5G16510.2; AT5G16510.
KEGG; ath:AT5G16510; -.
Araport; AT5G16510; -.
TAIR; locus:2171362; AT5G16510.
eggNOG; ENOG410IHBF; Eukaryota.
eggNOG; ENOG410YC4P; LUCA.
HOGENOM; HOG000234443; -.
InParanoid; Q9FFD2; -.
KO; K13379; -.
OMA; DVWNGLC; -.
OrthoDB; EOG09360DFB; -.
PhylomeDB; Q9FFD2; -.
BioCyc; ARA:AT5G16510-MONOMER; -.
PRO; PR:Q9FFD2; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FFD2; baseline and differential.
Genevisible; Q9FFD2; AT.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0016866; F:intramolecular transferase activity; IEA:InterPro.
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; IBA:GO_Central.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0033356; P:UDP-L-arabinose metabolic process; IBA:GO_Central.
InterPro; IPR004901; RGP.
InterPro; IPR037595; RGP_fam.
PANTHER; PTHR31682; PTHR31682; 1.
Pfam; PF03214; RGP; 1.
PIRSF; PIRSF016429; UPTG; 1.
1: Evidence at protein level;
Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
Glycoprotein; Golgi apparatus; Isomerase; Reference proteome.
CHAIN 1 348 Probable UDP-arabinopyranose mutase 5.
/FTId=PRO_0000410988.
MOTIF 100 102 DXD motif.
{ECO:0000250|UniProtKB:Q8H8T0}.
SITE 148 148 Required for activity.
{ECO:0000250|UniProtKB:Q8H8T0}.
SITE 155 155 Required for activity.
{ECO:0000250|UniProtKB:Q8H8T0}.
CARBOHYD 148 148 N-linked (Glc...) arginine.
{ECO:0000250|UniProtKB:P80607}.
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


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