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Probable UDP-arabinopyranose mutase 1 (EC 5.4.99.30) (Amylogenin) (Golgi-associated protein se-wap41) (Reversibly glycosylated polypeptide) (RGP) (UDP-L-arabinose mutase 1) (UDP-glucose:protein transglucosylase) (UPTG)

 RGP1_MAIZE              Reviewed;         364 AA.
P80607; Q9SAQ2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
09-SEP-2003, sequence version 2.
23-MAY-2018, entry version 96.
RecName: Full=Probable UDP-arabinopyranose mutase 1 {ECO:0000305};
EC=5.4.99.30 {ECO:0000250|UniProtKB:Q8H8T0};
AltName: Full=Amylogenin {ECO:0000303|PubMed:8521968};
AltName: Full=Golgi-associated protein se-wap41 {ECO:0000303|Ref.1};
AltName: Full=Reversibly glycosylated polypeptide {ECO:0000305};
Short=RGP {ECO:0000305};
AltName: Full=UDP-L-arabinose mutase 1 {ECO:0000305};
AltName: Full=UDP-glucose:protein transglucosylase {ECO:0000303|Ref.4};
Short=UPTG {ECO:0000303|Ref.4};
Name=UPTG {ECO:0000303|Ref.4};
Zea mays (Maize).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
Zea.
NCBI_TaxID=4577;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Jubile;
Katz A., Van Lent J.W.M., Kotlizky G., Yahalom A., Epel B.L.;
"Isolation of a maize 41 kDa Golgi associated protein.";
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 31-57; 133-193; 199-208; 244-254; 289-307 AND
337-359, AND GLYCOSYLATION AT ARG-158.
PubMed=8521968; DOI=10.1016/0014-5793(95)01247-6;
Singh D.G., Lomako J., Lomako W.M., Whelan W.J., Meyer H.E., Serwe M.,
Metzger J.W.;
"Beta-glucosylarginine: a new glucose-protein bond in a self-
glucosylating protein from sweet corn.";
FEBS Lett. 376:61-64(1995).
[3]
PROTEIN SEQUENCE OF 61-75.
TISSUE=Coleoptile;
AGRICOLA=IND20551642; DOI=10.1007/BF00224104;
Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C.,
Pernollet J.-C., Zivy M., de Vienne D.;
"The maize two dimensional gel protein database: towards an integrated
genome analysis program.";
Theor. Appl. Genet. 93:997-1005(1996).
[4]
FUNCTION.
Rothschild A., Tandecarz J.S.;
"UDP-glucose:protein transglucosylase in developing maize endosperm.";
Plant Sci. 97:119-127(1994).
[5]
SUBCELLULAR LOCATION.
Epel B.L., Van Lent J.W.M., Cohen L., Kotlizky G., Katz A.,
Yahalom A.;
"A 41kDa protein isolated from maize mesocotyl cell walls
immunolocalizes to plasmodesmata.";
Protoplasma 191:70-78(1996).
[6]
FUNCTION.
PubMed=8832094;
Rothschild A., Wald F.A., Bocca S.N., Tandecarz J.S.;
"Inhibition of UDP-glucose: protein transglucosylase by a maize
endosperm protein factor.";
Cell. Mol. Biol. 42:645-651(1996).
[7]
FUNCTION.
PubMed=9620435;
Wald F.A., Rothschild A., Moreno S., Tandecarz J.S.;
"Identification of a UPTG inhibitor protein from maize endosperm: high
homology with sucrose synthase protein.";
Cell. Mol. Biol. 44:397-406(1998).
-!- FUNCTION: Probable UDP-L-arabinose mutase involved in the
biosynthesis of cell wall non-cellulosic polysaccharides (By
similarity). Was initially shown to possess an autoglycosylating
activity which is dependent on the presence of UDP-glucose and
manganese (Ref.4, PubMed:8832094, PubMed:9620435).
{ECO:0000250|UniProtKB:Q8H8T0, ECO:0000269|PubMed:8832094,
ECO:0000269|PubMed:9620435, ECO:0000269|Ref.4}.
-!- CATALYTIC ACTIVITY: UDP-beta-L-arabinofuranose = UDP-beta-L-
arabinopyranose. {ECO:0000250|UniProtKB:Q8H8T0}.
-!- 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: Homopentamer or homohexamer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|Ref.5}.
Cell junction, plasmodesma {ECO:0000269|Ref.5}. Golgi apparatus
{ECO:0000269|Ref.5}. Note=Cell wall-associated, with highest
concentrations on plasmodesmata. Also located in the Golgi
apparatus. {ECO:0000269|Ref.5}.
-!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
{ECO:0000250|UniProtKB:Q8H8T0}.
-!- PTM: Reversibly glycosylated by UDP-glucose, UDP-xylose and UDP-
galactose. {ECO:0000250|UniProtKB:Q8H8T0}.
-!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
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EMBL; U89897; AAB49896.1; -; mRNA.
PIR; T04331; T04331.
RefSeq; NP_001105598.1; NM_001112128.1.
UniGene; Zm.752; -.
SMR; P80607; -.
STRING; 4577.GRMZM2G073725_P01; -.
CAZy; GT75; Glycosyltransferase Family 75.
PaxDb; P80607; -.
PRIDE; P80607; -.
ProMEX; P80607; -.
GeneID; 542592; -.
KEGG; zma:542592; -.
MaizeGDB; 131466; -.
eggNOG; ENOG410IHTP; Eukaryota.
eggNOG; ENOG411144T; LUCA.
HOGENOM; HOG000234443; -.
KO; K13379; -.
Proteomes; UP000007305; Unplaced.
ExpressionAtlas; P80607; differential.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-SubCell.
GO; GO:0052691; F:UDP-arabinopyranose mutase activity; IEA:UniProtKB-EC.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0071669; P:plant-type cell wall organization or biogenesis; IEA:InterPro.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR004901; RGP.
InterPro; IPR037595; RGP_fam.
PANTHER; PTHR31682; PTHR31682; 1.
Pfam; PF03214; RGP; 1.
PIRSF; PIRSF016429; UPTG; 1.
SUPFAM; SSF53448; SSF53448; 2.
1: Evidence at protein level;
Cell junction; Cell wall; Cell wall biogenesis/degradation;
Cellulose biosynthesis; Complete proteome; Direct protein sequencing;
Glycoprotein; Golgi apparatus; Isomerase; Reference proteome;
Secreted.
CHAIN 1 364 Probable UDP-arabinopyranose mutase 1.
/FTId=PRO_0000221193.
MOTIF 110 112 DXD motif.
{ECO:0000250|UniProtKB:Q8H8T0}.
SITE 158 158 Required for activity.
{ECO:0000250|UniProtKB:Q8H8T0}.
SITE 165 165 Required for activity.
{ECO:0000250|UniProtKB:Q8H8T0}.
CARBOHYD 158 158 N-linked (Glc...) arginine.
{ECO:0000269|PubMed:8521968}.
CONFLICT 40 40 A -> P (in Ref. 2; AA sequence).
{ECO:0000305}.
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


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