RGP1_MAIZE
ID RGP1_MAIZE Reviewed; 364 AA.
AC P80607; Q9SAQ2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-SEP-2003, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Probable UDP-arabinopyranose mutase 1 {ECO:0000305};
DE EC=5.4.99.30 {ECO:0000250|UniProtKB:Q8H8T0};
DE AltName: Full=Amylogenin {ECO:0000303|PubMed:8521968};
DE AltName: Full=Golgi-associated protein se-wap41 {ECO:0000303|Ref.1};
DE AltName: Full=Reversibly glycosylated polypeptide {ECO:0000305};
DE Short=RGP {ECO:0000305};
DE AltName: Full=UDP-L-arabinose mutase 1 {ECO:0000305};
DE AltName: Full=UDP-glucose:protein transglucosylase {ECO:0000303|Ref.4};
DE Short=UPTG {ECO:0000303|Ref.4};
GN Name=UPTG {ECO:0000303|Ref.4};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Jubile;
RA Katz A., Van Lent J.W.M., Kotlizky G., Yahalom A., Epel B.L.;
RT "Isolation of a maize 41 kDa Golgi associated protein.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 31-57; 133-193; 199-208; 244-254; 289-307 AND 337-359,
RP AND GLYCOSYLATION AT ARG-158.
RX PubMed=8521968; DOI=10.1016/0014-5793(95)01247-6;
RA Singh D.G., Lomako J., Lomako W.M., Whelan W.J., Meyer H.E., Serwe M.,
RA Metzger J.W.;
RT "Beta-glucosylarginine: a new glucose-protein bond in a self-glucosylating
RT protein from sweet corn.";
RL FEBS Lett. 376:61-64(1995).
RN [3]
RP PROTEIN SEQUENCE OF 61-75.
RC TISSUE=Coleoptile;
RX AGRICOLA=IND20551642; DOI=10.1007/BF00224104;
RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., Pernollet J.-C.,
RA Zivy M., de Vienne D.;
RT "The maize two dimensional gel protein database: towards an integrated
RT genome analysis program.";
RL Theor. Appl. Genet. 93:997-1005(1996).
RN [4]
RP FUNCTION.
RA Rothschild A., Tandecarz J.S.;
RT "UDP-glucose:protein transglucosylase in developing maize endosperm.";
RL Plant Sci. 97:119-127(1994).
RN [5]
RP SUBCELLULAR LOCATION.
RA Epel B.L., Van Lent J.W.M., Cohen L., Kotlizky G., Katz A., Yahalom A.;
RT "A 41kDa protein isolated from maize mesocotyl cell walls immunolocalizes
RT to plasmodesmata.";
RL Protoplasma 191:70-78(1996).
RN [6]
RP FUNCTION.
RX PubMed=8832094;
RA Rothschild A., Wald F.A., Bocca S.N., Tandecarz J.S.;
RT "Inhibition of UDP-glucose: protein transglucosylase by a maize endosperm
RT protein factor.";
RL Cell. Mol. Biol. 42:645-651(1996).
RN [7]
RP FUNCTION.
RX PubMed=9620435;
RA Wald F.A., Rothschild A., Moreno S., Tandecarz J.S.;
RT "Identification of a UPTG inhibitor protein from maize endosperm: high
RT homology with sucrose synthase protein.";
RL Cell. Mol. Biol. 44:397-406(1998).
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 (Ref.4,
CC PubMed:8832094, PubMed:9620435). {ECO:0000250|UniProtKB:Q8H8T0,
CC ECO:0000269|PubMed:8832094, ECO:0000269|PubMed:9620435,
CC ECO:0000269|Ref.4}.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|Ref.5}. Cell
CC junction, plasmodesma {ECO:0000269|Ref.5}. Golgi apparatus
CC {ECO:0000269|Ref.5}. Note=Cell wall-associated, with highest
CC concentrations on plasmodesmata. Also located in the Golgi apparatus.
CC {ECO:0000269|Ref.5}.
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. {ECO:0000250|UniProtKB:Q8H8T0}.
CC -!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
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DR EMBL; U89897; AAB49896.1; -; mRNA.
DR PIR; T04331; T04331.
DR RefSeq; NP_001105598.1; NM_001112128.1.
DR AlphaFoldDB; P80607; -.
DR STRING; 4577.GRMZM2G073725_P01; -.
DR CAZy; GT75; Glycosyltransferase Family 75.
DR PaxDb; P80607; -.
DR PRIDE; P80607; -.
DR ProMEX; P80607; -.
DR GeneID; 542592; -.
DR KEGG; zma:542592; -.
DR MaizeGDB; 131466; -.
DR eggNOG; ENOG502QSDP; Eukaryota.
DR OrthoDB; 662486at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P80607; baseline and differential.
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: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..364
FT /note="Probable UDP-arabinopyranose mutase 1"
FT /id="PRO_0000221193"
FT MOTIF 110..112
FT /note="DXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT SITE 158
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT SITE 165
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT CARBOHYD 158
FT /note="N-linked (Glc...) arginine"
FT /evidence="ECO:0000269|PubMed:8521968"
FT CONFLICT 40
FT /note="A -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 41204 MW; 00CEC4FD30378D0C CRC64;
MAGTVTVPGS STPSTPLLKD ELDIVIPTIR NLDFLEMWRA FFQPYHLIIV QDGDPTKTIK
VPEGFDYELY NRNDINRILG PKASCISFKD SACRCFGYMV SKKKYIYTID DDCFVAKDPS
GKDINALEQH IKNLLSPSTP FFFNTLYDPY REGADFVRGY PFSLREGAHT AVSHGLWLNI
PDYDAPTQLV KPKERNERYV DAVMTIPKGT LFPMCGMNLA FDRDLIGPAM YFGLMGDGQP
IGRYDDMWAG WCVKVICDHL SLGVKTGLPY IWHSKASNPF VNLKKEYKGI FWQEDIIPFF
QNVTIPKDCD TVQKCYIYLS GQVKEKLGTI DPYFVKLGDA MVTWIEAWDE LNPSTPAAAN
GKAK
