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   02-SEP-2026, entry version 100.
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   SMR; Q9SC19; -.
DR   FunCoup; Q9SC19; 1825.
DR   STRING; 4113.Q9SC19; -.
DR   GlyCosmos; Q9SC19; 1 site, No reported glycans.
DR   PaxDb; 4113-Q9SC19; -.
DR   eggNOG; ENOG502QSDP; Eukaryota.
DR   InParanoid; Q9SC19; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-SubCell.
DR   GO; GO:0052691; F:UDP-arabinopyranose mutase activity; ISS:UniProtKB.
DR   GO; GO:0009101; P:glycoprotein biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0071669; P:plant-type cell wall organization or biogenesis; IEA:InterPro.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR004901; RGP.
DR   InterPro; IPR037595; RGP_fam.
DR   PANTHER; PTHR31682:SF36; UDP-ARABINOPYRANOSE MUTASE 1-RELATED; 1.
DR   PANTHER; PTHR31682; UDP-ARABINOSE MUTASE; 1.
DR   Pfam; PF03214; RGP; 1.
DR   PIRSF; PIRSF016429; UPTG; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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
//