RGP1_SOLTU
ID RGP1_SOLTU Reviewed; 365 AA.
AC Q9SC19;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Probable UDP-arabinopyranose mutase 1 {ECO:0000305};
DE EC=5.4.99.30 {ECO:0000250|UniProtKB:Q8H8T0};
DE AltName: Full=Reversibly glycosylated polypeptide 1 {ECO:0000303|PubMed:10580281};
DE Short=RGP1 {ECO:0000303|PubMed:10580281};
DE AltName: Full=UDP-L-arabinose mutase 1 {ECO:0000305};
DE AltName: Full=UDP-glucose:protein transglucosylase 1 {ECO:0000303|PubMed:10580281};
DE Short=UPTG 1 {ECO:0000303|PubMed:10580281};
GN Name=UPTG1 {ECO:0000303|PubMed:10580281};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000312|EMBL:CAB64206.2};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 95-109, FUNCTION,
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Stolon tip {ECO:0000269|PubMed:10580281};
RX PubMed=10580281; DOI=10.1016/s0981-9428(99)00117-5;
RA Bocca S.N., Kissen R., Rojas-Beltran J.A., Noel F., Gebhardt C., Moreno S.,
RA du Jardin P., Tandecarz J.S.;
RT "Molecular cloning and characterization of the enzyme UDP-glucose:protein
RT transglucosylase from potato.";
RL Plant Physiol. Biochem. 37:809-819(1999).
RN [2]
RP FUNCTION.
RX PubMed=2941300; DOI=10.1111/j.1432-1033.1986.tb09700.x;
RA Moreno S., Cardini C.E., Tandecarz J.S.;
RT "Alpha-glucan synthesis on a protein primer, uridine diphosphoglucose:
RT protein transglucosylase I. Separation from starch synthetase and
RT phosphorylase and a study of its properties.";
RL Eur. J. Biochem. 157:539-545(1986).
RN [3]
RP GLYCOSYLATION.
RX PubMed=16669042; DOI=10.1104/pp.99.4.1342;
RA Ardila F.J., Tandecarz J.S.;
RT "Potato tuber UDP-glucose:protein transglucosylase catalyzes its own
RT glucosylation.";
RL Plant Physiol. 99:1342-1347(1992).
RN [4]
RP GLYCOSYLATION, AND SUBUNIT.
RA Bocca S.N., Rothschild A., Tandecarz J.S.;
RT "Initiation of starch biosynthesis: purification and characterization of
RT UDP-glucose:protein transglucosylase from potato tubers.";
RL Plant Physiol. Biochem. 35:205-212(1997).
CC -!- FUNCTION: Probable UDP-L-arabinose mutase involved in the biosynthesis
CC of cell wall non-cellulosic polysaccharides (By similarity). Was
CC initially shown to possess an autoglycosylating activity which is
CC dependent on the presence of UDP-glucose and manganese (Probable)
CC (PubMed:10580281). {ECO:0000250|UniProtKB:Q8H8T0,
CC ECO:0000269|PubMed:10580281, ECO:0000305|PubMed:2941300}.
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:Q8H8T0};
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: Homopentamer or homohexamer. {ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:P80607}. Cell junction, plasmodesma
CC {ECO:0000250|UniProtKB:P80607}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P80607}. Note=Cell wall-associated, with highest
CC concentrations on plasmodesmata. Also located in the Golgi apparatus
CC (By similarity). {ECO:0000250|UniProtKB:P80607}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including root,
CC tuber, leaf, petiole, shoot, stolon and stem.
CC {ECO:0000269|PubMed:10580281}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:Q8H8T0}.
CC -!- PTM: Reversibly glycosylated by UDP-glucose, UDP-xylose and UDP-
CC galactose, but not UDP-mannose. {ECO:0000269|PubMed:10580281,
CC ECO:0000269|PubMed:16669042, ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
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DR EMBL; AJ223252; CAB64206.2; -; mRNA.
DR AlphaFoldDB; Q9SC19; -.
DR STRING; 4113.PGSC0003DMT400072896; -.
DR CAZy; GT75; Glycosyltransferase Family 75.
DR eggNOG; ENOG502QSDP; Eukaryota.
DR InParanoid; Q9SC19; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q9SC19; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0052691; F:UDP-arabinopyranose mutase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
DR GO; GO:0033356; P:UDP-L-arabinose metabolic process; IBA:GO_Central.
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 junction; Cell wall; Cell wall biogenesis/degradation;
KW Cellulose biosynthesis; Direct protein sequencing; Glycoprotein;
KW Golgi apparatus; Isomerase; Reference proteome; Secreted.
FT CHAIN 1..365
FT /note="Probable UDP-arabinopyranose mutase 1"
FT /id="PRO_0000221195"
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 365 AA; 41805 MW; B71C6E94D4D1827C CRC64;
MAAATPLLKD ELDIVIPTIR NLDFLEMWRP FFQPYHLIIV QDGDPSKIIK VPEGFDYELY
NRNDINRILG PKASCISFKD SACRCFGYMV SKKKYIYTID DDCFVAKDPS GKDINALEQH
IKNLLCPSTP HFFNTLYDPY RDGADFVRGY PFSMREGAPT AVSHGLWLNI PDYDAPTQLV
KPHERNTRYV DAVMTIPKGT LFPMCGMNLA FDRDLIGPAM YFGLMGDGQP IGRYDDMWAG
WCTKVICDHL GLGIKTGLPY IWHSKASNPF VNLKKEYNGI FWQEEIIPFF QAATLPKECT
TVQQCYLELS KQVKKKLSSI DPYFTKLGEA MVTWIEAWDE LNLLGTTWLS CLSPMVQQRL
KSRCY
